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  • Amino Acid Sequence  (181)
  • Male  (145)
  • American Association for the Advancement of Science (AAAS)  (304)
  • MDPI Publishing
  • PANGAEA
  • 1995-1999  (304)
  • 1995  (304)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (304)
  • MDPI Publishing
  • PANGAEA
Years
  • 1995-1999  (304)
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
    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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  • 2
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    FFA-1, a protein that promotes the formation of replication centers within nuclei (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-29
    Description: In the nuclei of eukaryotic cells, initiation of DNA replication occurs at a discrete number of foci. One component of these foci is the DNA replication factor RP-A. Here, the process leading to the association of RP-A with foci was reconstituted with cytosolic fractions derived from Xenopus eggs. With the use of this fractionated system, a 170-kilodalton protein required for the assembly of RP-A into foci was identified and purified. The protein appears to be an integral component of the foci at which replication of DNA is initiated in eukaryotic nuclei.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, H -- Newport, J -- GM33523/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1995 Sep 29;269(5232):1883-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, San Diego, Department of Biology, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569932" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/*metabolism ; Cell-Free System ; Cytosol/chemistry ; *DNA Replication ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/*metabolism ; Female ; Male ; Molecular Weight ; Oocytes ; Orientation ; Proteins/chemistry/*metabolism ; Replication Protein A ; Xenopus
    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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  • 3
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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
    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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  • 4
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    Dissociation of synchronization and excitability in furosemide blockade of epileptiform activity (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-06
    Description: Furosemide, a chloride cotransport inhibitor, reversibly blocked synchronized burst discharges in hippocampal slices without reducing the pyramidal cell response to single electrical stimuli. Images of the intrinsic optical signal acquired during these slice experiments indicated that furosemide coincidentally blocked changes in extracellular space. In urethane-anesthetized rats, systemically injected furosemide blocked kainic acid-induced electrical discharges recorded from cortex. These results suggest that (i) neuronal synchronization involved in epileptiform activity can be dissociated from synaptic excitability; (ii) nonsynaptic mechanisms, possibly associated with furosemide-sensitive cell volume regulation, may be critical for synchronization of neuronal activity; and (iii) agents that affect extracellular volume may have clinical utility as antiepileptic drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hochman, D W -- Baraban, S C -- Owens, J W -- Schwartzkroin, P A -- NS07144/NS/NINDS NIH HHS/ -- NS15317/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Oct 6;270(5233):99-102.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurological Surgery, University of Washington, Seattle 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569957" target="_blank"〉PubMed〈/a〉
    Keywords: 4-Aminopyridine/pharmacology ; Animals ; Anticonvulsants/*pharmacology ; Bicuculline/pharmacology ; Electric Stimulation ; Entorhinal Cortex/physiology ; Extracellular Space/drug effects/physiology ; Female ; Furosemide/*pharmacology ; Hippocampus/drug effects/*physiology ; In Vitro Techniques ; Kainic Acid/pharmacology ; Magnesium/pharmacology ; Male ; Membrane Potentials/drug effects ; Potassium/pharmacology ; Pyramidal Cells/drug effects/*physiology ; Rats ; Rats, Sprague-Dawley ; Status Epilepticus/chemically induced/*physiopathology ; Synaptic Transmission/drug effects
    Print ISSN: 0036-8075
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  • 5
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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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  • 6
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    Requirement of FGF-4 for postimplantation mouse development (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-13
    Description: Fibroblast growth factors (FGFs) are thought to influence many processes in vertebrate development because of their diverse sites of expression and wide range of biological activities in in vitro culture systems. As a means of elucidating embryonic functions of FGF-4, gene targeting was used to generate mice harboring a disrupted Fgf4 gene. Embryos homozygous for the null allele underwent uterine implantation and induced uterine decidualization but did not develop substantially thereafter. As was consistent with their behavior in vivo, Fgf4 null embryos cultured in vitro displayed severely impaired proliferation of the inner cell mass, whereas growth and differentiation of the inner cell mass were rescued when null embryos were cultured in the presence of FGF-4 protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feldman, B -- Poueymirou, W -- Papaioannou, V E -- DeChiara, T M -- Goldfarb, M -- HD21988/HD/NICHD NIH HHS/ -- HD27198/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 Jan 13;267(5195):246-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Integrated Program in Cellular, Molecular, and Biophysical Studies, Columbia University College of Physicians and Surgeons, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809630" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blastocyst/cytology/physiology ; Crosses, Genetic ; Culture Techniques ; Embryonic Development/*physiology ; Embryonic and Fetal Development/*physiology ; Female ; Fibroblast Growth Factor 4 ; Fibroblast Growth Factors/genetics/pharmacology/*physiology ; Gene Targeting ; Heterozygote ; Male ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Morula/drug effects/physiology ; Phenotype ; Pregnancy ; Proto-Oncogene Proteins/genetics/pharmacology/*physiology ; Recombinant Proteins/pharmacology
    Print ISSN: 0036-8075
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  • 7
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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
    Print ISSN: 0036-8075
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  • 8
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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
    Print ISSN: 0036-8075
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  • 9
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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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  • 10
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    The complexities of conception (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aitken, R J -- New York, N.Y. -- Science. 1995 Jul 7;269(5220):39-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Reproductive Biology Unit, Medical Research Council, Edinburgh, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604276" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Egg Proteins/*metabolism ; Female ; Humans ; Lectins/metabolism ; Male ; Membrane Glycoproteins/*metabolism ; Mice ; Phosphorylation ; Proto-Oncogene Proteins ; Receptor Protein-Tyrosine Kinases/*metabolism ; Receptors, Cell Surface/*metabolism ; Sperm-Ovum Interactions/*physiology ; Spermatozoa/metabolism ; Zