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  • Amino Acid Sequence  (181)
  • American Association for the Advancement of Science (AAAS)  (181)
  • American Meteorological Society
  • Nature Publishing Group
  • 1995-1999  (181)
  • 1940-1944
  • 1995  (181)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (181)
  • American Meteorological Society
  • Nature Publishing Group
Years
  • 1995-1999  (181)
  • 1940-1944
Year
  • 1
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    Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-28
    Description: DCoH, the dimerization cofactor of hepatocyte nuclear factor-1, stimulates gene expression by associating with specific DNA binding proteins and also catalyzes the dehydration of the biopterin cofactor of phenylalanine hydroxylase. The x-ray crystal structure determined at 3 angstrom resolution reveals that DCoH forms a tetramer containing two saddle-shaped grooves that comprise likely macromolecule binding sites. Two equivalent enzyme active sites flank each saddle, suggesting that there is a spatial connection between the catalytic and binding activities. Structural similarities between the DCoH fold and nucleic acid-binding proteins argue that the saddle motif has evolved to bind diverse ligands or that DCoH unexpectedly may bind nucleic acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Endrizzi, J A -- Cronk, J D -- Wang, W -- Crabtree, G R -- Alber, T -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):556-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720-3206, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725101" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Gene Expression Regulation ; Hydro-Lyases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; Transcription Factors/*chemistry/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Orphanin FQ: a neuropeptide that activates an opioidlike G protein-coupled receptor (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: A heptadecapeptide was identified and purified from porcine brain tissue as a ligand for an orphan heterotrimeric GTP-binding protein (G protein)-coupled receptor (LC132) that is similar in sequence to opioid receptors. This peptide, orphanin FQ, has a primary structure reminiscent of that of opioid peptides. Nanomolar concentrations of orphanin FQ inhibited forskolin-stimulated adenylyl cyclase activity in cells transfected with LC132. This inhibitory activity was not affected by the addition of opioid ligands, nor did the peptide activate opioid receptors. Orphanin FQ bound to its receptor in a saturable manner and with high affinity. When injected intracerebroventricularly into mice, orphanin FQ caused a decrease in locomotor activity but did not induce analgesia in the hot-plate test. However, the peptide produced hyperalgesia in the tail-flick assay. Thus, orphanin FQ may act as a transmitter in the brain by modulating nociceptive and locomotor behavior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reinscheid, R K -- Nothacker, H P -- Bourson, A -- Ardati, A -- Henningsen, R A -- Bunzow, J R -- Grandy, D K -- Langen, H -- Monsma, F J Jr -- Civelli, O -- DA 08562/DA/NIDA NIH HHS/ -- DA 09620/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):792-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pharma Division, Hoffmann-La Roche AG, Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481766" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclase Inhibitors ; Amino Acid Sequence ; Analgesics/pharmacology ; Animals ; CHO Cells ; Colforsin/pharmacology ; Cricetinae ; GTP-Binding Proteins/*metabolism ; Hypothalamus/chemistry ; Injections, Intraventricular ; Injections, Spinal ; Ligands ; Mice ; Molecular Sequence Data ; Motor Activity/drug effects ; Opioid Peptides/chemistry/*isolation & purification/*metabolism/pharmacology ; Pain Measurement ; Receptors, Neuropeptide/*metabolism ; Receptors, Opioid/*metabolism ; Swine ; Transfection
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  • 3
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    A neuropeptide gene defined by the Drosophila memory mutant amnesiac (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: Mutations in genes required for associative learning and memory in Drosophila exist, but isolation of the genes has been difficult because most are defined by a single, chemically induced allele. Here, a simplified genetic screen was used to identify candidate genes involved in learning and memory. Second site suppressors of the dunce (dnc) female sterility phenotype were isolated with the use of transposon mutagenesis. One suppressor mutation that was recovered mapped in the amnesiac (amn) gene. Cloning of the locus revealed that amn encodes a previously uncharacterized neuropeptide gene. Thus, with the cloning of amn, specific neuropeptides are implicated in the memory process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feany, M B -- Quinn, W G -- New York, N.Y. -- Science. 1995 May 12;268(5212):869-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754370" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Codon ; DNA Transposable Elements ; DNA, Complementary/genetics ; Drosophila/*genetics/physiology ; *Drosophila Proteins ; Female ; *Genes, Insect ; Growth Hormone-Releasing Hormone/chemistry/genetics ; Male ; Memory/*physiology ; Molecular Sequence Data ; Mutagenesis, Insertional ; Mutation ; Neuropeptides/chemistry/*genetics ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Sequence Homology, Amino Acid ; Suppression, Genetic
    Print ISSN: 0036-8075
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  • 4
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    Mutations in Fas associated with human lymphoproliferative syndrome and autoimmunity (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-02
    Description: Fas (also known as Apo1 and CD95) is a cell surface receptor involved in apoptotic cell death. Fas expression and function were analyzed in three children (including two siblings) with a lymphoproliferative syndrome, two of whom also had autoimmune disorders. A large deletion in the gene encoding Fas and no detectable cell surface expression characterized the most affected patient. Clinical manifestations in the two related patients were less severe: Fas-mediated apoptosis was impaired and a deletion within the intracytoplasmic domain was detected. These findings illustrate the crucial regulatory role of Fas and may provide a molecular basis for some autoimmune diseases in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rieux-Laucat, F -- Le Deist, F -- Hivroz, C -- Roberts, I A -- Debatin, K M -- Fischer, A -- de Villartay, J P -- New York, N.Y. -- Science. 1995 Jun 2;268(5215):1347-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut National de la Sante et de la Recherche Medicale (INSERM) U 429, Hopital Necker-Enfants Malades, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7539157" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD95 ; Antigens, Surface/chemistry/*genetics/physiology ; Apoptosis ; Autoimmune Diseases/*genetics/immunology/pathology ; Base Sequence ; Child ; Female ; *Frameshift Mutation ; Humans ; Infant ; Lymphoproliferative Disorders/*genetics/immunology/pathology ; Male ; Molecular Sequence Data ; Sequence Deletion ; Syndrome ; Thrombocytopenia/genetics/immunology/pathology
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  • 5
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    Aggressive behavior and altered amounts of brain serotonin and norepinephrine in mice lacking MAOA (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-23
    Description: Deficiency in monoamine oxidase A (MAOA), an enzyme that degrades serotonin and norepinephrine, has recently been shown to be associated with aggressive behavior in men of a Dutch family. A line of transgenic mice was isolated in which transgene integration caused a deletion in the gene encoding MAOA, providing an animal model of MAOA deficiency. In pup brains, serotonin concentrations were increased up to ninefold, and serotonin-like immunoreactivity was present in catecholaminergic neurons. In pup and adult brains, norepinephrine concentrations were increased up to twofold, and cytoarchitectural changes were observed in the somatosensory cortex. Pup behavioral alterations, including trembling, difficulty in righting, and fearfulness were reversed by the serotonin synthesis inhibitor parachlorophenylalanine. Adults manifested a distinct behavioral syndrome, including enhanced aggression in males.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844866/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2844866/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cases, O -- Seif, I -- Grimsby, J -- Gaspar, P -- Chen, K -- Pournin, S -- Muller, U -- Aguet, M -- Babinet, C -- Shih, J C -- K05 MH 00796/MH/NIMH NIH HHS/ -- R01 MH 37020/MH/NIMH NIH HHS/ -- R37 MH 39085/MH/NIMH NIH HHS/ -- R37 MH039085/MH/NIMH NIH HHS/ -- R37 MH039085-23/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1763-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre National de la Recherche Scientifique (CNRS), Unite de Recherche Associee (URA), Institut Curie, Orsay, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792602" target="_blank"〉PubMed〈/a〉
    Keywords: Aggression/*physiology ; Amino Acid Sequence ; Animals ; Base Sequence ; Blotting, Southern ; Brain/*metabolism ; Disease Models, Animal ; Dopamine/metabolism ; Female ; Interferon-beta/genetics ; Male ; Mice ; Mice, Inbred C3H ; Mice, Transgenic ; Molecular Sequence Data ; Monoamine Oxidase/*deficiency ; Norepinephrine/*metabolism ; Sequence Deletion ; Serotonin/*metabolism
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  • 6
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    Protein lipidation in cell signaling (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-14
    Description: The ability of cells to communicate with and respond to their external environment is critical for their continued existence. A universal feature of this communication is that the external signal must in some way penetrate the lipid bilayer surrounding the cell. In most cases of such signal acquisition, the signaling entity itself does not directly enter the cell but rather transmits its information to specific proteins present on the surface of the cell membrane. These proteins then communicate with additional proteins associated with the intracellular face of the membrane. Membrane localization and function of many of these proteins are dependent on their covalent modification by specific lipids, and it is the processes involved that form the focus of this article.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Casey, P J -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):221-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Cancer Biology, Duke University Medical Center, Durham, NC 27710-3686, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716512" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Animals ; Cell Membrane/*metabolism ; GTP-Binding Proteins/*metabolism ; Glycosylphosphatidylinositols/*metabolism ; *Lipid Metabolism ; Molecular Sequence Data ; Protein-Tyrosine Kinases/*metabolism ; *Signal Transduction
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  • 7
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    Peptide binding and presentation by mouse CD1 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-14
    Description: CD1 molecules are distantly related to the major histocompatibility complex (MHC) class I proteins. They are of unknown function. Screening random peptide phage display libraries with soluble empty mouse CD1 (mCD1) identified a peptide binding motif. It consists of three anchor positions occupied by aromatic or bulky hydrophobic amino acids. Equilibrium binding studies demonstrated that mCD1 binds peptides containing the appropriate motif with relatively high affinity. However, in contrast to classical MHC class I molecules, strong binding to mCD1 required relatively long peptides. Peptide-specific, mCD1-restricted T cell responses can be raised, which suggests that the findings are of immunological significance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castano, A R -- Tangri, S -- Miller, J E -- Holcombe, H R -- Jackson, M R -- Huse, W D -- Kronenberg, M -- Peterson, P A -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):223-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542403" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigen Presentation ; Antigens, CD/chemistry/*immunology/metabolism ; Antigens, CD1 ; Cell Line ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Peptides/chemistry/*immunology/metabolism ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection
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  • 8
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    Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-05
    Description: Lactacystin is a Streptomyces metabolite that inhibits cell cycle progression and induces neurite outgrowth in a murine neuroblastoma cell line. Tritium-labeled lactacystin was used to identify the 20S proteasome as its specific cellular target. Three distinct peptidase activities of this enzyme complex (trypsin-like, chymotrypsin-like, and peptidylglutamyl-peptide hydrolyzing activities) were inhibited by lactacystin, the first two irreversibly and all at different rates. None of five other proteases were inhibited, and the ability of lactacystin analogs to inhibit cell cycle progression and induce neurite outgrowth correlated with their ability to inhibit the proteasome. Lactacystin appears to modify covalently the highly conserved amino-terminal threonine of the mammalian proteasome subunit X (also called MB1), a close homolog of the LMP7 proteasome subunit encoded by the major histocompatibility complex. This threonine residue may therefore have a catalytic role, and subunit X/MB1 may be a core component of an amino-terminal-threonine protease activity of the proteasome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fenteany, G -- Standaert, R F -- Lane, W S -- Choi, S -- Corey, E J -- Schreiber, S L -- New York, N.Y. -- Science. 1995 May 5;268(5211):726-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7732382" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcysteine/*analogs & derivatives/pharmacology ; Amino Acid Sequence ; Animals ; Carrier Proteins/metabolism ; Cattle ; Chromatography, High Pressure Liquid ; Cysteine Endopeptidases/*drug effects/metabolism ; Cysteine Proteinase Inhibitors/*pharmacology ; Electrophoresis, Polyacrylamide Gel ; Mice ; Molecular Sequence Data ; Multienzyme Complexes/*drug effects/metabolism ; Nerve Tissue Proteins/metabolism ; Neurons/*drug effects ; Proteasome Endopeptidase Complex ; Threonine/*drug effects ; Tumor Cells, Cultured
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  • 9
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    A strategy for a convergent synthesis of N-linked glycopeptides on a solid support (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-14
    Description: Oligosaccharides and glycopeptides are of considerable importance in molecular biology and pharmacology. However, their synthesis is complicated by the large number of different linking sites between each saccharide unit, the need for stereochemical control, the chemical sensitivity of the glycopeptide bonds, and the need to harmonize diverse protecting groups. Here, an efficient solid-phase synthesis of three N-linked glycopeptides based on glycal assembly is presented. The peptide domain can be extended while the ensemble remains bound to the polymer. The glycopeptides synthesized here are among the largest N-linked glycopeptides ever accessed by either solution- or solid-phase synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roberge, J Y -- Beebe, X -- Danishefsky, S J -- AI 16943/AI/NIAID NIH HHS/ -- T32 CA62948/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):202-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618080" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Carbohydrate Conformation ; Carbohydrate Sequence ; Glycopeptides/*chemical synthesis/chemistry/isolation & purification ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Oligosaccharides/chemistry ; Peptides/chemistry
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  • 10
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    Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-10
    Description: The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus, a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100 degrees C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal form averaging. AOR consists of two identical subunits, each containing an Fe4S4 cluster and a molybdopterin-based tungsten cofactor that is analogous to the molybdenum cofactor found in a large class of oxotransferases. Whereas the general features of the tungsten coordination in this cofactor were consistent with a previously proposed structure, each AOR subunit unexpectedly contained two molybdopterin molecules that coordinate a tungsten by a total of four sulfur ligands, and the pterin system was modified by an intramolecular cyclization that generated a three-ringed structure. In comparison to other proteins, the hyperthermophilic enzyme AOR has a relatively small solvent-exposed surface area, and a relatively large number of both ion pairs and buried atoms. These properties may contribute to the extreme thermostability of this enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chan, M K -- Mukund, S -- Kletzin, A -- Adams, M W -- Rees, D C -- 1F32 GM15006/GM/NIGMS NIH HHS/ -- GM50775/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1463-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, Pasadena, CA 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7878465" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Oxidoreductases/*chemistry/metabolism ; Amino Acid Sequence ; Archaea/*enzymology ; Binding Sites ; *Coenzymes ; Computer Graphics ; Crystallography, X-Ray ; Enzyme Stability ; Ferrous Compounds ; Metalloproteins/analysis/chemistry ; Models, Molecular ; Molecular Sequence Data ; Organometallic Compounds/analysis/*chemistry ; Oxidation-Reduction ; Protein Conformation ; Protein Structure, Secondary ; Pteridines/analysis/chemistry ; Pterins/analysis/*chemistry ; Surface Properties ; Temperature ; Tungsten/analysis/*chemistry
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  • 11
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    Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-19
    Description: The three-dimensional structure of the complex formed by two plasma proteins, transthyretin and retinol-binding protein, was determined from x-ray diffraction data to a nominal resolution of 3.1 angstroms. One tetramer of transthyretin was bound to two molecules of retinol-binding protein. The two retinol-binding protein molecules established molecular interactions with the same transthyretin dimer, and each also made contacts with one of the other two monomers. Thus, the other two potential binding sites in a transthyretin tetramer were blocked. The amino acid residues of the retinol-binding protein that were involved in the contacts were close to the retinol-binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Monaco, H L -- Rizzi, M -- Coda, A -- New York, N.Y. -- Science. 1995 May 19;268(5213):1039-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, University of Pavia, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754382" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biopolymers ; Chickens ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Molecular Sequence Data ; Prealbumin/*chemistry ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Retinol-Binding Proteins/*chemistry ; Retinol-Binding Proteins, Plasma ; Sequence Homology, Amino Acid
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  • 12
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    Requirement for Src family protein tyrosine kinases in G2 for fibroblast cell division (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-15
    Description: The protein tyrosine kinase c-Src is transiently activated at the transition from the G2 phase to mitosis in the cell cycle of mammalian fibroblasts. Fyn and Yes, the other members of the Src family present in fibroblasts, were also found to be activated at mitosis. In cells microinjected with a neutralizing antibody specific for Src, Fyn, and Yes (anti-cst.1) during G2, cell division was inhibited by 75 percent. The block occurred before nuclear envelope breakdown. Antibodies specific for phosphatidylinositol-3 kinase alpha and phospholipase C-gamma 1 had no effect. Microinjection of the Src homology 2 (SH2) domain of Fyn was also inhibitory. Functional redundancy between members of the Src family was observed; a Src-specific antibody had no effect in NIH 3T3 cells but inhibited cell division in fibroblasts in which the only functional Src family kinase was Src itself. Thus, Src family kinases and proteins associating with their SH2 domains are required for entry into mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roche, S -- Fumagalli, S -- Courtneidge, S A -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1567-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut National de la Sante et de la Recherche Medicale (INSERM) faculte de Pharmacie, Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7545311" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Enzyme Activation ; *G2 Phase ; Isoenzymes/immunology/metabolism ; Mice ; Microinjections ; *Mitosis ; Molecular Sequence Data ; Nocodazole/pharmacology ; Phospholipase C gamma ; Protein-Tyrosine Kinases/immunology/*metabolism ; Proto-Oncogene Proteins/immunology/*metabolism ; Proto-Oncogene Proteins c-fyn ; Proto-Oncogene Proteins c-yes ; Proto-Oncogene Proteins pp60(c-src)/immunology/metabolism ; Type C Phospholipases/immunology/metabolism ; *src-Family Kinases
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    Requirement of serine phosphorylation for formation of STAT-promoter complexes (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-31
    Description: Members of the interleukin-6 family of cytokines bind to and activate receptors that contain a common subunit, gp130. This leads to the activation of Stat3 and Stat1, two cytoplasmic signal transducers and activators of transcription (STATs), by tyrosine phosphorylation. Serine phosphorylation of Stat3 was constitutive and was enhanced by signaling through gp130. In cells of lymphoid and neuronal origins, inhibition of serine phosphorylation prevented the formation of complexes of DNA with Stat3-Stat3 but not with Stat3-Stat1 or Stat1-Stat1 dimers. In vitro serine dephosphorylation of Stat3 also inhibited DNA binding of Stat3-Stat3. The requirement of serine phosphorylation for Stat3-Stat3.DNA complex formation was inversely correlated with the affinity of Stat3-Stat3 for the binding site. Thus, serine phosphorylation appears to enhance or to be required for the formation of stable Stat3-Stat3.DNA complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, X -- Blenis, J -- Li, H C -- Schindler, C -- Chen-Kiang, S -- CA46595/CA/NCI NIH HHS/ -- HL 21006/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1990-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Brookdale Center for Molecular Biology, Mount Sinai School of Medicine, New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701321" target="_blank"〉PubMed〈/a〉
    Keywords: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Nucleus/metabolism ; Ciliary Neurotrophic Factor ; Cytoplasm/metabolism ; DNA/metabolism ; DNA-Binding Proteins/*metabolism ; Humans ; Interleukin-6/metabolism/*pharmacology ; Isoquinolines/pharmacology ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins/pharmacology ; Phosphorylation ; Piperazines/pharmacology ; *Promoter Regions, Genetic ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; Serine/*metabolism ; Signal Transduction ; Threonine/metabolism ; Trans-Activators/*metabolism ; Tumor Cells, Cultured ; Tyrosine/metabolism
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  • 14
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    Ethylene insensitivity conferred by Arabidopsis ERS gene (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-22
    Description: ERS (ethylene response sensor), a gene in the Arabidopsis thaliana ethylene hormone-response pathway, was uncovered by cross-hybridization with the Arabidopsis ETR1 gene. The deduced ERS protein has sequence similarity with the amino-terminal domain and putative histidine protein kinase domain of ETR1, but it does not have a receiver domain as found in ETR1. A missense mutation identical to the dominant etr1-4 mutation was introduced into the ERS gene. The altered ERS gene conferred dominant ethylene insensitivity to wild-type Arabidopsis. Double-mutant analysis indicates that ERS acts upstream of the CTR1 protein kinase gene in the ethylene-response pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hua, J -- Chang, C -- Sun, Q -- Meyerowitz, E M -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1712-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569898" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/chemistry/drug effects/*genetics/physiology ; Arabidopsis Proteins ; Base Sequence ; Cloning, Molecular ; Ethylenes/*pharmacology ; *Genes, Plant ; Kanamycin Resistance ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phenotype ; Plant Proteins/chemistry/*genetics/physiology ; Plants, Genetically Modified ; *Receptors, Cell Surface
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  • 15
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    Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: The crystal structure of the aldehyde oxido-reductase (Mop) from the sulfate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas has been determined at 2.25 A resolution by multiple isomorphous replacement and refined. The protein, a homodimer of 907 amino acid residues subunits, is a member of the xanthine oxidase family. The protein contains a molybdopterin cofactor (Mo-co) and two different [2Fe-2S] centers. It is folded into four domains of which the first two bind the iron sulfur centers and the last two are involved in Mo-co binding. Mo-co is a molybdenum molybdopterin cytosine dinucleotide. Molybdopterin forms a tricyclic system with the pterin bicycle annealed to a pyran ring. The molybdopterin dinucleotide is deeply buried in the protein. The cis-dithiolene group of the pyran ring binds the molybdenum, which is coordinated by three more (oxygen) ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Romao, M J -- Archer, M -- Moura, I -- Moura, J J -- LeGall, J -- Engh, R -- Schneider, M -- Hof, P -- Huber, R -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1170-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Instituto de Tecnologia Quimica e Biologica, Oeiras, Portugal.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502041" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Oxidoreductases/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Coenzymes/chemistry/metabolism ; Crystallization ; Crystallography, X-Ray ; Cytosine Nucleotides/chemistry/metabolism ; Desulfovibrio/*enzymology ; Drosophila melanogaster/enzymology ; Electron Transport ; Hydrogen Bonding ; Iron/chemistry ; Ligands ; Metalloproteins/chemistry/metabolism ; Molecular Sequence Data ; Molybdenum/chemistry/metabolism ; Oxidation-Reduction ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Pteridines/chemistry/metabolism ; Pterins/chemistry/metabolism ; Xanthine ; Xanthine Oxidase/*chemistry ; Xanthines/metabolism
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  • 16
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    Integrins and modulation of transmitter release from motor nerve terminals by stretch (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-15
    Description: The stretch of a frog muscle within the physiological range can more than double the spontaneous and evoked release of neurotransmitter from its motor nerve terminals. Here, stretch enhancement of release was suppressed by peptides containing the sequence arginine-glycine-aspartic acid (RGD), which blocks integrin binding. Integrin antibodies also inhibited the enhancement obtained by stretching. Stretch enhancement depended on intraterminal calcium derived both from external calcium and from internal stores. Muscle stretch thus might enhance the release of neurotransmitters either by elevating internal calcium concentrations or by increasing the sensitivity of transmitter release to calcium in the nerve terminal.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, B M -- Grinnell, A D -- NS06232/NS/NINDS NIH HHS/ -- NS30673/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1578-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jerry Lewis Neuromuscular Research Center, University of California at Los Angeles School of Medicine, 90024, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667637" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium/metabolism ; In Vitro Techniques ; Integrins/*physiology ; Membrane Potentials ; Microelectrodes ; Molecular Sequence Data ; Motor Endplate/physiology ; Motor Neurons/*physiology ; Neuromuscular Junction/*physiology ; Neurotransmitter Agents/*metabolism ; Oligopeptides/pharmacology ; Rana pipiens
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  • 17
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    Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: Ubiquitin is a highly conserved polypeptide found in all eukaryotes. The major function of ubiquitin is to target proteins for complete or partial degradation by a multisubunit protein complex called the proteasome. Here, the Drosophila fat facets gene, which is required for the appropriate determination of particular cells in the fly eye, was shown to encode a ubiquitin-specific protease (Ubp), an enzyme that cleaves ubiquitin from ubiquitin-protein conjugates. The Fat facets protein (FAF) acts as a regulatory Ubp that prevents degradation of its substrate by the proteasome. Flies bearing fat facets gene mutations were used to show that a Ubp is cell type--and substrate-specific and a regulator of cell fate decisions in a multicellular organism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Y -- Baker, R T -- Fischer-Vize, J A -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1828-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Texas, Austin 78712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525378" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Cell Differentiation/genetics ; Cysteine/metabolism ; Drosophila/embryology/enzymology/genetics ; Endopeptidases/genetics/*metabolism ; Escherichia coli ; Eye/embryology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Recombinant Fusion Proteins/genetics/metabolism ; Ubiquitins/*metabolism ; beta-Galactosidase/genetics
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  • 18
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    PER protein interactions and temperature compensation of a circadian clock in Drosophila (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-02-24
    Description: The periods of circadian clocks are relatively temperature-insensitive. Indeed, the perL mutation in the Drosophila melanogaster period gene, a central component of the clock, affects temperature compensation as well as period length. The per protein (PER) contains a dimerization domain (PAS) within which the perL mutation is located. Amino acid substitutions at the perL position rendered PER dimerization temperature-sensitive. In addition, another region of PER interacted with PAS, and the perL mutation enhanced this putative intramolecular interaction, which may compete with PAS-PAS intermolecular interactions. Therefore, temperature compensation of circadian period in Drosophila may be due in part to temperature-independent PER activity, which is based on competition between inter- and intramolecular interactions with similar temperature coefficients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Z J -- Curtin, K D -- Rosbash, M -- GM-33205/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1169-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Brandeis University, Department of Biology, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855598" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Biological Clocks ; *Circadian Rhythm ; Drosophila Proteins ; Drosophila melanogaster/genetics/*physiology ; Gene Expression Regulation ; Genes, Insect ; Molecular Sequence Data ; Nuclear Proteins/chemistry/genetics/*metabolism ; Period Circadian Proteins ; Point Mutation ; Temperature
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  • 19
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    Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-04
    Description: Phosphoinositide-3 kinase activity is implicated in diverse cellular responses triggered by mammalian cell surface receptors and in the regulation of protein sorting in yeast. Receptors with intrinsic and associated tyrosine kinase activity recruit heterodimeric phosphoinositide-3 kinases that consist of p110 catalytic subunits and p85 adaptor molecules containing Src homology 2 (SH2) domains. A phosphoinositide-3 kinase isotype, p110 gamma, was cloned and characterized. The p110 gamma enzyme was activated in vitro by both the alpha and beta gamma subunits of heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins) and did not interact with p85. A potential pleckstrin homology domain is located near its amino terminus. The p110 gamma isotype may link signaling through G protein-coupled receptors to the generation of phosphoinositide second messengers phosphorylated in the D-3 position.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stoyanov, B -- Volinia, S -- Hanck, T -- Rubio, I -- Loubtchenkov, M -- Malek, D -- Stoyanova, S -- Vanhaesebroeck, B -- Dhand, R -- Nurnberg, B -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):690-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Research Unit in Growth Factor Signal Transduction, Medical Faculty, University of Jena, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624799" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cloning, Molecular ; Enzyme Activation ; GTP-Binding Proteins/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Humans ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositols/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Tumor Cells, Cultured
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  • 20
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    The white gene of Ceratitis capitata: a phenotypic marker for germline transformation (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-22
    Description: Reliable germline transformation is required for molecular studies and ultimately for genetic control of economically important insects, such as the Mediterranean fruit fly (medfly) Ceratitis capitata. A prerequisite for the establishment and maintenance of transformant lines is selectable or phenotypically dominant markers. To this end, a complementary DNA clone derived from the medfly white gene was isolated, which showed substantial similarity to white genes in Drosophila melanogaster and other Diptera. It is correlated with a spontaneous mutation causing white eyes in the medfly and can be used to restore partial eye color in transgenic Drosophila carrying a null mutation in the endogenous white gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwiebel, L J -- Saccone, G -- Zacharopoulou, A -- Besansky, N J -- Favia, G -- Collins, F H -- Louis, C -- Kafatos, F C -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):2005-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL), Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533095" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Cloning, Molecular ; Diptera/chemistry/*genetics ; *Drosophila Proteins ; Drosophila melanogaster/genetics ; Eye Color/genetics ; Eye Proteins/chemistry/*genetics ; *Genes, Insect ; Genetic Markers ; Insect Hormones/chemistry/genetics ; Molecular Sequence Data ; Mutation ; Phenotype ; Sequence Alignment ; *Transformation, Genetic
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  • 21
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    A region of adenylyl cyclase 2 critical for regulation by G protein beta gamma subunits (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-26
    Description: Receptor-mediated activation of heterotrimeric guanine nucleotide-binding proteins (G proteins) results in the dissociation of alpha from beta gamma subunits, thereby allowing both to regulate effectors. Little is known about the regions of effectors required for recognition of G beta gamma. A peptide encoding residues 956 to 982 of adenylyl cyclase 2 specifically blocked G beta gamma stimulation of adenylyl cyclase 2, phospholipase C-beta 3, potassium channels, and beta-adrenergic receptor kinase as well as inhibition of calmodulin-stimulated adenylyl cyclases, but had no effect on interactions between G beta gamma and G alpha o. Substitutions in this peptide identified a functionally important motif, Gln-X-X-Glu-Arg, that is also conserved in regions of potassium channels and beta-adrenergic receptor kinases that participate in G beta gamma interactions. Thus, the region defined by residues 956 to 982 of adenylyl cyclase 2 may contain determinants important for receiving signals from G beta gamma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, J -- DeVivo, M -- Dingus, J -- Harry, A -- Li, J -- Sui, J -- Carty, D J -- Blank, J L -- Exton, J H -- Stoffel, R H -- CA-44998/CA/NCI NIH HHS/ -- DK-37219/DK/NIDDK NIH HHS/ -- DK-38761/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 May 26;268(5214):1166-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Mount Sinai School of Medicine, City University of New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7761832" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclase Inhibitors ; Adenylyl Cyclases/*chemistry/metabolism ; Amino Acid Sequence ; Animals ; Cell Line ; Enzyme Activation/physiology ; GTP-Binding Proteins/chemistry/*physiology ; Guanosine Triphosphate/physiology ; In Vitro Techniques ; Molecular Sequence Data ; Peptide Fragments/chemical synthesis/chemistry/physiology ; Potassium Channels/physiology ; Rats ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptors, Adrenergic, beta/metabolism ; Signal Transduction/physiology ; Structure-Activity Relationship ; Type C Phospholipases/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 22
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    Possible exceptions to rules for alpha-helix termination by glycine (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altschuler, E L -- Lades, M -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1451-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660132" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; Glycine/*chemistry ; Molecular Sequence Data ; Protein Folding ; *Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry
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  • 23
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    Involvement of CRAF1, a relative of TRAF, in CD40 signaling (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-10
    Description: CD40 is a receptor on the surface of B lymphocytes, the activation of which leads to B cell survival, growth, and differentiation. A yeast two-hybrid screen identified a gene, CRAF1, encoding a protein that interacts directly with the CD40 cytoplasmic tail through a region of similarity to the tumor necrosis factor-alpha (TNF-alpha) receptor-associated factors. Overexpression of a truncated CRAF1 gene inhibited CD40-mediated up-regulation of CD23. A region of CRAF1 was similar to the TNF-alpha receptor-associated factors TRAF1 and TRAF2 and so defined a shared TRAF-C domain that was necessary and sufficient for CD40 binding and homodimerization. The CRAF1 sequence also predicted a long amphipathic helix, a pattern of five zinc fingers, and a zinc ring finger. It is likely that other members of the TNF receptor superfamily use CRAF-related proteins in their signal transduction processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheng, G -- Cleary, A M -- Ye, Z S -- Hong, D I -- Lederman, S -- Baltimore, D -- 5-T32-GM07367/GM/NIGMS NIH HHS/ -- A122346/PHS HHS/ -- R01-CA55713/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Mar 10;267(5203):1494-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7533327" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/*metabolism ; Antigens, CD40 ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; Humans ; Mice ; Molecular Sequence Data ; Protein Structure, Secondary ; Proteins/chemistry/genetics/*physiology ; Receptors, IgE/metabolism ; Sequence Homology, Amino Acid ; *Signal Transduction ; TNF Receptor-Associated Factor 1 ; TNF Receptor-Associated Factor 2 ; TNF Receptor-Associated Factor 3 ; Up-Regulation ; Zinc Fingers
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  • 24
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    Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-11
    Description: In the molecular scheme of living organisms, adenosine 3',5'-monophosphate (cyclic AMP or cAMP) has been a universal second messenger. In eukaryotic cells, the primary receptors for cAMP are the regulatory subunits of cAMP-dependent protein kinase. The crystal structure of a 1-91 deletion mutant of the type I alpha regulatory subunit was refined to 2.8 A resolution. Each of the two tandem cAMP binding domains provides an extensive network of hydrogen bonds that buries the cyclic phosphate and the ribose between two beta strands that are linked by a short alpha helix. Each adenine base stacks against an aromatic ring that lies outside the beta barrel. This structure provides a molecular basis for understanding how cAMP binds cooperatively to its receptor protein, thus mediating activation of the kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Su, Y -- Dostmann, W R -- Herberg, F W -- Durick, K -- Xuong, N H -- Ten Eyck, L -- Taylor, S S -- Varughese, K I -- GM07313/GM/NIGMS NIH HHS/ -- GM34921/GM/NIGMS NIH HHS/ -- RR01644/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):807-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla 92093-0654, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638597" target="_blank"〉PubMed〈/a〉
    Keywords: Affinity Labels ; Amino Acid Sequence ; Binding Sites ; Carrier Proteins/*chemistry/genetics/metabolism ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; Cyclic AMP/analogs & derivatives/*metabolism ; Cyclic AMP-Dependent Protein Kinases/*chemistry ; Enzyme Activation ; Hydrogen Bonding ; *Intracellular Signaling Peptides and Proteins ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary
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  • 25
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    Aberrant subcellular localization of BRCA1 in breast cancer (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: The BRCA1 gene product was identified as a 220-kilodalton nuclear phosphoprotein in normal cells, including breast ductal epithelial cells, and in 18 of 20 tumor cell lines derived from tissues other than breast and ovary. In 16 of 17 breast and ovarian cancer lines and 17 of 17 samples of cells obtained from malignant effusions, however, BRCA1 localized mainly in cytoplasm. Absence of BRCA1 or aberrant subcellular location was also observed to a variable extent in histological sections of many breast cancer biopsies. These findings suggest that BRCA1 abnormalities may be involved in the pathogenesis of many breast cancers, sporadic as well as familial.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Y -- Chen, C F -- Riley, D J -- Allred, D C -- Chen, P L -- Von Hoff, D -- Osborne, C K -- Lee, W H -- CA58318/CA/NCI NIH HHS/ -- EY05758/EY/NEI NIH HHS/ -- P50CA58183/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):789-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Medicine/Institute of Biotechnology, University of Texas Health Science Center at San Antonio 78245, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481765" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; BRCA1 Protein ; Base Sequence ; Breast/*chemistry ; Breast Neoplasms/*chemistry/ultrastructure ; Cell Fractionation ; Cell Line ; Cell Nucleus/chemistry ; Cytoplasm/*chemistry ; Female ; Humans ; Male ; Molecular Sequence Data ; Mutation ; Neoplasm Proteins/*analysis/genetics/metabolism ; Neoplasms/chemistry/ultrastructure ; Ovarian Neoplasms/chemistry/ultrastructure ; Pleural Effusion, Malignant/chemistry/pathology ; Transcription Factors/*analysis/genetics/metabolism ; Tumor Cells, Cultured
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    Crystal structure of Pseudomonas mevalonii HMG-CoA reductase at 3.0 angstrom resolution (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-23
    Description: The rate-limiting step in cholesterol biosynthesis in mammals is catalyzed by 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase, a four-electron oxidoreductase that converts HMG-CoA to mevalonate. The crystal structure of HMG-CoA reductase from Pseudomonas mevalonii was determined at 3.0 angstrom resolution by multiple isomorphous replacement. The structure reveals a tightly bound dimer that brings together at the subunit interface the conserved residues implicated in substrate binding and catalysis. These dimers are packed about a threefold crystallographic axis, forming a hexamer with 23 point group symmetry. Difference Fourier studies reveal the binding sites for the substrates HMG-CoA and reduced or oxidized nicotinamide adenine dinucleotide [NAD(H)] and demonstrate that the active sites are at the dimer interfaces. The HMG-CoA is bound by a domain with an unusual fold, consisting of a central alpha helix surrounded by a triangular set of walls of beta sheets and alpha helices. The NAD(H) is bound by a domain characterized by an antiparallel beta structure that defines a class of dinucleotide-binding domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawrence, C M -- Rodwell, V W -- Stauffacher, C V -- AI 127713/AI/NIAID NIH HHS/ -- HL 47113/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1758-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792601" target="_blank"〉PubMed〈/a〉
    Keywords: Acyl Coenzyme A/metabolism ; Amino Acid Sequence ; Binding Sites ; Computer Graphics ; Crystallography, X-Ray ; Fourier Analysis ; Hydroxymethylglutaryl CoA Reductases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; NAD/metabolism ; Protein Folding ; Protein Structure, Secondary ; Pseudomonas/*enzymology
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    Conversion of Xenopus ectoderm into neurons by NeuroD, a basic helix-loop-helix protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: Basic helix-loop-helix (bHLH) proteins are instrumental in determining cell type during development. A bHLH protein, termed NeuroD, for neurogenic differentiation, has now been identified as a differentiation factor for neurogenesis because (i) it is expressed transiently in a subset of neurons in the central and peripheral nervous systems at the time of their terminal differentiation into mature neurons and (ii) ectopic expression of neuroD in Xenopus embryos causes premature differentiation of neuronal precursors. Furthermore, neuroD can convert presumptive epidermal cells into neurons and also act as a neuronal determination gene. However, unlike another previously identified proneural gene (XASH-3), neuroD seems competent to bypass the normal inhibitory influences that usually prevent neurogenesis in ventral and lateral ectoderm and is capable of converting most of the embryonic ectoderm into neurons. The data suggest that neuroD may participate in the terminal differentiation step during vertebrate neuronal development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, J E -- Hollenberg, S M -- Snider, L -- Turner, D L -- Lipnick, N -- Weintraub, H -- New York, N.Y. -- Science. 1995 May 12;268(5212):836-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754368" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Basic Helix-Loop-Helix Transcription Factors ; Cell Adhesion Molecules, Neuronal/biosynthesis ; Cell Differentiation/*genetics ; Cloning, Molecular ; Ectoderm/*cytology ; Gene Expression Regulation, Developmental ; *Helix-Loop-Helix Motifs/genetics ; Mice ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/*genetics/physiology ; Nervous System/cytology/embryology ; Neural Crest/cytology ; Neurons/*cytology/metabolism ; Sequence Alignment ; Xenopus
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    Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: TFIID is a multisubunit protein complex comprised of the TATA-binding protein (TBP) and multiple TBP-associated factors (TAFs). The TAFs in TFIID are essential for activator-dependent transcription. The cloning of a complementary DNA encoding a human TFIID TAF, TAFII55, that has no known homolog in Drosophila TFIID is now described. TAFII55 is shown to interact with the largest subunit (TAFII230) of human TFIID through its central region and with multiple activators--including Sp1, YY1, USF, CTF, adenoviral E1A, and human immunodeficiency virus-type 1 Tat proteins--through a distinct amino-terminal domain. The TAFII55-interacting region of Sp1 was localized to its DNA-binding domain, which is distinct from the glutamine-rich activation domains previously shown to interact with Drosophila TAFII110. Thus, this human TFIID TAF may be a co-activator that mediates a response to multiple activators through a distinct mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiang, C M -- Roeder, R G -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):531-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824954" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/metabolism ; Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA-Binding Proteins/metabolism ; Erythroid-Specific DNA-Binding Factors ; Gene Products, tat/metabolism ; HeLa Cells ; Humans ; Molecular Sequence Data ; Sp1 Transcription Factor/chemistry/metabolism ; *TATA-Binding Protein Associated Factors ; TATA-Box Binding Protein ; Trans-Activators/chemistry/genetics/*metabolism ; Transcription Factor TFIID ; Transcription Factors/*chemistry/*metabolism ; Upstream Stimulatory Factors ; YY1 Transcription Factor
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    Absence of p350 subunit of DNA-activated protein kinase from a radiosensitive human cell line (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-24
    Description: The radiosensitive rodent mutant cell line xrs-5 is defective in DNA double-strand break repair and lacks the Ku component of the DNA-activated protein kinase, DNA-PK. Here radiosensitive human cell lines were analyzed for DNA-PK activity and for the presence of related proteins. The radiosensitive human malignant glioma M059J cell line was found to be defective in DNA double-strand break repair, but fails to express the p350 subunit of DNA-PK. These results suggest that DNA-PK kinase activity is involved in DNA double-strand break repair.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lees-Miller, S P -- Godbout, R -- Chan, D W -- Weinfeld, M -- Day, R S 3rd -- Barron, G M -- Allalunis-Turner, J -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1183-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Science, University of Calgary, Alberta, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855602" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigens, Nuclear ; CHO Cells ; Cell Line, Transformed ; Cricetinae ; DNA/metabolism ; *DNA Helicases ; *DNA Repair ; DNA-Activated Protein Kinase ; DNA-Binding Proteins/analysis ; Gamma Rays ; Humans ; Molecular Sequence Data ; Nuclear Proteins/analysis ; Protein-Serine-Threonine Kinases/*metabolism ; *Radiation Tolerance ; Tumor Cells, Cultured
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    Reconstitution of IKATP: an inward rectifier subunit plus the sulfonylurea receptor (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: A member of the inwardly rectifying potassium channel family was cloned here. The channel, called BIR (Kir6.2), was expressed in large amounts in rat pancreatic islets and glucose-responsive insulin-secreting cell lines. Coexpression with the sulfonylurea receptor SUR reconstituted an inwardly rectifying potassium conductance of 76 picosiemens that was sensitive to adenosine triphosphate (ATP) (IKATP) and was inhibited by sulfonylureas and activated by diazoxide. The data indicate that these pancreatic beta cell potassium channels are a complex composed of at least two subunits--BIR, a member of the inward rectifier potassium channel family, and SUR, a member of the ATP-binding cassette superfamily. Gene mapping data show that these two potassium channel subunit genes are clustered on human chromosome 11 at position 11p15.1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Inagaki, N -- Gonoi, T -- Clement, J P 4th -- Namba, N -- Inazawa, J -- Gonzalez, G -- Aguilar-Bryan, L -- Seino, S -- Bryan, J -- DK44311/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1166-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Medicine, Chiba University School of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502040" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Triphosphate/pharmacology ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; Cloning, Molecular ; Cricetinae ; Diazoxide/pharmacology ; Humans ; Islets of Langerhans/metabolism ; KATP Channels ; Mice ; Molecular Sequence Data ; Potassium/*metabolism ; Potassium Channels/*chemistry/genetics/*metabolism ; *Potassium Channels, Inwardly Rectifying ; Rats ; Receptors, Drug/*chemistry/metabolism ; Rubidium/metabolism ; Sulfonylurea Compounds/pharmacology ; Sulfonylurea Receptors
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    A morbillivirus that caused fatal disease in horses and humans (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-07
    Description: A morbillivirus has been isolated and added to an increasing list of emerging viral diseases. This virus caused an outbreak of fatal respiratory disease in horses and humans. Genetic analyses show it to be only distantly related to the classic morbilliviruses rinderpest, measles, and canine distemper. When seen by electron microscopy, viruses had 10- and 18-nanometer surface projections that gave them a "double-fringed" appearance. The virus induced syncytia that developed in the endothelium of blood vessels, particularly the lungs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Murray, K -- Selleck, P -- Hooper, P -- Hyatt, A -- Gould, A -- Gleeson, L -- Westbury, H -- Hiley, L -- Selvey, L -- Rodwell, B -- New York, N.Y. -- Science. 1995 Apr 7;268(5207):94-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CSIRO Australian Animal Health Laboratory, East Geelong, Victoria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701348" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Animals ; Base Sequence ; Cercopithecus aethiops ; Disease Outbreaks/*veterinary ; Female ; Horse Diseases/epidemiology/mortality/*virology ; Horses ; Humans ; Kidney/virology ; Lung/virology ; Male ; Middle Aged ; Molecular Sequence Data ; Morbillivirus/genetics/*isolation & purification ; Morbillivirus Infections/epidemiology/mortality/*veterinary/*virology ; Pregnancy ; Queensland/epidemiology ; Respiratory Tract Infections/veterinary/virology ; Spleen/virology ; Vero Cells ; Virus Cultivation
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    Casein kinase II alpha transgene-induced murine lymphoma: relation to theileriosis in cattle (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-02-10
    Description: Infection of cattle with the protozoan parasite Theileria parva results in a fatal lymphoproliferative syndrome that is associated with the overexpression of casein kinase II. The role of this enzyme in the pathogenesis of lymphoproliferative disorders was investigated by expressing the catalytic subunit in lymphocytes of transgenic mice. Adult transgenic mice displayed a stochastic propensity to develop lymphoma; co-expression of a c-myc transgene in addition to casein kinase II resulted in neonatal leukemia. Thus, the casein kinase II gene can serve as an oncogene, and its dysregulated expression is capable of transforming lymphocytes in a two-step pathway with c-myc.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seldin, D C -- Leder, P -- 1-K08-HL0286-01/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 10;267(5199):894-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Howard Hughes Medical Institute, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7846532" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Casein Kinase II ; Cattle ; *Cell Transformation, Neoplastic ; Cloning, Molecular ; Gene Expression Regulation, Enzymologic ; Gene Rearrangement, T-Lymphocyte ; Genes, myc ; Leukemia/etiology ; Lymphocytes/enzymology ; Lymphoma/enzymology/*etiology/genetics ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Theileriasis/*enzymology ; Up-Regulation
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    Crystal structure of the mammalian Grb2 adaptor (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-14
    Description: The mammalian growth factor receptor-binding protein Grb2 is an adaptor that mediates activation of guanine nucleotide exchange on Ras. Grb2 binds to the receptor through its SH2 domain and to the carboxyl-terminal domain of Son of sevenless through its two SH3 domains. It is thus a key element in the signal transduction pathway. The crystal structure of Grb2 was determined to 3.1 angstrom resolution. The asymmetric unit is composed of an embedded dimer. The interlaced junctions between the SH2 and SH3 domains bring the two adjacent faces of the SH3 domains in van der Waals contact but leave room for the binding of proline-rich peptides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maignan, S -- Guilloteau, J P -- Fromage, N -- Arnoux, B -- Becquart, J -- Ducruix, A -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):291-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Biologie Structurale, Unite Mixte de Recherche CNRS-Universite de Paris-Sud, Gif sur Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716522" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Binding Sites ; Computer Graphics ; Crystallization ; Crystallography, X-Ray ; GRB2 Adaptor Protein ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Proteins/*chemistry/metabolism ; *Receptor, Epidermal Growth Factor/metabolism
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    Architectures of class-defining and specific domains of glutamyl-tRNA synthetase (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-03-31
    Description: The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and refined at 2.5 A resolution. The amino-terminal half of GluRS shows a geometrical similarity with that of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) of the same subclass in class I, comprising the class I-specific Rossmann fold domain and the intervening subclass-specific alpha/beta domain. These domains were found to have two GluRS-specific, secondary-structure insertions, which then participated in the specific recognition of the D and acceptor stems of tRNA(Glu) as indicated by mutagenesis analyses based on the docking properties of GluRS and tRNA. In striking contrast to the beta-barrel structure of the GlnRS carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an all-alpha-helix architecture, an alpha-helix cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nureki, O -- Vassylyev, D G -- Katayanagi, K -- Shimizu, T -- Sekine, S -- Kigawa, T -- Miyazawa, T -- Yokoyama, S -- Morikawa, K -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1958-65.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biochemistry, School of Science, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701318" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acyl-tRNA Synthetases/chemistry ; Anticodon ; Biological Evolution ; Computer Graphics ; Crystallography, X-Ray ; Escherichia coli/enzymology ; Glutamate-tRNA Ligase/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; RNA, Transfer, Glu/chemistry/metabolism ; Sequence Alignment ; Thermus thermophilus/*enzymology
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    A Drosophila homolog of the yeast origin recognition complex (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-12-08
    Description: Genes from Drosophila melanogaster have been identified that encode proteins homologous to Orc2p and Orc5p of the Saccharomyces cerevisiae origin recognition complex (ORC). The abundance of the Drosophila Orc2p homolog DmORC2 is developmentally regulated and is greatest during the earliest stages of embryogenesis, concomitant with the highest rate of DNA replication. Fractionation of embryo nuclear extracts revealed that DmORC2 is found in a tightly associated complex with five additional polypeptides, much like the yeast ORC. These studies will enable direct testing of the initiator-based model of replication in a metazoan.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gossen, M -- Pak, D T -- Hansen, S K -- Acharya, J K -- Botchan, M R -- CA30490/CA/NCI NIH HHS/ -- ES-01896/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1674-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502079" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; *DNA Replication ; DNA, Complementary/genetics ; DNA-Binding Proteins/analysis/*chemistry/*genetics/physiology ; Drosophila melanogaster/chemistry/embryology/*genetics ; Embryo, Nonmammalian/chemistry ; *Genes, Insect ; Molecular Sequence Data ; Molecular Weight ; Origin Recognition Complex ; *Replication Origin ; Repressor Proteins/analysis/*chemistry/*genetics/physiology ; Saccharomyces cerevisiae/genetics ; Sequence Homology
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    Transcriptional activation by tetracyclines in mammalian cells (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-23
    Description: A transcriptional transactivator was developed that fuses the VP16 activation domain with a mutant Tet repressor from Escherichia coli. This transactivator requires certain tetracycline (Tc) derivatives for specific DNA binding. Thus, addition of doxycycline to HeLa cells that constitutively synthesized the transactivator and that contained an appropriate, stably integrated reporter unit rapidly induced gene expression more than a thousandfold. The specificity of the Tet repressor-operator-effector interaction and the pharmacological characteristics of Tc's make this regulatory system well suited for the control of gene activities in vivo, such as in transgenic animals and possibly in gene therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gossen, M -- Freundlieb, S -- Bender, G -- Muller, G -- Hillen, W -- Bujard, H -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1766-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zentrum fur Molekulare Biologie der Universitat Heidelberg, (ZMDH), Im Neuenheimer Feld 282, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792603" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Doxycycline/*pharmacology ; Genes, Reporter ; HeLa Cells ; Humans ; Molecular Sequence Data ; Operator Regions, Genetic ; Recombinant Fusion Proteins/genetics ; Repressor Proteins/chemistry/*genetics ; Simplexvirus ; Trans-Activators/*genetics ; Transcriptional Activation/*drug effects ; Transfection ; Viral Proteins/genetics
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    Structure of the Arabidopsis RPM1 gene enabling dual specificity disease resistance (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-11
    Description: Plants can recognize pathogens through the action of disease resistance (R) genes, which confer resistance to pathogens expressing unique corresponding avirulence (avr) genes. The molecular basis of this gene-for-gene specificity is unknown. The Arabidopsis thaliana RPM1 gene enables dual specificity to pathogens expressing either of two unrelated Pseudomonas syringae avr genes. Despite this function, RPM1 encodes a protein sharing molecular features with recently described single-specificity R genes. Surprisingly, RPM1 is lacking from naturally occurring, disease-susceptible Arabidopsis accessions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grant, M R -- Godiard, L -- Straube, E -- Ashfield, T -- Lewald, J -- Sattler, A -- Innes, R W -- Dangl, J L -- R29 GM 46451/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):843-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Delbruck Laboratory, Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638602" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*genetics/microbiology ; *Arabidopsis Proteins ; Base Sequence ; Genes, Bacterial ; *Genes, Plant ; Genetic Complementation Test ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Plant Diseases/*genetics ; Plant Proteins/chemistry/*genetics ; Plants, Genetically Modified ; Polymorphism, Restriction Fragment Length ; Pseudomonas/genetics/growth & development/pathogenicity ; Transformation, Genetic ; Virulence/genetics
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    Molecular basis of the cauliflower phenotype in Arabidopsis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: Genetic studies demonstrate that two Arabidopsis genes, CAULIFLOWER and APETALA1, encode partially redundant activities involved in the formation of floral meristems, the first step in the development of flowers. Isolation of the CAULIFLOWER gene from Arabidopsis reveals that it is closely related in sequence to APETALA1. Like APETALA1, CAULIFLOWER is expressed in young flower primordia and encodes a MADS-domain, indicating that it may function as a transcription factor. Analysis of the cultivated garden variety of cauliflower (Brassica oleracea var. botrytis) reveals that its CAULIFLOWER gene homolog is not functional, suggesting a molecular basis for one of the oldest recognized flower abnormalities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kempin, S A -- Savidge, B -- Yanofsky, M F -- GM07313/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):522-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093-0116.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824951" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Arabidopsis/chemistry/*genetics/physiology ; *Arabidopsis Proteins ; Base Sequence ; Brassica/genetics ; DNA-Binding Proteins/chemistry/*genetics/physiology ; *Genes, Plant ; Genetic Complementation Test ; *Homeodomain Proteins ; In Situ Hybridization ; *MADS Domain Proteins ; Molecular Sequence Data ; Phenotype ; Plant Proteins/chemistry/*genetics/physiology ; RNA, Plant/genetics/metabolism
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    Designer tissues take hold (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Service, R F -- New York, N.Y. -- Science. 1995 Oct 13;270(5234):230-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569968" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Artificial Organs ; *Biocompatible Materials ; *Biomedical Engineering ; Cartilage, Articular/cytology/transplantation ; Cell Transplantation ; Culture Techniques ; Endothelium, Vascular/cytology ; Humans ; Liver/cytology ; Molecular Sequence Data ; Neurons/cytology ; *Organoids ; Skin, Artificial ; Tissue Transplantation
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  • 40
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    A receptor kinase-like protein encoded by the rice disease resistance gene, Xa21 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: The rice Xa21 gene, which confers resistance to Xanthomonas oryzae pv. oryzae race 6, was isolated by positional cloning. Fifty transgenic rice plants carrying the cloned Xa21 gene display high levels of resistance to the pathogen. The sequence of the predicted protein, which carries both a leucine-rich repeat motif and a serine-threonine kinase-like domain, suggests a role in cell surface recognition of a pathogen ligand and subsequent activation of an intracellular defense response. Characterization of Xa21 should facilitate understanding of plant disease resistance and lead to engineered resistance in rice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Song, W Y -- Wang, G L -- Chen, L L -- Kim, H S -- Pi, L Y -- Holsten, T -- Gardner, J -- Wang, B -- Zhai, W X -- Zhu, L H -- Fauquet, C -- Ronald, P -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1804-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Pathology, University of California, Davis 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525370" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; *Genes, Plant ; Genetic Linkage ; Molecular Sequence Data ; Oryza/enzymology/*genetics/microbiology ; Plant Diseases ; Plant Proteins/*genetics/metabolism ; Plants, Genetically Modified ; Protein-Serine-Threonine Kinases/*genetics/metabolism ; Receptor Protein-Tyrosine Kinases ; Receptors, Cell Surface/*genetics/metabolism ; Xanthomonas/physiology
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  • 41
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    KAI1, a metastasis suppressor gene for prostate cancer on human chromosome 11p11.2 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: A gene from human chromosome 11p11.2 was isolated and was shown to suppress metastasis when introduced into rat AT6.1 prostate cancer cells. Expression of this gene, designated KAI1, was reduced in human cell lines derived from metastatic prostate tumors. KAI1 specifies a protein of 267 amino acids, with four hydrophobic and presumably transmembrane domains and one large extracellular hydrophilic domain with three potential N-glycosylation sites. KAI1 is evolutionarily conserved, is expressed in many human tissues, and encodes a member of a structurally distinct family of leukocyte surface glycoproteins. Decreased expression of this gene may be involved in the malignant progression of prostate and other cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dong, J T -- Lamb, P W -- Rinker-Schaeffer, C W -- Vukanovic, J -- Ichikawa, T -- Isaacs, J T -- Barrett, J C -- CA 58236/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 May 12;268(5212):884-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Carcinogenesis, National Institute of Environmental Health Sciences, National Institute of Health, Research Triangle Park, NC 27709, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754374" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/chemistry/*genetics/physiology ; Antigens, CD82 ; Base Sequence ; Biological Evolution ; *Chromosomes, Human, Pair 11 ; Gene Expression ; *Genes, Tumor Suppressor ; Humans ; Male ; Membrane Glycoproteins/chemistry/*genetics/physiology ; Mice ; Mice, SCID ; Molecular Sequence Data ; Neoplasm Metastasis/*genetics ; Prostatic Neoplasms/*genetics/pathology ; *Proto-Oncogene Proteins ; Rats ; Transfection ; Tumor Cells, Cultured
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  • 42
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    A VAMP-binding protein from Aplysia required for neurotransmitter release (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-15
    Description: Before the fusion of synaptic vesicles with the plasma membrane, a protein complex is thought to form between VAMP--an integral membrane protein of the vesicle--and two proteins associated with the plasma membrane, SNAP-25 and syntaxin. The yeast two-hybrid interaction cloning system has now been used to identify additional proteins from Aplysia that interact directly with VAMP. A 33-kilodalton membrane protein, termed VAP-33 (VAMP-associated protein of 33 kilodaltons), was identified whose corresponding messenger RNA was detected only in the central nervous system and the gill of Aplysia. Presynaptic injection of antibodies specific for VAP-33 inhibited synaptic transmission, which suggests that VAP-33 is required for the exocytosis of neurotransmitter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Skehel, P A -- Martin, K C -- Kandel, E R -- Bartsch, D -- R37 MH45923-06/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1580-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, College of Physicians and Surgeons of Columbia University, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7667638" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aplysia ; Base Sequence ; Carrier Proteins/chemistry/genetics/*physiology ; Cells, Cultured ; Central Nervous System/chemistry ; Cloning, Molecular ; Exocytosis ; Gills/innervation ; Membrane Proteins/chemistry/genetics/*metabolism/*physiology ; Molecular Sequence Data ; Molecular Weight ; Motor Neurons/physiology ; Nerve Tissue Proteins/*metabolism ; Neurons/*physiology ; Neurons, Afferent/physiology ; Neurotransmitter Agents/*metabolism ; R-SNARE Proteins ; *Synaptic Transmission ; Synaptic Vesicles/physiology ; *Vesicular Transport Proteins
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  • 43
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    Gene trap tagging of PROLIFERA, an essential MCM2-3-5-like gene in Arabidopsis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-12
    Description: Gene trap transposon mutagenesis can identify essential genes whose functions in later development are obscured by an early lethal phenotype. In higher plants, many genes are required for haploid gametophyte viability, so that the phenotypic effects of their disruption cannot be readily observed in the diploid plant body. The PROLIFERA (PRL) gene, identified by gene trap transposon mutagenesis in Arabidopsis, is required for megaga-metophyte and embryo development. Reporter gene expression patterns revealed that PRL was expressed in dividing cells throughout the plant. PRL is related to the MCM2-3-5 family of yeast genes that are required for the initiation of DNA replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Springer, P S -- McCombie, W R -- Sundaresan, V -- Martienssen, R A -- New York, N.Y. -- Science. 1995 May 12;268(5212):877-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7754372" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*genetics/growth & development/physiology ; *Arabidopsis Proteins ; Base Sequence ; Cell Cycle Proteins/genetics ; Crosses, Genetic ; DNA Transposable Elements ; Fungal Proteins/genetics ; *Genes, Plant ; Genes, Reporter ; Minichromosome Maintenance Complex Component 7 ; Molecular Sequence Data ; Mutagenesis, Insertional ; Phenotype ; Plant Proteins/chemistry/*genetics ; Seeds/growth & development ; Sequence Alignment
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    Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: Peptide synthetases involved in the nonribosomal synthesis of peptide secondary metabolites possess a highly conserved domain structure. The arrangement of these domains within the multifunctional enzymes determines the number and order of the amino acid constituents of the peptide product. A general approach has been developed for targeted substitution of amino acid-activating domains within the srfA operon, which encodes the protein templates for the synthesis of the lipopeptide antibiotic surfactin in Bacillus subtilis. Exchange of domain-coding regions of bacterial and fungal origin led to the construction of hybrid genes that encoded peptide synthetases with altered amino acid specificities and the production of peptides with modified amino acid sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stachelhaus, T -- Schneider, A -- Marahiel, M A -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):69-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemie/Fachbereich Chemie, Philipps-University of Marburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604280" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aminoacylation ; Anti-Bacterial Agents/*biosynthesis/chemistry/pharmacology ; Bacillus/genetics ; Bacillus subtilis/genetics ; Bacterial Proteins/*biosynthesis/chemistry/pharmacology ; Base Sequence ; Cloning, Molecular ; Genes, Bacterial ; Genes, Fungal ; Hemolysis/drug effects ; Lipopeptides ; Mass Spectrometry ; Molecular Sequence Data ; Operon ; Penicillium chrysogenum/genetics ; Peptide Synthases/chemistry/*genetics ; *Peptides, Cyclic ; *Protein Engineering ; Recombinant Fusion Proteins/biosynthesis/chemistry/pharmacology ; Transformation, Bacterial
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  • 45
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    A regulatory role for ARF6 in receptor-mediated endocytosis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-24
    Description: Adenosine diphosphate-ribosylation factor 6 (ARF6), ARF6 mutants, and ARF1 were transiently expressed in Chinese hamster ovary cells, and the effects on receptor-mediated endocytosis were assessed. Overexpressed ARF6 localized to the cell periphery and led to a redistribution of transferrin receptors to the cell surface and a decrease in the rate of uptake of transferrin. Similar results were obtained when a mutant defective in guanosine triphosphate hydrolysis was expressed. Expression of a dominant negative mutant, ARF6(T27N), resulted in an intracellular distribution of transferrin receptors and an inhibition of transferrin recycling to the cell surface. In contrast, overexpression of ARF1 had little or no effect on these parameters of endocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Souza-Schorey, C -- Li, G -- Colombo, M I -- Stahl, P D -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1175-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855600" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1 ; ADP-Ribosylation Factors ; Amino Acid Sequence ; Animals ; Base Sequence ; CHO Cells ; Cell Membrane/metabolism ; Cricetinae ; *Endocytosis ; GTP-Binding Proteins/analysis/genetics/*physiology ; Golgi Apparatus/metabolism/ultrastructure ; Kinetics ; Molecular Sequence Data ; Mutation ; Receptors, Transferrin/metabolism ; Transferrin/metabolism
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  • 46
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    Identification of a graft versus host disease-associated human minor histocompatibility antigen (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-09
    Description: Minor histocompatibility antigen disparities between human leukocyte antigen (HLA)-matched bone marrow donors and recipients are a major risk factor for graft versus host disease (GVHD). An HLA-A2.1-restricted cytotoxic T cell clone that recognized the minor histocompatibility antigen HA-2 was previously isolated from a patient with severe GVHD after HLA-identical bone marrow transplantation. The HLA-A2.1-bound peptide representing HA-2 has now been identified. This peptide appears to originate from a member of the non-filament-forming class I myosin family. Because HA-2 has a phenotype frequency of 95 percent in the HLA-A2.1-positive population, it is a candidate for immunotherapeutic intervention in bone marrow transplantation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉den Haan, J M -- Sherman, N E -- Blokland, E -- Huczko, E -- Koning, F -- Drijfhout, J W -- Skipper, J -- Shabanowitz, J -- Hunt, D F -- Engelhard, V H -- AI20963/AI/NIAID NIH HHS/ -- AI33993/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 9;268(5216):1476-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunohaematology, University Hospital, Leiden, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7539551" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bone Marrow Transplantation ; Epitopes ; Female ; Graft vs Host Disease/*immunology ; HLA-A2 Antigen/immunology ; Humans ; Mass Spectrometry ; Minor Histocompatibility Antigens/chemistry/*immunology ; Molecular Sequence Data ; Neoplasm Proteins/chemistry/*immunology ; Oligopeptides/chemistry/immunology ; T-Lymphocytes, Cytotoxic/immunology
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  • 47
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    Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-03-03
    Description: Many members of the cytokine receptor superfamily initiate intracellular signaling by activating members of the Jak family of tyrosine kinases. Activation of the same Jaks by multiple cytokines raises the question of how these cytokines activate distinct intracellular signaling pathways. Selection of particular substrates--the transcriptional activator Stat3 and protein tyrosine phosphatase PTP1D--that characterize responses to the ciliary neurotrophic factor-interleukin-6 cytokine family depended not on which Jak was activated, but was instead determined by specific tyrosine-based motifs in the receptor components--gp130 and LIFR--shared by these cytokines. Further, these tyrosine-based motifs were modular, because addition of a Stat3-specifying motif to another cytokine receptor, that for erythropoietin, caused it to activate Stat3 in a ligand-dependent fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stahl, N -- Farruggella, T J -- Boulton, T G -- Zhong, Z -- Darnell, J E Jr -- Yancopoulos, G D -- New York, N.Y. -- Science. 1995 Mar 3;267(5202):1349-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7871433" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Antigens, CD ; Cell Line ; Cytokine Receptor gp130 ; DNA-Binding Proteins/*metabolism ; *Growth Inhibitors ; Interleukin-6/pharmacology ; Intracellular Signaling Peptides and Proteins ; Leukemia Inhibitory Factor ; *Lymphokines ; Membrane Glycoproteins/chemistry/*metabolism ; Molecular Sequence Data ; Phosphorylation ; Point Mutation ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/metabolism ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Cytokine/chemistry/*metabolism ; Receptors, OSM-LIF ; Recombinant Fusion Proteins/metabolism ; STAT3 Transcription Factor ; *Signal Transduction ; Trans-Activators/*metabolism ; Tyrosine/metabolism
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  • 48
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    Antigen-specific development of primary and memory T cells in vivo (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-04-07
    Description: The expansion and contraction of specific helper T cells in the draining lymph nodes of normal mice after injection with antigen was followed. T cell receptors from purified primary and memory responder cells had highly restricted junctional regions, indicating antigen-driven selection. Selection for homogeneity in the length of the third complementarity-determining region (CDR3) occurs before selection for some of the characteristic amino acids, indicating the importance of this parameter in T cell receptor recognition. Ultimately, particular T cell receptor sequences come to predominate in the secondary response and others disappear, showing the selective preservation or expansion of specific T cell clones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McHeyzer-Williams, M G -- Davis, M M -- New York, N.Y. -- Science. 1995 Apr 7;268(5207):106-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7535476" target="_blank"〉PubMed〈/a〉
    Keywords: Adjuvants, Immunologic ; Amino Acid Sequence ; Animals ; Antigens/*immunology ; Antigens, CD44 ; Base Sequence ; Carrier Proteins/biosynthesis ; Cell Adhesion Molecules/biosynthesis ; Immunologic Memory/*immunology ; L-Selectin ; Lymphocyte Activation/immunology ; Mice ; Molecular Sequence Data ; Receptors, Antigen, T-Cell, alpha-beta/biosynthesis/chemistry ; Receptors, Cell Surface/biosynthesis ; Receptors, Lymphocyte Homing/biosynthesis ; T-Lymphocytes, Helper-Inducer/*immunology
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  • 49
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    Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-27
    Description: Cell fate is determined by cell-specific activation of transcription factor sigma F after asymmetric division during sporulation by Bacillus subtilis. The activity of sigma F is governed by SpoIIAA, SpoIIAB, and SpoIIE, a membrane protein localized at the polar septum. SpoIIAB binds to and inhibits sigma F, and SpoIIAA inhibits SpoIIAB, which prevents SpoIIAB from binding to sigma F. SpoIIAB is also a serine kinase that inactivates SpoIIAA. Here, it is demonstrated that SpoIIE dephosphorylates SpoIIAA-P and overcomes SpoIIAB-mediated inhibition of sigma F. The finding that SpoIIE is a serine phosphatase links asymmetric division to the pathway governing cell-specific gene transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duncan, L -- Alper, S -- Arigoni, F -- Losick, R -- Stragier, P -- GM18568/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):641-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570023" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Bacillus subtilis/cytology/genetics/*physiology ; Bacterial Proteins/antagonists & inhibitors/*metabolism ; Cell Division ; Molecular Sequence Data ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; Sigma Factor/antagonists & inhibitors/*metabolism ; Spores, Bacterial/*physiology ; *Transcription Factors ; *Transcription, Genetic
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  • 50
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    A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-01
    Description: A mutated cyclin-dependent kinase 4 (CDK4) was identified as a tumor-specific antigen recognized by HLA-A2. 1-restricted autologous cytolytic T lymphocytes (CTLs) in a human melanoma. The mutated CDK4 allele was present in autologous cultured melanoma cells and metastasis tissue, but not in the patient's lymphocytes. The mutation, an arginine-to-cysteine exchange at residue 24, was part of the CDK4 peptide recognized by CTLs and prevented binding of the CDK4 inhibitor p16INK4a, but not of p21 or of p27KIP1. The same mutation was found in one additional melanoma among 28 melanomas analyzed. These results suggest that mutation of CDK4 can create a tumor-specific antigen and can disrupt the cell-cycle regulation exerted by the tumor suppressor p16INK4a.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolfel, T -- Hauer, M -- Schneider, J -- Serrano, M -- Wolfel, C -- Klehmann-Hieb, E -- De Plaen, E -- Hankeln, T -- Meyer zum Buschenfelde, K H -- Beach, D -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1281-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medizinische Klinik und Poliklinik, Johannes Gutenberg-Universitat, Mainz, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652577" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carrier Proteins/metabolism/*pharmacology ; *Cell Cycle Proteins ; Cell Line ; Cloning, Molecular ; Cyclin-Dependent Kinase 4 ; Cyclin-Dependent Kinase Inhibitor p15 ; Cyclin-Dependent Kinase Inhibitor p16 ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclin-Dependent Kinase Inhibitor p27 ; *Cyclin-Dependent Kinases ; Cyclins/metabolism/pharmacology ; HLA-A2 Antigen/immunology ; Humans ; Melanoma/enzymology/*immunology ; Microtubule-Associated Proteins/metabolism/pharmacology ; Molecular Sequence Data ; Point Mutation ; Polymerase Chain Reaction ; Protein-Serine-Threonine Kinases/antagonists & ; inhibitors/genetics/*immunology/metabolism ; *Proto-Oncogene Proteins ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Laminin beta 2 (S-laminin): a new player at the synapse (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, Z W -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):362-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20814, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618101" target="_blank"〉PubMed〈/a〉
    Keywords: Agrin/physiology ; Amino Acid Sequence ; Animals ; Basement Membrane/metabolism ; Laminin/*physiology ; Molecular Sequence Data ; Motor Neurons/*physiology ; Nerve Regeneration ; Neurites/physiology ; Neuromuscular Junction/*physiology ; Oligopeptides/physiology ; Receptors, Cholinergic/metabolism ; Signal Transduction ; Synapses/*physiology
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    Participation of the protein Go in multiple aspects of behavior in C. elegans (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-17
    Description: The goa-1 gene encoding the alpha subunit of the heterotrimeric guanosine triphosphate-binding protein (G protein) Go from Caenorhabditis elegans is expressed in most neurons, and in the muscles involved in egg laying and male mating. Reduction-of-function mutations in goa-1 caused a variety of behavioral defects including hyperactive movement, premature egg laying, and male impotence. Expression of the activated Go alpha subunit (G alpha o) in transgenic nematodes resulted in lethargic movement, delayed egg laying, and reduced mating efficiency. Induced expression of activated G alpha o in adults was sufficient to cause these phenotypes, indicating that G alpha o mediates behavior through its role in neuronal function and the functioning of specialized muscles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendel, J E -- Korswagen, H C -- Liu, K S -- Hajdu-Cronin, Y M -- Simon, M I -- Plasterk, R H -- Sternberg, P W -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7886455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Base Sequence ; Behavior, Animal ; Caenorhabditis elegans/genetics/*physiology ; Disorders of Sex Development ; Female ; GTP-Binding Proteins/genetics/*physiology ; Genes, Helminth ; Male ; Molecular Sequence Data ; Movement ; Muscles/innervation/physiology ; Mutation ; Neurons/physiology ; Oviposition ; Phenotype ; Serotonin/pharmacology ; Sexual Behavior, Animal
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    Domain interaction between NMDA receptor subunits and the postsynaptic density protein PSD-95 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-22
    Description: The N-methyl-D-aspartate (NMDA) receptor subserves synaptic glutamate-induced transmission and plasticity in central neurons. The yeast two-hybrid system was used to show that the cytoplasmic tails of NMDA receptor subunits interact with a prominent postsynaptic density protein PSD-95. The second PDZ domain in PSD-95 binds to the seven-amino acid, COOH-terminal domain containing the terminal tSXV motif (where S is serine, X is any amino acid, and V is valine) common to NR2 subunits and certain NR1 splice forms. Transcripts encoding PSD-95 are expressed in a pattern similar to that of NMDA receptors, and the NR2B subunit co-localizes with PSD-95 in cultured rat hippocampal neurons. The interaction of these proteins may affect the plasticity of excitatory synapses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kornau, H C -- Schenker, L T -- Kennedy, M B -- Seeburg, P H -- NS-28710/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1737-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Biology (ZMBH), University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569905" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Cytoplasm/chemistry ; Genes, Reporter ; Hippocampus/*metabolism ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins ; Molecular Sequence Data ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Neuronal Plasticity ; Neurons/*metabolism ; RNA Splicing ; Rats ; Receptors, N-Methyl-D-Aspartate/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
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    Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-06
    Description: The genetic properties of the [URE3] non-Mendelian element of Saccharomyces cerevisiae suggest that it is a prion (infectious protein) form of Ure2p, a regulator of nitrogen catabolism. In extracts from [URE3] strains, Ure2p was partially resistant to proteinase K compared with Ure2p from wild-type extracts. Overexpression of Ure2p in wild-type strains induced a 20- to 200-fold increase in the frequency with which [URE3] arose. Overexpression of just the amino-terminal 65 residues of Ure2p increased the frequency of [URE3] induction 6000-fold. Without this "prion-inducing domain" the carboxyl-terminal domain performed the nitrogen regulation function of Ure2p, but could not be changed to the [URE3] prion state. Thus, this domain induced the prion state in trans, whereas in cis it conferred susceptibility of the adjoining nitrogen regulatory domain to prion infections.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Masison, D C -- Wickner, R B -- New York, N.Y. -- Science. 1995 Oct 6;270(5233):93-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Genetics of Simple Eukaryotes, National Institute of Diabetes, Digestive and Kidney Disease, National Institutes of Health, Bethesda, MD 20892-0830, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569955" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Endopeptidase K ; Fungal Proteins/chemistry/*genetics/metabolism ; Genes, Fungal ; Genetic Complementation Test ; Glutathione Peroxidase ; Molecular Sequence Data ; Nitrogen/metabolism ; Plasmids ; Prions/*genetics/metabolism ; Promoter Regions, Genetic ; Saccharomyces cerevisiae/chemistry/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Sequence Deletion ; Serine Endopeptidases/metabolism
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    Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-11-10
    Description: Polychlorinated biphenyls (PCBs) typify a class of stable aromatic pollutants that are targeted by bioremediation strategies. In the aerobic degradation of biphenyl by bacteria, the key step of ring cleavage is catalyzed by an Fe(II)-dependent extradiol dioxygenase. The crystal structure of 2,3-dihydroxybiphenyl 1,2-dioxygenase from a PCB-degrading strain of Pseudomonas cepacia has been determined at 1.9 angstrom resolution. The monomer comprises amino- and carboxyl-terminal domains. Structural homology between and within the domains reveals evolutionary relationships within the extradiol dioxygenase family. The iron atom has five ligands in square pyramidal geometry: one glutamate and two histidine side chains, and two water molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Han, S -- Eltis, L D -- Timmis, K N -- Muchmore, S W -- Bolin, J T -- GM 52831/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):976-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481800" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biodegradation, Environmental ; Crystallography, X-Ray ; *Dioxygenases ; Evolution, Molecular ; Ferrous Compounds/chemistry/metabolism ; Hydrogen Bonding ; Ligands ; Models, Molecular ; Molecular Sequence Data ; Oxygen/chemistry/metabolism ; Oxygenases/*chemistry/metabolism ; Polychlorinated Biphenyls/metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Pseudomonas/*enzymology ; Sequence Alignment
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    Structure-based design of transcription factors (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-01-06
    Description: Computer modeling suggested that transcription factors with novel sequence specificities could be designed by combining known DNA binding domains. This structure-based strategy was tested by construction of a fusion protein, ZFHD1, that contained zinc fingers 1 and 2 from Zif268, a short polypeptide linker, and the homeodomain from Oct-1. The fusion protein bound optimally to a sequence containing adjacent homeodomain (TAATTA) and zinc finger (NGGGNG) subsites. When fused to an activation domain, ZFHD1 regulated promoter activity in vivo in a sequence-specific manner. Analysis of known protein-DNA complexes suggests that many other DNA binding proteins could be designed in a similar fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pomerantz, J L -- Sharp, P A -- Pabo, C O -- P01-CA42063/CA/NCI NIH HHS/ -- P30-CA14051/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):93-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809612" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Computer Simulation ; DNA-Binding Proteins/*chemistry/genetics/metabolism ; Gene Expression Regulation ; Homeodomain Proteins/chemistry ; Host Cell Factor C1 ; Models, Molecular ; Molecular Sequence Data ; Octamer Transcription Factor-1 ; Promoter Regions, Genetic ; Protein Engineering ; Recombinant Fusion Proteins/*chemistry/metabolism ; Transcription Factors/*chemistry/genetics/metabolism ; Transfection ; *Zinc Fingers
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    Tissue- and species-specific expression of sp56, a mouse sperm fertilization protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: Mouse sperm recognize and bind to ZP3, one of three glycoproteins in the egg's zona pellucida. A mouse sperm protein, sp56, was identified that has the characteristics expected of the sperm protein responsible for recognition of ZP3. The complementary DNA encoding sp56 was isolated, and its primary sequence indicates that sp56 is a member of a superfamily of protein receptors. It was shown that sp56 expression is restricted to mouse spermatids and that the presence or absence of sp56 on sperm from different species accounts for species specificity of sperm-egg recognition in mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bookbinder, L H -- Cheng, A -- Bleil, J D -- R01 HD 27847/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):86-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scripps Research Institute, Department of Molecular Biology, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604284" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cricetinae ; Egg Proteins/*metabolism ; Female ; Guinea Pigs ; Humans ; Male ; Membrane Glycoproteins/*metabolism ; Mice ; Molecular Sequence Data ; Molecular Weight ; Organ Specificity ; RNA, Messenger/analysis/genetics ; Receptors, Cell Surface/*biosynthesis/chemistry/genetics/metabolism ; Species Specificity ; Sperm-Ovum Interactions/*physiology ; Spermatids/metabolism ; Spermatozoa/*metabolism ; Zona Pellucida/*metabolism
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    Conformation and function of the N-linked glycan in the adhesion domain of human CD2 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-01
    Description: The adhesion domain of human CD2 bears a single N-linked carbohydrate. The solution structure of a fragment of CD2 containing the covalently bound high-mannose N-glycan [-(N-acetylglucosamine)2-(mannose)5-8] was solved by nuclear magnetic resonance. The stem and two of three branches of the carbohydrate structure are well defined and the mobility of proximal glycan residues is restricted. Mutagenesis of all residues in the vicinity of the glycan suggests that the glycan is not a component of the CD2-CD58 interface; rather, the carbohydrate stabilizes the protein fold by counterbalancing an unfavorable clustering of five positive charges centered about lysine-61 of CD2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wyss, D F -- Choi, J S -- Li, J -- Knoppers, M H -- Willis, K J -- Arulanandam, A R -- Smolyar, A -- Reinherz, E L -- Wagner, G -- New York, N.Y. -- Science. 1995 Sep 1;269(5228):1273-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7544493" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylglucosamine/chemistry ; Amino Acid Sequence ; Animals ; Antigens, CD/metabolism ; Antigens, CD2/*chemistry/metabolism ; Antigens, CD58 ; Binding Sites ; CHO Cells ; Carbohydrate Conformation ; Carbohydrate Sequence ; Cell Adhesion ; Cricetinae ; Glycosylation ; Humans ; Magnetic Resonance Spectroscopy ; Membrane Glycoproteins/metabolism ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligosaccharides/*chemistry ; *Protein Conformation
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  • 59
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    Revealing the architecture of a K+ channel pore through mutant cycles with a peptide inhibitor (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-04-14
    Description: Thermodynamic mutant cycles provide a formalism for studying energetic coupling between amino acids on the interaction surface in a protein-protein complex. This approach was applied to the Shaker potassium channel and to a high-affinity peptide inhibitor (scorpion toxin) that binds to its pore entryway. The assignment of pairwise interactions defined the spatial arrangement of channel amino acids with respect to the known inhibitor structure. A strong constraint was placed on the Shaker channel pore-forming region by requiring its amino-terminal border to be 12 to 15 angstroms from the central axis. This method is directly applicable to sodium, calcium, and other ion channels where inhibitor or modulatory proteins bind with high affinity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hidalgo, P -- MacKinnon, R -- GM43949/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):307-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716527" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Oocytes ; Potassium Channels/*chemistry/genetics/metabolism ; Scorpion Venoms/*metabolism ; Shaker Superfamily of Potassium Channels ; Thermodynamics ; Toxins, Biological/*metabolism ; Xenopus laevis
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    Identification of a member of the MAPKKK family as a potential mediator of TGF-beta signal transduction (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-12-22
    Description: The mitogen-activated protein kinase (MAPK) pathway is a conserved eukaryotic signaling module that converts receptor signals into various outputs. MAPK is activated through phosphorylation by MAPK kinase (MAPKK), which is first activated by MAPKK kinase (MAPKKK). A genetic selection based on a MAPK pathway in yeast was used to identify a mouse protein kinase (TAK1) distinct from other members of the MAPKKK family. TAK1 was shown to participate in regulation of transcription by transforming growth factor-beta (TGF-beta). Furthermore, kinase activity of TAK1 was stimulated in response to TGF-beta and bone morphogenetic protein. These results suggest that TAK1 functions as a mediator in the signaling pathway of TGF-beta superfamily members.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamaguchi, K -- Shirakabe, K -- Shibuya, H -- Irie, K -- Oishi, I -- Ueno, N -- Taniguchi, T -- Nishida, E -- Matsumoto, K -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):2008-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Faculty of Science, Nagoya University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533096" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Bone Morphogenetic Proteins ; Cell Line ; Cloning, Molecular ; Epidermal Growth Factor/pharmacology ; *Gene Expression Regulation ; Genes, Reporter ; *MAP Kinase Kinase Kinases ; Mice ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases/*metabolism ; Proteins/pharmacology ; Saccharomyces cerevisiae/genetics ; *Signal Transduction ; Transfection ; Transforming Growth Factor beta/*pharmacology
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    Inhibitors of HIV nucleocapsid protein zinc fingers as candidates for the treatment of AIDS (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-11-17
    Description: Strategies for the treatment of human immunodeficiency virus-type 1 (HIV-1) infection must contend with the obstacle of drug resistance. HIV-1 nucleocapsid protein zinc fingers are prime antiviral targets because they are mutationally intolerant and are required both for acute infection and virion assembly. Nontoxic disulfide-substituted benzamides were identified that attack the zinc fingers, inactivate cell-free virions, inhibit acute and chronic infections, and exhibit broad antiretroviral activity. The compounds were highly synergistic with other antiviral agents, and resistant mutants have not been detected. Zinc finger-reactive compounds may offer an anti-HIV strategy that restricts drug-resistance development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rice, W G -- Supko, J G -- Malspeis, L -- Buckheit, R W Jr -- Clanton, D -- Bu, M -- Graham, L -- Schaeffer, C A -- Turpin, J A -- Domagala, J -- Gogliotti, R -- Bader, J P -- Halliday, S M -- Coren, L -- Sowder, R C 2nd -- Arthur, L O -- Henderson, L E -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1194-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Antiviral Drug Mechanisms, PRI/DynCorp., National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502043" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antiviral Agents/chemistry/pharmacokinetics/*pharmacology ; Benzamides/chemistry/pharmacokinetics/*pharmacology ; Biological Availability ; Capsid/chemistry/*metabolism ; *Capsid Proteins ; Cell Line ; Disulfides/chemistry/pharmacokinetics/*pharmacology ; Drug Resistance, Microbial ; Drug Synergism ; Gene Products, gag/*antagonists & inhibitors/chemistry ; HIV-1/*drug effects/physiology ; Humans ; Male ; Mice ; Molecular Sequence Data ; *Viral Proteins ; Zinc Fingers/*drug effects ; gag Gene Products, Human Immunodeficiency Virus
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  • 62
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    Similarity of sli-1, a regulator of vulval development in C. elegans, to the mammalian proto-oncogene c-cbl (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-25
    Description: Vulval induction during Caenorhabditis elegans development is mediated by LET-23, a homolog of the mammalian epidermal growth factor receptor tyrosine kinase. The sli-1 gene is a negative regulator of LET-23 and is shown here to encode a protein similar to c-Cbl, a mammalian proto-oncoprotein. SLI-1 and c-Cbl share approximately 55 percent amino acid identity over a stretch of 390 residues, which includes a C3HC4 zinc-binding motif known as the RING finger, and multiple consensus binding sites for Src homology 3 (SH3) domains. SLI-1 and c-Cbl may define a new class of proteins that modify receptor tyrosine kinase-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoon, C H -- Lee, J -- Jongeward, G D -- Sternberg, P W -- New York, N.Y. -- Science. 1995 Aug 25;269(5227):1102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7652556" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Caenorhabditis elegans/*genetics/growth & development ; *Caenorhabditis elegans Proteins ; Conserved Sequence ; DNA, Complementary/genetics ; Female ; *Genes, Helminth ; *Genes, Regulator ; Helminth Proteins/chemistry/*genetics/metabolism ; Humans ; Molecular Sequence Data ; Mutation ; Proto-Oncogene Proteins/chemistry/*genetics ; Proto-Oncogene Proteins c-cbl ; Receptor, Epidermal Growth Factor/metabolism ; Sequence Alignment ; Signal Transduction ; *Ubiquitin-Protein Ligases ; Vulva/growth & development
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    Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-10
    Description: Integrin receptors mediate cell adhesion, signal transduction, and cytoskeletal organization. How a single transmembrane receptor can fulfill multiple functions was clarified by comparing roles of receptor occupancy and aggregation. Integrin occupancy by monovalent ligand induced receptor redistribution, but minimal tyrosine phosphorylation signaling or cytoskeletal protein redistribution. Aggregation of integrins by noninhibitory monoclonal antibodies on beads induced intracellular accumulations of pp125FAK and tensin, as well as phosphorylation, but no accumulation of other cytoskeletal proteins such as talin. Combining antibody-mediated clustering with monovalent ligand occupancy induced accumulation of seven cytoskeletal proteins, including alpha-actinin, talin, and F-actin, thereby mimicking multivalent interactions with fibronectin or polyvalent peptides. Integrins therefore mediate a complex repertoire of functions through the distinct effects of receptor aggregation, receptor occupancy, or both together.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyamoto, S -- Akiyama, S K -- Yamada, K M -- New York, N.Y. -- Science. 1995 Feb 10;267(5199):883-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Developmental Biology, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892-4370.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7846531" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Cell Adhesion Molecules/metabolism ; Cell Membrane/*metabolism ; Cells, Cultured ; Cytoskeletal Proteins/*metabolism ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Humans ; Integrins/*physiology ; Ligands ; Microfilament Proteins/metabolism ; Molecular Sequence Data ; Oligopeptides/metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Signal Transduction ; Tyrosine/metabolism
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    Role of yeast insulin-degrading enzyme homologs in propheromone processing and bud site selection (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-20
    Description: The Saccharomyces cerevisiae AXL1 gene product Axl1p shares homology with the insulin-degrading enzyme family of endoproteases. Yeast axl1 mutants showed a defect in a-factor pheromone secretion, and a probable site of processing by Axl1p was identified within the a-factor precursor. In addition, Axl1p appears to function as a morphogenetic determinant for axial bud site selection. Amino acid substitutions within the presumptive active site of Axl1p caused defects in propheromone processing but failed to perturb bud site selection. Thus, Axl1p has been shown to participate in the dual regulation of distinct signaling pathways, and a member of the insulinase family has been implicated in propeptide processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Adames, N -- Blundell, K -- Ashby, M N -- Boone, C -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):464-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569998" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Membrane/metabolism ; Cloning, Molecular ; Fungal Proteins/chemistry/genetics/metabolism/*physiology ; Genes, Fungal ; Insulysin/chemistry/genetics/*physiology ; Lipoproteins/genetics/*metabolism ; Metalloendopeptidases ; Molecular Sequence Data ; Morphogenesis ; Mutagenesis, Site-Directed ; Phenotype ; Pheromones/genetics/*metabolism ; Protein Precursors/genetics/*metabolism ; Protein Processing, Post-Translational ; Saccharomyces cerevisiae/cytology/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Signal Transduction
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    Cloning of the beta cell high-affinity sulfonylurea receptor: a regulator of insulin secretion (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-21
    Description: Sulfonylureas are a class of drugs widely used to promote insulin secretion in the treatment of non-insulin-dependent diabetes mellitus. These drugs interact with the sulfonylurea receptor of pancreatic beta cells and inhibit the conductance of adenosine triphosphate (ATP)-dependent potassium (KATP) channels. Cloning of complementary DNAs for the high-affinity sulfonylurea receptor indicates that it is a member of the ATP-binding cassette or traffic ATPase superfamily with multiple membrane-spanning domains and two nucleotide binding folds. The results suggest that the sulfonylurea receptor may sense changes in ATP and ADP concentration, affect KATP channel activity, and thereby modulate insulin release.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aguilar-Bryan, L -- Nichols, C G -- Wechsler, S W -- Clement, J P 4th -- Boyd, A E 3rd -- Gonzalez, G -- Herrera-Sosa, H -- Nguy, K -- Bryan, J -- Nelson, D A -- DK41898/DK/NIDDK NIH HHS/ -- DK44311/DK/NIDDK NIH HHS/ -- HL45742/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):423-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716547" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cloning, Molecular ; Cricetinae ; Insulin/*secretion ; Islets of Langerhans/*metabolism ; Molecular Sequence Data ; Phosphorylation ; Potassium Channels/chemistry/*genetics/metabolism ; *Potassium Channels, Inwardly Rectifying ; Protein Folding ; Protein Structure, Secondary ; Receptors, Drug/chemistry/*genetics/metabolism ; Sequence Alignment ; Sulfonylurea Compounds/metabolism ; Sulfonylurea Receptors ; Transfection ; Tumor Cells, Cultured
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    Crystal structure of the MATa1/MAT alpha 2 homeodomain heterodimer bound to DNA (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-13
    Description: The Saccharomyces cerevisiae MATa1 and MAT alpha 2 homeodomain proteins, which play a role in determining yeast cell type, form a heterodimer that binds DNA and represses transcription in a cell type-specific manner. Whereas the alpha 2 and a1 proteins on their own have only modest affinity for DNA, the a1/alpha 2 heterodimer binds DNA with high specificity and affinity. The three-dimensional crystal structure of the a1/alpha 2 homeodomain heterodimer bound to DNA was determined at a resolution of 2.5 A. The a1 and alpha 2 homeodomains bind in a head-to-tail orientation, with heterodimer contacts mediated by a 16-residue tail located carboxyl-terminal to the alpha 2 homeodomain. This tail becomes ordered in the presence of a1, part of it forming a short amphipathic helix that packs against the a1 homeodomain between helices 1 and 2. A pronounced 60 degree bend is induced in the DNA, which makes possible protein-protein and protein-DNA contacts that could not take place in a straight DNA fragment. Complex formation mediated by flexible protein-recognition peptides attached to stably folded DNA binding domains may prove to be a general feature of the architecture of other classes of eukaryotic transcriptional regulators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, T -- Stark, M R -- Johnson, A D -- Wolberger, C -- GM-37049/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 13;270(5234):262-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205-2185, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569974" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; DNA, Fungal/*chemistry/metabolism ; Fungal Proteins/*chemistry/metabolism ; Homeodomain Proteins/*chemistry/metabolism ; Hydrogen Bonding ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Operator Regions, Genetic ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Repressor Proteins/*chemistry/metabolism ; Saccharomyces cerevisiae/*chemistry/genetics ; *Saccharomyces cerevisiae Proteins ; Transcription, Genetic
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    Construction of a soluble adenylyl cyclase activated by Gs alpha and forskolin (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-23
    Description: A soluble adenylyl cyclase was constructed by linkage of portions of the cytosolic domains of the mammalian type I and type II enzymes. The soluble enzyme was stimulated by both forskolin and the alpha subunit of the heterotrimeric guanine nucleotide-binding protein (G protein) Gs (Gs alpha). Expression of the construct complemented the catabolic defect in a strain of Escherichia coli that is deficient in adenylyl cyclase activity. The active, approximately 60-kilodalton enzyme accumulated in the cytoplasmic fraction of E. coli to yield activities in excess of 1 nanomole per minute per milligram of protein. The two sets of transmembrane helices of mammalian adenylyl cyclases are thus not necessary for the catalytic or the most characteristic regulatory activities of the enzyme. This system may be useful for both genetic and biochemical analysis of G protein-regulated adenylyl cyclases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, W J -- Gilman, A G -- GM34497/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jun 23;268(5218):1769-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7792604" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/chemistry/*metabolism ; Amino Acid Sequence ; Base Sequence ; Colforsin/*pharmacology ; Cyclic AMP/metabolism ; Cytoplasm/enzymology ; Enzyme Activation ; Escherichia coli/enzymology ; GTP-Binding Proteins/chemistry/genetics/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Molecular Sequence Data ; Solubility ; Transformation, Genetic
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    A mechanism for the specific immunogenicity of heat shock protein-chaperoned peptides (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-15
    Description: Endogenously synthesized antigenic determinants are generally presented on major histocompatibility complex (MHC) class I molecules, whereas exogenous determinants are presented by MHC class II molecules. Here, it is shown that exogenous antigens chaperoned by a heat shock protein can be channeled into the endogenous pathway, presented by MHC class I molecules, and recognized by CD8+ T lymphocytes. This pathway is functional only in a subset of macrophages among the cell types tested. These observations provide a basis for the tumor-specific and virus-specific immunogenicity of cognate heat shock protein preparations and offer a mechanism for the classical phenomenon of cross-priming.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suto, R -- Srivastava, P K -- CA44786/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 15;269(5230):1585-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Fordham University, Bronx, NY 10458, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7545313" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigen Presentation ; Antigens, Neoplasm/*immunology ; Antigens, Viral/*immunology ; Cells, Cultured ; Chaperonins/*immunology ; Cytotoxicity, Immunologic ; Epitopes ; Histocompatibility Antigens Class I/immunology ; Macrophages/*immunology ; Macrophages, Peritoneal/immunology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Peptides/immunology ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection ; Tumor Necrosis Factor-alpha/metabolism ; Vesicular stomatitis Indiana virus/*immunology
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    Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-14
    Description: One Ras-dependent protein kinase cascade leading from growth factor receptors to the ERK (extracellular signal-regulated kinases) subgroup of mitogen-activated protein kinases (MAPKs) is dependent on the protein kinase Raf-1, which activates the MEK (MAPK or ERK kinase) dual specificity kinases. A second protein kinase cascade leading to activation of the Jun kinases (JNKs) is dependent on MEKK (MEK kinase). A dual-specificity kinase that activates JNK, named JNKK, was identified that functions between MEKK and JNK. JNKK activated the JNKs but did not activate the ERKs and was unresponsive to Raf-1 in transfected HeLa cells. JNKK also activated another MAPK, p38 (Mpk2; the mammalian homolog of HOG1 from yeast), whose activity is regulated similarly to that of the JNKs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, A -- Minden, A -- Martinetto, H -- Claret, F X -- Lange-Carter, C -- Mercurio, F -- Johnson, G L -- Karin, M -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):286-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California-San Diego School of Medicine, La Jolla 92093-0636, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716521" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Enzyme Activation ; Epidermal Growth Factor/pharmacology ; HeLa Cells ; Humans ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase 4 ; *MAP Kinase Kinase Kinase 1 ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Protein Kinases/chemistry/*metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-raf ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Transfection ; p38 Mitogen-Activated Protein Kinases
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    Minimization of a polypeptide hormone (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-12-08
    Description: A stepwise approach for reducing the size of a polypeptide hormone, atrial natriuretic peptide (ANP), from 28 residues to 15 while retaining high biopotency is described. Systematic structural and functional analysis identified a discontinuous functional epitope for receptor binding and activation, most of which was placed onto a smaller ring (Cys6 to Cys17) that was created by repositioning the ANP native disulfide bond (Cys7 to Cys23). High affinity was subsequently restored by optimizing the remaining noncritical residues by means of phage display. Residues that flanked the mini-ring structure were then deleted in stages, and affinity losses were rectified by additional phage-sorting experiments. Thus, structural and functional data on hormones, coupled with phage display methods, can be used to shrink the hormones to moieties more amendable to small-molecule design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, B -- Tom, J Y -- Oare, D -- Yen, R -- Fairbrother, W J -- Wells, J A -- Cunningham, B C -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1657-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Engineering, Genenteeh, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502074" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Atrial Natriuretic Factor/*chemistry/genetics/immunology/metabolism ; Base Sequence ; Cell Line ; Cyclic GMP/metabolism ; Epitopes ; Guanylate Cyclase/metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Protein Conformation ; *Protein Engineering ; Receptors, Atrial Natriuretic Factor/metabolism
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    A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-02-24
    Description: Mandelate racemase and muconate lactonizing enzyme are structurally homologous but catalyze different reactions, each initiated by proton abstraction from carbon. The structural similarity to mandelate racemase of a previously unidentified gene product was used to deduce its function as a galactonate dehydratase. In this enzyme superfamily that has evolved to catalyze proton abstraction from carbon, three variations of homologous active site architectures are now represented: lysine and histidine bases in the active site of mandelate racemase, only a lysine base in the active site of muconate lactonizing enzyme, and only a histidine base in the active site of galactonate dehydratase. This discovery supports the hypothesis that new enzymatic activities evolve by recruitment of a protein catalyzing the same type of chemical reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Babbitt, P C -- Mrachko, G T -- Hasson, M S -- Huisman, G W -- Kolter, R -- Ringe, D -- Petsko, G A -- Kenyon, G L -- Gerlt, J A -- GM-34572/GM/NIGMS NIH HHS/ -- GM-40570/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1159-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855594" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Histidine/metabolism ; Hydro-Lyases/chemistry/genetics/*metabolism ; *Intramolecular Lyases ; Isomerases/chemistry/*metabolism ; Lysine/metabolism ; Molecular Sequence Data ; Open Reading Frames ; Operon ; *Protons ; Pseudomonas putida/*enzymology/genetics ; Racemases and Epimerases/chemistry/*metabolism
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    FAP-1: a protein tyrosine phosphatase that associates with Fas (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-21
    Description: Fas is a cell surface receptor that controls a poorly understood signal transduction pathway that leads to cell death by means of apoptosis. A protein tyrosine phosphatase, FAP-1, capable of interacting with the cytosolic domain of Fas, was identified. The carboxyl terminal 15 amino acids of Fas are necessary and sufficient for interaction with FAP-1. FAP-1 expression is highest in tissues and cell lines that are relatively resistant to Fas-mediated cytotoxicity. Gene transfer-mediated elevations in FAP-1 partially abolished Fas-induced apoptosis in a T cell line. These findings are consistent with an inhibitory effect of FAP-1 on Fas signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sato, T -- Irie, S -- Kitada, S -- Reed, J C -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):411-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉La Jolla Cancer Research Foundation, Oncogene and Tumor Suppressor Gene Program, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7536343" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD95 ; Antigens, Surface/genetics/*metabolism ; Apoptosis ; Base Sequence ; Cell Line ; Cloning, Molecular ; DNA, Complementary/genetics ; Humans ; Mice ; Molecular Sequence Data ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; T-Lymphocytes/cytology
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    A human telomeric protein (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-12-08
    Description: Telomeres are multifunctional elements that shield chromosome ends from degradation and end-to-end fusions, prevent activation of DNA damage checkpoints, and modulate the maintenance of telomeric DNA by telomerase. A major protein component of human telomeres has been identified and cloned. This factor, TRF, contains one Myb-type DNA-binding repeat and an amino-terminal acidic domain. Immunofluorescent labeling shows that TRF specifically colocalizes with telomeric DNA in human interphase cells and is located at chromosome ends during metaphase. The presence of TRF along the telomeric TTAGGG repeat array demonstrates that human telomeres form a specialized nucleoprotein complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chong, L -- van Steensel, B -- Broccoli, D -- Erdjument-Bromage, H -- Hanish, J -- Tempst, P -- de Lange, T -- GM49046/GM/NIGMS NIH HHS/ -- P30 CA08748-29/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1663-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Cell Biology and Genetics, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502076" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Nucleus/chemistry ; Cloning, Molecular ; DNA-Binding Proteins/analysis/*chemistry/genetics/isolation & purification ; HeLa Cells ; Humans ; Interphase ; Metaphase ; Molecular Sequence Data ; Molecular Weight ; Repetitive Sequences, Nucleic Acid ; Sequence Alignment ; Telomere/*chemistry ; Transfection
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    Association of protein kinase A and protein phosphatase 2B with a common anchoring protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-06
    Description: Specificity of protein kinases and phosphatases may be achieved through compartmentalization with preferred substrates. In neurons, adenosine 3', 5'-monophosphate (cAMP)-dependent protein kinase (PKA) is localized at postsynaptic densities by association of its regulatory subunit with an A kinase anchor protein, AKAP79. Interaction cloning experiments demonstrated that AKAP79 also binds protein phosphatase 2B, or calcineurin (CaN). A ternary complex of PKA, AKAP, and CaN was isolated from bovine brain, and colocalization of the kinase and the phosphatase was established in neurites of cultured hippocampal neurons. The putative CaN-binding domain of AKAP79 is similar to that of the immunophilin FKBP-12, and AKAP79 inhibited CaN phosphatase activity. These results suggest that both PKA and CaN are targeted to subcellular sites by association with a common anchor protein and thereby regulate the phosphorylation state of key neuronal substrates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coghlan, V M -- Perrino, B A -- Howard, M -- Langeberg, L K -- Hicks, J B -- Gallatin, W M -- Scott, J D -- DK09059/DK/NIDDK NIH HHS/ -- GM48231/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):108-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7528941" target="_blank"〉PubMed〈/a〉
    Keywords: A Kinase Anchor Proteins ; *Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Binding Sites ; *Brain Chemistry ; Calcineurin ; Calmodulin-Binding Proteins/analysis/antagonists & inhibitors/*metabolism ; Carrier Proteins/analysis ; Cattle ; Cells, Cultured ; Cyclic AMP-Dependent Protein Kinases/analysis/*metabolism ; Hippocampus/chemistry ; Molecular Sequence Data ; Neurites/chemistry ; Phosphoprotein Phosphatases/analysis/antagonists & inhibitors/*metabolism ; Phosphorylation ; Proteins/*metabolism/pharmacology ; Rats ; Recombinant Proteins/pharmacology ; Tacrolimus/pharmacology
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  • 75
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    Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: The Elongin (SIII) complex activates elongation by mammalian RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin is a heterotrimer composed of A, B, and C subunits of 110, 18, and 15 kilodaltons, respectively. Here, the mammalian Elongin A gene was isolated and expressed, and the Elongin (SIII) complex reconstituted with recombinant subunits. Elongin A is shown to function as the transcriptionally active component of Elongin (SIII) and Elongin B and C as regulatory subunits. Whereas Elongin C assembles with Elongin A to form an AC complex with increased specific activity, Elongin B, a member of the ubiquitin-homology gene family, appears to serve a chaperone-like function, facilitating assembly and enhancing stability of the Elongin (SIII) complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aso, T -- Lane, W S -- Conaway, J W -- Conaway, R C -- GM41628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1439-43.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular and Cell Biology, Oklahoma Medical Research Foundation, Oklahoma City 73104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660129" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Genes, Tumor Suppressor ; *Ligases ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; RNA Polymerase II/*metabolism ; RNA, Messenger/biosynthesis ; Recombinant Proteins/metabolism ; Temperature ; Transcription Factors/chemistry/genetics/isolation & purification/*metabolism ; *Transcription, Genetic ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein
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  • 76
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    The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-22
    Description: Hydrolysis of guanosine triphosphate (GTP) by the small guanosine triphosphatase (GTPase) adenosine diphosphate ribosylation factor-1 (ARF1) depends on a GTPase-activating protein (GAP). A complementary DNA encoding the ARF1 GAP was cloned from rat liver and predicts a protein with a zinc finger motif near the amino terminus. The GAP function required an intact zinc finger and additional amino-terminal residues. The ARF1 GAP was localized to the Golgi complex and was redistributed into a cytosolic pattern when cells were treated with brefeldin A, a drug that prevents ARF1-dependent association of coat proteins with the Golgi. Thus, the GAP is likely to be recruited to the Golgi by an ARF1-dependent mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cukierman, E -- Huber, I -- Rotman, M -- Cassel, D -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1999-2002.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533093" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1 ; ADP-Ribosylation Factors ; Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Brefeldin A ; Cloning, Molecular ; Cyclopentanes/pharmacology ; Cytosol/metabolism ; DNA, Complementary ; GTP-Binding Proteins/*metabolism ; GTPase-Activating Proteins ; Golgi Apparatus/*metabolism ; Guanosine Triphosphate/metabolism ; Liver/metabolism ; Molecular Sequence Data ; Proteins/chemistry/genetics/isolation & purification/*metabolism ; Rats ; *Zinc Fingers
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  • 77
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    Pineal serotonin N-acetyltransferase: expression cloning and molecular analysis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-08
    Description: Pineal serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, or AA-NAT) generates the large circadian rhythm in melatonin, the hormone that coordinates daily and seasonal physiology in some mammals. Complementary DNA encoding ovine AA-NAT was cloned. The abundance of AA-NAT messenger RNA (mRNA) during the day was high in the ovine pineal gland and somewhat lower in retina. AA-NAT mRNA was found unexpectedly in the pituitary gland and in some brain regions. The night-to-day ratio of ovine pineal AA-NAT mRNA is less than 2. In contrast, the ratio exceeds 150 in rats. AA-NAT represents a family within a large superfamily of acetyltransferases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Coon, S L -- Roseboom, P H -- Baler, R -- Weller, J L -- Namboodiri, M A -- Koonin, E V -- Klein, D C -- New York, N.Y. -- Science. 1995 Dec 8;270(5242):1681-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section on Neuroendocrinology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502081" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arylamine N-Acetyltransferase/*genetics/metabolism ; Brain/metabolism ; Cell Line ; Circadian Rhythm ; *Cloning, Molecular ; DNA, Complementary/genetics ; Molecular Sequence Data ; Pineal Gland/*enzymology/metabolism ; Pituitary Gland/metabolism ; RNA, Messenger/genetics/metabolism ; Rats ; Retina/metabolism ; Sequence Alignment ; Sheep ; Transfection
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  • 78
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    Solution structure of the epithelial cadherin domain responsible for selective cell adhesion (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-20
    Description: Cadherins are calcium-dependent cell adhesion molecules containing extracellular repeats of approximately 110 amino acids. The three-dimensional structure of the amino-terminal repeat of mouse epithelial cadherin was determined by multidimensional heteronuclear magnetic resonance spectroscopy. The calcium ion was bound by a short alpha helix and by loops at one end of the seven-stranded beta-barrel structure. An exposed concave face is in a position to provide homophilic binding specificity and was also sensitive to calcium ligation. Unexpected structural similarities with the immunoglobulin fold suggest an evolutionary relation between calcium-dependent and calcium-independent cell adhesion molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Overduin, M -- Harvey, T S -- Bagby, S -- Tong, K I -- Yau, P -- Takeichi, M -- Ikura, M -- New York, N.Y. -- Science. 1995 Jan 20;267(5196):386-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824937" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD2/chemistry ; Binding Sites ; Cadherins/*chemistry/metabolism/physiology ; Calcium/*metabolism ; *Cell Adhesion ; Hydrogen Bonding ; Immunoglobulins/chemistry ; Mice ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary
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  • 79
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    Activation of a G protein complex by aggregation of beta-1,4-galactosyltransferase on the surface of sperm (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-22
    Description: Fertilization is initiated by the species-specific binding of sperm to the extracellular coat of the egg. One sperm receptor for the mouse egg is beta-1,4-galactosyltransferase (GalTase), which binds O-linked oligosaccharides on the egg coat glycoprotein ZP3. ZP3 binding induces acrosomal exocytosis through the activation of a pertussis toxin-sensitive heterotrimeric guanine nucleotide-binding protein (G protein). The cytoplasmic domain of sperm surface GalTase bound to and activated a heterotrimeric G protein complex that contained the Gi alpha subunit. Aggregation of GalTase by multivalent ligands elicited G protein activation. Sperm from transgenic mice that overexpressed GalTase had higher rates of G protein activation than did wild-type sperm, which rendered transgenic sperm hypersensitive to their ZP3 ligand. Thus, the cytoplasmic domain of cell surface GalTase appears to enable it to function as a signal-transducing receptor for extracellular oligosaccharide ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gong, X -- Dubois, D H -- Miller, D J -- Shur, B D -- R01 HD22590/HD/NICHD NIH HHS/ -- R01 HD23479/HD/NICHD NIH HHS/ -- T32 HD07324/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Sep 22;269(5231):1718-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569899" target="_blank"〉PubMed〈/a〉
    Keywords: Acrosome/physiology ; Adenosine Diphosphate Ribose/metabolism ; Amino Acid Sequence ; Animals ; Cell Membrane/enzymology/metabolism ; Egg Proteins/*metabolism ; GTP-Binding Proteins/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Ligands ; Male ; Membrane Glycoproteins/*metabolism ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; N-Acetyllactosamine Synthase/*metabolism ; Peptide Fragments/metabolism ; Pertussis Toxin ; *Receptors, Cell Surface ; Signal Transduction ; Spermatozoa/enzymology/*metabolism ; Virulence Factors, Bordetella/pharmacology ; Zona Pellucida/*chemistry
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  • 80
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    Tobacco MAP kinase: a possible mediator in wound signal transduction pathways (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-12-22
    Description: A complementary DNA encoding a mitogen-activated protein (MAP) kinase homolog has been isolated from tobacco plants. Transcripts of the corresponding gene were not observed in healthy tobacco leaves but began to accumulate 1 minute after mechanical wounding. In tobacco plants transformed with the cloned complementary DNA, trans inactivation of the endogenous homologous gene occurred, and both production of wound-induced jasmonic acid and accumulation of wound-inducible gene transcripts were inhibited. In contrast, the levels of salicylic acid and transcripts for pathogen-inducible, acidic pathogenesis-related proteins were increased upon wounding. These results indicate that this MAP kinase is part of the initial response of higher plants to mechanical wounding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seo, S -- Okamoto, M -- Seto, H -- Ishizuka, K -- Sano, H -- Ohashi, Y -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1988-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533090" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/chemistry/*genetics/metabolism ; Cyclopentanes/metabolism ; DNA, Complementary/genetics ; *Genes, Plant ; Molecular Sequence Data ; Oxylipins ; Phospholipases A/metabolism ; Phosphorylation ; Plant Proteins/metabolism ; Plants, Genetically Modified ; *Plants, Toxic ; Salicylates/metabolism ; Salicylic Acid ; *Signal Transduction ; Tobacco/*enzymology/genetics
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  • 81
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    Presynaptic component of long-term potentiation visualized at individual hippocampal synapses (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-16
    Description: Long-term potentiation has previously been studied with electrophysiological techniques that do not readily separate presynaptic and postsynaptic contributions. Changes in exocytotic-endocytotic cycling have now been monitored at synapses between cultured rat hippocampal neurons by measuring the differential uptake of antibodies that recognize the intraluminal domain of the synaptic vesicle protein synaptotagmin. Vesicular cycling increased markedly during glutamate-induced long-term potentiation. The degree of potentiation was heterogeneous, appearing greater at synapses at which the initial extent of vesicular turnover was low. Thus, changes in presynaptic activity were visualized directly and the spatial distribution of potentiation could be determined at the level of single synaptic boutons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malgaroli, A -- Ting, A E -- Wendland, B -- Bergamaschi, A -- Villa, A -- Tsien, R W -- Scheller, R H -- D.016/Telethon/Italy -- New York, N.Y. -- Science. 1995 Jun 16;268(5217):1624-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Scientific Institute San Raffaele, Milan, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7777862" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Calcium-Binding Proteins ; Cells, Cultured ; Glutamic Acid/pharmacology ; Hippocampus/*cytology/physiology ; Long-Term Potentiation/drug effects/*physiology ; Membrane Glycoproteins/analysis/immunology ; Molecular Sequence Data ; Nerve Tissue Proteins/analysis/immunology ; Neurons/*physiology ; Patch-Clamp Techniques ; Potassium/pharmacology ; Presynaptic Terminals/drug effects/*physiology ; Pyrroles/pharmacology ; Rats ; Receptors, N-Methyl-D-Aspartate/physiology ; *Synaptic Transmission/drug effects ; Synaptic Vesicles/chemistry/metabolism ; Synaptotagmins
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  • 82
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    Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: Germ-line mutations of the von Hippel-Lindau tumor suppressor gene (VHL) predispose individuals to a variety of human tumors, and somatic mutations of this gene have been identified in sporadic renal cell carcinomas and cerebellar hemangioblastomas. Two transcriptional elongation factors, Elongin B and C, were shown to bind in vitro and in vivo to a short, colinear region of the VHL protein (pVHL) that is frequently mutated in human tumors. A peptide replica of this region inhibited binding of pVHL to Elongin B and C whereas a point-mutant derivative, corresponding to a naturally occurring VHL missense mutation, had no effect. These results suggest that the tumor suppression function of pVHL may be linked to its ability to bind to Elongin B and C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kibel, A -- Iliopoulos, O -- DeCaprio, J A -- Kaelin, W G Jr -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1444-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660130" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carcinoma, Renal Cell ; *Genes, Tumor Suppressor ; Germ-Line Mutation ; Humans ; *Ligases ; Mice ; Molecular Sequence Data ; Nuclear Proteins/genetics/*metabolism ; Point Mutation ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/*metabolism ; Transfection ; Tumor Cells, Cultured ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein ; von Hippel-Lindau Disease/genetics
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  • 83
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    An ethylene-inducible component of signal transduction encoded by never-ripe (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: The ripening-impaired tomato mutant Never-ripe (Nr) is insensitive to the plant hormone ethylene. The gene that cosegregates with the Nr locus encodes a protein with homology to the Arabidopsis ethylene receptor ETR1 but is lacking the response regulator domain found in ETR1 and related prokaryotic two-component signal transducers. A single amino acid change in the sensor domain confers ethylene insensitivity when expressed in transgenic tomato plants. Modulation of NR gene expression during fruit ripening controls response to the hormone ethylene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilkinson, J Q -- Lanahan, M B -- Yen, H C -- Giovannoni, J J -- Klee, H J -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1807-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Monsanto Company, Chesterfield, MO 63198, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525371" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics ; Base Sequence ; DNA Primers ; Ethylenes/*metabolism ; Genes, Plant ; Lycopersicon esculentum/*genetics/growth & development/metabolism ; Molecular Sequence Data ; Mutation ; Plant Proteins/*genetics/metabolism ; *Receptors, Cell Surface ; Sequence Homology, Amino Acid ; *Signal Transduction
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  • 84
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    A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-07-14
    Description: CD22 is a membrane immunoglobulin (mIg)-associated protein of B cells. CD22 is tyrosine-phosphorylated when mIg is ligated. Tyrosine-phosphorylated CD22 binds and activates SHP, a protein tyrosine phosphatase known to negatively regulate signaling through mIg. Ligation of CD22 to prevent its coaggregation with mIg lowers the threshold at which mIg activates the B cell by a factor of 100. In secondary lymphoid organs, CD22 may be sequestered away from mIg through interactions with counterreceptors on T cells. Thus, CD22 is a molecular switch for SHP that may bias mIg signaling to anatomic sites rich in T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doody, G M -- Justement, L B -- Delibrias, C C -- Matthews, R J -- Lin, J -- Thomas, M L -- Fearon, D T -- GM-46524/GM/NIGMS NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):242-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Wellcome Trust Immunology Unit, Department of Medicine, University of Cambridge, School of Clinical Medicine, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618087" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/*immunology/metabolism ; Antigens, Differentiation, B-Lymphocyte/*immunology/metabolism ; B-Lymphocytes/*immunology ; *Cell Adhesion Molecules ; Cells, Cultured ; Humans ; Immunoglobulin M/immunology ; Intracellular Signaling Peptides and Proteins ; *Lectins ; *Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/*metabolism ; Recombinant Proteins/metabolism ; Sialic Acid Binding Ig-like Lectin 2 ; Signal Transduction ; Tumor Cells, Cultured
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  • 85
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    Self-release of CLIP in peptide loading of HLA-DR molecules (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-24
    Description: The assembly and transport of major histocompatibility complex (MHC) class II molecules require interaction with the invariant chain. A fragment of the invariant chain, CLIP, occupies the peptide-binding groove of the class II molecule. At endosomal pH, the binding of CLIP to human MHC class II HLA-DR molecules was counteracted by its amino-terminal segment (residues 81 to 89), which facilitated rapid release. The CLIP (81-89) fragment also catalyzed the release of CLIP(90-105) and a subset of other self-peptides, probably by transient interaction with an effector site outside the groove. Thus, CLIP may facilitate peptide loading through an allosteric release mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kropshofer, H -- Vogt, A B -- Stern, L J -- Hammerling, G J -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1357-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Immunology, German Cancer Research Center, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481823" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, Differentiation, B-Lymphocyte/chemistry/*metabolism ; Binding Sites ; Cell Line ; HLA-DR3 Antigen/*metabolism ; Histocompatibility Antigens Class II/chemistry/*metabolism ; Humans ; Hydrogen-Ion Concentration ; Lysine/chemistry ; Molecular Sequence Data ; Peptide Fragments/metabolism ; Proline/chemistry ; Protein Conformation
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  • 86
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    Inhibition of transcription elongation by the VHL tumor suppressor protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: Germline mutations in the von Hippel-Lindau tumor suppressor gene (VHL) predispose individuals to a variety of tumors, including renal carcinoma, hemangioblastoma of the central nervous system, and pheochromocytoma. Here, a cellular transcription factor, Elongin (SIII), is identified as a functional target of the VHL protein. Elongin (SIII) is a heterotrimer consisting of a transcriptionally active subunit (A) and two regulatory subunits (B and C) that activate transcription elongation by RNA polymerase II. The VHL protein was shown to bind tightly and specifically to the Elongin B and C subunits and to inhibit Elongin (SIII) transcriptional activity in vitro. These findings reveal a potentially important transcriptional regulatory network in which the VHL protein may play a key role.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duan, D R -- Pause, A -- Burgess, W H -- Aso, T -- Chen, D Y -- Garrett, K P -- Conaway, R C -- Conaway, J W -- Linehan, W M -- Klausner, R D -- GM41628/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1402-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Urologic Oncology Section, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660122" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cloning, Molecular ; Gene Expression Regulation ; *Genes, Tumor Suppressor ; HeLa Cells ; Humans ; *Ligases ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/genetics/*metabolism ; RNA Polymerase II/metabolism ; Recombinant Proteins/metabolism ; Transcription Factors/chemistry/isolation & purification/*metabolism ; *Transcription, Genetic ; *Tumor Suppressor Proteins ; *Ubiquitin-Protein Ligases ; Von Hippel-Lindau Tumor Suppressor Protein ; von Hippel-Lindau Disease/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 87
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    A subclass of bHLH proteins required for cardiac morphogenesis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-22
    Description: Skeletal muscle development is controlled by a family of muscle-specific basic helix-loop-helix (bHLH) transcription factors. Two bHLH genes, dHAND and eHAND, have now been isolated that are expressed in the bilateral heart primordia and subsequently throughout the primitive tubular heart and its derivatives during chick and mouse embryogenesis. Incubation of stage 8 chick embryos with dHAND and eHAND antisense oligonucleotides revealed that either oligonucleotide alone had no effect on embryonic development, whereas together they arrested development at the looping heart tube stage. Thus, dHAND and eHAND may play redundant roles in the regulation of the morphogenetic events of vertebrate heart development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Srivastava, D -- Cserjesi, P -- Olson, E N -- New York, N.Y. -- Science. 1995 Dec 22;270(5244):1995-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Texas M. D. Anderson Cancer Center, Houston 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8533092" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Basic Helix-Loop-Helix Transcription Factors ; Cardiovascular System/embryology/metabolism ; Chick Embryo ; DNA-Binding Proteins/biosynthesis/chemistry/*genetics/physiology ; Embryonic and Fetal Development ; Gene Expression ; Heart/*embryology ; *Helix-Loop-Helix Motifs ; In Situ Hybridization ; MEF2 Transcription Factors ; Mesoderm/metabolism ; Mice ; Molecular Sequence Data ; Morphogenesis ; Myocardium/metabolism ; *Myogenic Regulatory Factors ; Oligonucleotides, Antisense/pharmacology ; Transcription Factors/biosynthesis/chemistry/*genetics/physiology ; Zebrafish Proteins
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  • 88
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    Solution structure of a bovine immunodeficiency virus Tat-TAR peptide-RNA complex (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: The Tat protein of bovine immunodeficiency virus (BIV) binds to its target RNA, TAR, and activates transcription. A 14-amino acid arginine-rich peptide corresponding to the RNA-binding domain of BIV Tat binds specifically to BIV TAR, and biochemical and in vivo experiments have identified the amino acids and nucleotides required for binding. The solution structure of the RNA-peptide complex has now been determined by nuclear magnetic resonance spectroscopy. TAR forms a virtually continuous A-form helix with two unstacked bulged nucleotides. The peptide adopts a beta-turn conformation and sits in the major groove of the RNA. Specific contacts are apparent between critical amino acids in the peptide and bases and phosphates in the RNA. The structure is consistent with all biochemical data and demonstrates ways in which proteins can recognize the major groove of RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Puglisi, J D -- Chen, L -- Blanchard, S -- Frankel, A D -- AI08591/AI/NIAID NIH HHS/ -- AI29135/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1200-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502045" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Composition ; Base Sequence ; Gene Products, tat/*chemistry/metabolism ; Hydrogen Bonding ; Immunodeficiency Virus, Bovine/*chemistry ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Conformation ; Protein Structure, Secondary ; RNA, Viral/*chemistry/metabolism
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  • 89
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    Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-03
    Description: Mammalian mitogen-activated protein (MAP) kinases include extracellular signal-regulated protein kinase (ERK), c-Jun amino-terminal kinase (JNK), and p38 subgroups. These MAP kinase isoforms are activated by dual phosphorylation on threonine and tyrosine. Two human MAP kinase kinases (MKK3 and MKK4) were cloned that phosphorylate and activate p38 MAP kinase. These MKK isoforms did not activate the ERK subgroup of MAP kinases, but MKK4 did activate JNK. These data demonstrate that the activators of p38 (MKK3 and MKK4), JNK (MKK4), and ERK (MEK1 and MEK2) define independent MAP kinase signal transduction pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Derijard, B -- Raingeaud, J -- Barrett, T -- Wu, I H -- Han, J -- Ulevitch, R J -- Davis, R J -- AI15136/AI/NIAID NIH HHS/ -- CA58396/CA/NCI NIH HHS/ -- GM37696/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 3;267(5198):682-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01605.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7839144" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cloning, Molecular ; Enzyme Activation ; Humans ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase 3 ; *MAP Kinase Kinase 4 ; Mitogen-Activated Protein Kinase 1 ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Protein-Tyrosine Kinases/chemistry/*metabolism ; *Signal Transduction ; Substrate Specificity ; Transfection ; p38 Mitogen-Activated Protein Kinases
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 90
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    A specialized pathway affecting virulence glycoconjugates of Leishmania (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-29
    Description: For virulence and transmission, the protozoan parasite Leishmania must assemble a complex glycolipid on the cell surface, the lipophosphoglycan (LPG). Functional complementation identified the gene LPG2, which encodes an integral Golgi membrane protein implicated in intracellular compartmentalization of LPG biosynthesis. Ipg2- mutants lack only characteristic disaccharide-phosphate repeats, normally present on both LPG and other surface or secreted molecules considered critical for infectivity. In contrast, a related yeast gene, VAN2/VRG4, is essential and required for general Golgi function. These results suggest that LPG2 participates in a specialized virulence pathway, which may offer an attractive target for chemotherapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Descoteaux, A -- Luo, Y -- Turco, S J -- Beverley, S M -- AI31078/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 29;269(5232):1869-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569927" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carbohydrate Sequence ; Cell Compartmentation ; Genes, Fungal ; *Genes, Protozoan ; Genetic Complementation Test ; Glycosphingolipids/*biosynthesis/chemistry/genetics/*physiology ; Glycosylation ; Golgi Apparatus/*metabolism ; Leishmania donovani/genetics/metabolism/*pathogenicity ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Protozoan Proteins/chemistry/genetics/*physiology ; Virulence/genetics ; Yeasts/genetics
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  • 91
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    Cytotoxic T lymphocyte lysis inhibited by viable HIV mutants (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-24
    Description: Immune evasion by the human immunodeficiency virus (HIV) is unexplained but may involve the mutation of viral antigens. When cytotoxic T lymphocytes engaged CD4-positive cells that were acutely infected with HIV bearing natural variant epitopes in reverse transcriptase, substantial inhibition of specific antiviral lysis was observed. Mutant viruses capable of these transactive effects could facilitate the persistence of a broad range of HIV variants in the face of an active and specific immune response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meier, U C -- Klenerman, P -- Griffin, P -- James, W -- Koppe, B -- Larder, B -- McMichael, A -- Phillips, R -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1360-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Nuffield Department of Clinical Medicine, John Radcliffe Hospital, Headington, Oxford, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481824" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigenic Variation ; Base Sequence ; CD4-Positive T-Lymphocytes/immunology/virology ; Cell Line ; *Cytotoxicity, Immunologic ; Epitopes/genetics ; HIV Antigens/genetics/*immunology ; HIV Reverse Transcriptase ; HIV-1/enzymology/genetics/*immunology ; HLA-B8 Antigen/immunology ; Humans ; *Immune Tolerance ; Molecular Sequence Data ; RNA-Directed DNA Polymerase/genetics/*immunology ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes, Cytotoxic/*immunology
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  • 92
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    First-principles calculation of the folding free energy of a three-helix bundle protein (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-21
    Description: The folding and unfolding of a three-helix bundle protein were explored with molecular-dynamics simulations, cluster analysis, and weighted-histogram techniques. The folding-unfolding process occurs by means of a "folding funnel," in which a uniform and broad distribution of conformational states is accessible outside of the native manifold. This distribution narrows near a transition region and becomes compact within the native manifold. Key thermodynamic steps in folding include initial interactions around the amino-terminal helix-turn-helix motif, interactions between helices I and II, and, finally, the docking of helix III onto the helix I-II subdomain. A metastable minimum in the calculated free-energy surface is observed at approximately 1.5 times the native volume. Folding-unfolding thermodynamics are dominated by the opposing influences of protein-solvent energy, which favors unfolding, and the overall entropy, which favors folding by means of the hydrophobic effect.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boczko, E M -- Brooks, C L 3rd -- GM48807/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):393-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618103" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Computer Graphics ; Helix-Loop-Helix Motifs ; Models, Molecular ; Molecular Sequence Data ; Peptide Fragments/*chemistry ; *Protein Folding ; *Protein Structure, Secondary ; Staphylococcal Protein A/*chemistry ; Thermodynamics
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  • 93
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    The ethylene signal transduction pathway in plants (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-05
    Description: Ethylene (C2H4), the chemically simplest plant hormone, is among the best-characterized plant growth regulators. It participates in a variety of stress responses and developmental processes. Genetic studies in Arabidopsis have defined a number of genes in the ethylene signal transduction pathway. Isolation of two of these genes has revealed that plants sense this gas through a combination of proteins that resemble both prokaryotic and eukaryotic signaling proteins. Ethylene signaling components are likely conserved for responses as diverse as cell elongation, cell fate patterning in the root epidermis, and fruit ripening. Genetic manipulation of these genes will provide agriculture with new tools to prevent or modify ethylene responses in a variety of plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ecker, J R -- New York, N.Y. -- Science. 1995 May 5;268(5211):667-75.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Pennsylvania, Philadelphia 19104-6018, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7732375" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Ethylenes ; Molecular Sequence Data ; Mutation ; Plant Development ; Plant Growth Regulators/*physiology ; *Plant Physiological Phenomena ; Plants/genetics ; Signal Transduction/*physiology
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  • 94
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    Interaction of a tyrosine kinase from human sperm with the zona pellucida at fertilization (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: A 95-kilodalton mouse sperm protein with characteristics of a protein tyrosine kinase has been identified as a receptor for ZP3, a glycoprotein in the egg's extracellular matrix. The structure of the human homolog was determined by screening an expression library from human testis; a testis-specific complementary DNA was isolated that encodes a protein similar to receptor tyrosine kinases and appears to be expressed only in testicular germ cells. Antibodies against a synthetic peptide from the intracellular domain recognized a 95-kilodalton human sperm protein that contains phosphotyrosine; human ZP3 stimulates the kinase activity of this sperm protein. Synthetic peptides corresponding to regions of the predicted extracellular domain inhibited sperm binding to human zona pellucida. Availability of the primary sequence of a receptor for ZP3 provides a rational starting point for sperm-targeted contraceptive development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burks, D J -- Carballada, R -- Moore, H D -- Saling, P M -- HD 18201/HD/NICHD NIH HHS/ -- HD 29125/HD/NICHD NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):83-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Obstetrics and Gynecology, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7541556" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Egg Proteins/*metabolism ; Female ; Humans ; Male ; Membrane Glycoproteins/*metabolism ; Mice ; Molecular Sequence Data ; Molecular Weight ; Phosphorylation ; Phosphotyrosine ; Proto-Oncogene Proteins ; Receptor Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; *Receptors, Cell Surface ; Sperm-Ovum Interactions/*physiology ; Spermatozoa/*metabolism ; Tyrosine/analogs & derivatives/metabolism ; Zona Pellucida/*metabolism
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  • 95
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    Positional cloning and sequence analysis of the Drosophila clock gene, timeless (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: The Drosophila genes timeless (tim) and period (per) interact, and both are required for production of circadian rhythms. Here the positional cloning and sequencing of tim are reported. The tim gene encodes a previously uncharacterized protein of 1389 amino acids, and possibly another protein of 1122 amino acids. The arrhythmic mutation tim01 is a 64-base pair deletion that truncates TIM to 749 amino acids. Absence of sequence similarity to the PER dimerization motif (PAS) indicates that direct interaction between PER and TIM would require a heterotypic protein association.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Myers, M P -- Wager-Smith, K -- Wesley, C S -- Young, M W -- Sehgal, A -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):805-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, National Science Foundation Science and Technology Center for Biological Timing, and Laboratory of Genetics, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481771" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Clocks/*genetics ; Chromosome Mapping ; Circadian Rhythm/*genetics ; Cloning, Molecular ; *Drosophila Proteins ; Drosophila melanogaster/chemistry/*genetics/physiology ; *Genes, Insect ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Nuclear Proteins/chemistry/genetics ; Period Circadian Proteins ; Polymorphism, Restriction Fragment Length ; Proteins/chemistry/*genetics ; Sequence Analysis ; Sequence Deletion ; Sequence Homology, Amino Acid
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  • 96
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    Expression cloning of a protective Leishmania antigen (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-04-28
    Description: Parasite-specific CD4+ T cells have been shown to transfer protection against Leishmania major in susceptible BALB/c mice. An epitope-tagged expression library was used to identify the antigen recognized by a protective CD4+ T cell clone. The expression library allowed recombinant proteins made in bacteria to be captured by macrophages for presentation to T cells restricted to major histocompatibility complex class II. A conserved 36-kilodalton member of the tryptophan-aspartic acid repeat family of proteins was identified that was expressed in both stages of the parasite life cycle. A 24-kilodalton portion of this antigen protected susceptible mice when administered as a vaccine with interleukin-12 before infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mougneau, E -- Altare, F -- Wakil, A E -- Zheng, S -- Coppola, T -- Wang, Z E -- Waldmann, R -- Locksley, R M -- Glaichenhaus, N -- AI26918/AI/NIAID NIH HHS/ -- T32 DK07007/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):563-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Pharmacologie Moleculaire et Cellulaire, UPR411 CNRS, Valbonne, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725103" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Protozoan/chemistry/genetics/*immunology ; Cloning, Molecular ; Histocompatibility Antigens Class II/immunology ; Immunodominant Epitopes ; Interleukin-12/administration & dosage ; Interleukin-4/immunology ; Leishmania major/genetics/*immunology ; Leishmaniasis, Cutaneous/*prevention & control ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Protozoan Proteins/chemistry/genetics/*immunology ; Protozoan Vaccines/immunology ; Th1 Cells/*immunology ; Vaccines, Synthetic/immunology
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  • 97
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    A role for exonuclease I from S. pombe in mutation avoidance and mismatch correction (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-24
    Description: Exonuclease I (Exo I) from Schizosaccharomyces pombe, a 5'--〉3' double-stranded DNA exonuclease, is induced during meiotic prophase I. The exo1 gene is a member of a family of related DNA repair genes, including RAD2/rad13/xpgc and YKL510/rad2, conserved from yeast to humans. An exo1 mutant displays a mutator phenotype and alters activity of the ade6-M387 marker effect. These results suggest that Exo I acts in a pathway that corrects mismatched base pairs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Szankasi, P -- Smith, G R -- GM32194/GM/NIGMS NIH HHS/ -- P30 CA15704-20/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1166-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855597" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Composition ; Base Sequence ; Crosses, Genetic ; *DNA Repair ; DNA Replication ; DNA, Fungal/*metabolism ; Exodeoxyribonucleases/chemistry/genetics/*metabolism ; Meiosis ; Molecular Sequence Data ; *Mutation ; Recombination, Genetic ; Schizosaccharomyces/enzymology/*genetics/physiology
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  • 98
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    Mutations in the dystrophin-associated protein gamma-sarcoglycan in chromosome 13 muscular dystrophy (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-03
    Description: Severe childhood autosomal recessive muscular dystrophy (SCARMD) is a progressive muscle-wasting disorder common in North Africa that segregates with microsatellite markers at chromosome 13q12. Here, it is shown that a mutation in the gene encoding the 35-kilodalton dystrophin-associated glycoprotein, gamma-sarcoglycan, is likely to be the primary genetic defect in this disorder. The human gamma-sarcoglycan gene was mapped to chromosome 13q12, and deletions that alter its reading frame were identified in three families and one of four sporadic cases of SCARMD. These mutations not only affect gamma-sarcoglycan but also disrupt the integrity of the entire sarcoglycan complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noguchi, S -- McNally, E M -- Ben Othmane, K -- Hagiwara, Y -- Mizuno, Y -- Yoshida, M -- Yamamoto, H -- Bonnemann, C G -- Gussoni, E -- Denton, P H -- Kyriakides, T -- Middleton, L -- Hentati, F -- Ben Hamida, M -- Nonaka, I -- Vance, J M -- Kunkel, L M -- Ozawa, E -- NS23740/NS/NINDS NIH HHS/ -- P01-NS26630/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 3;270(5237):819-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Neuroscience, National Center for Neurology and Psychiatry, Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481775" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Human, Pair 13 ; *Cytoskeletal Proteins ; DNA, Complementary/genetics ; Dystrophin/chemistry/genetics/metabolism ; Humans ; Linkage Disequilibrium ; Membrane Glycoproteins/chemistry/*genetics/metabolism ; Molecular Sequence Data ; Molecular Weight ; Muscle, Skeletal/chemistry/metabolism ; Muscular Dystrophies/*genetics ; Mutation ; Phenotype ; Rabbits ; Sarcoglycans ; Sequence Deletion
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 99
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    DNA topoisomerase and recombinase activities in Nae I restriction endonuclease (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-24
    Description: Nae I endonuclease must bind to two DNA sequences for cleavage. Examination of the amino acid sequence of Nae I uncovered similarity to the active site of human DNA ligase I, except for leucine 43 in Nae I instead of the lysine essential for ligase activity. Changing leucine 43 to lysine 43 (L43K) changed Nae I activity: Nae I-L43K relaxed supercoiled DNA to yield DNA topoisomers and recombined DNA to give dimeric molecules. Interruption of the reactions of Nae I and Nae I-L43K with DNA demonstrated transient protein-DNA covalent complexes. These findings imply coupled endonuclease and ligase domains and link Nae I endonuclease to the topoisomerase and recombinase protein families.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jo, K -- Topal, M D -- New York, N.Y. -- Science. 1995 Mar 24;267(5205):1817-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, University of North Carolina Medical School, Chapel Hill 27599.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7892605" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; DNA Nucleotidyltransferases/*metabolism ; DNA Topoisomerases, Type I/*metabolism ; DNA, Circular/metabolism ; Deoxyribonucleases, Type II Site-Specific/chemistry/*metabolism ; *Integrases ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Recombinases ; Sequence Homology, Amino Acid
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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    Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major HIV-suppressive factors produced by CD8+ T cells (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-12-15
    Description: Evidence suggests that CD8+ T lymphocytes are involved in the control of human immunodeficiency virus (HIV) infection in vivo, either by cytolytic mechanisms or by the release of HIV-suppressive factors (HIV-SF). The chemokines RANTES, MIP-1 alpha, and MIP-1 beta were identified as the major HIV-SF produced by CD8+ T cells. Two active proteins purified from the culture supernatant of an immortalized CD8+ T cell clone revealed sequence identity with human RANTES and MIP-1 alpha. RANTES, MIP-1 alpha, and MIP-1 beta were released by both immortalized and primary CD8+ T cells. HIV-SF activity produced by these cells was completely blocked by a combination of neutralizing antibodies against RANTES, MIP-1 alpha, and MIP-1 beta. Recombinant human RANTES, MIP-1 alpha, and MIP-1 beta induced a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). These data may have relevance for the prevention and therapy of AIDS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cocchi, F -- DeVico, A L -- Garzino-Demo, A -- Arya, S K -- Gallo, R C -- Lusso, P -- New York, N.Y. -- Science. 1995 Dec 15;270(5243):1811-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Tumor Cell Biology, National Cancer Institute, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8525373" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Amino Acid Sequence ; Animals ; Antiviral Agents/*physiology ; CD8-Positive T-Lymphocytes/*immunology ; Cell Division/physiology ; Cell Line ; Cells, Cultured ; Chemokine CCL4 ; Chemokine CCL5/antagonists & inhibitors/*immunology ; Culture Media, Conditioned ; Cytokines/antagonists & inhibitors/*immunology ; Dose-Response Relationship, Immunologic ; Escherichia coli ; HIV Infections/immunology ; HIV-1/*immunology ; HIV-2/immunology ; Herpesvirus 6, Human/immunology ; Herpesvirus 7, Human/immunology ; Human T-lymphotropic virus 1/immunology ; Humans ; Immunoglobulin G/immunology ; Lymphocyte Activation ; Macaca nemestrina ; Macrophage Inflammatory Proteins ; Molecular Sequence Data ; Monokines/antagonists & inhibitors/*immunology ; Recombinant Proteins/immunology ; Simian Immunodeficiency Virus/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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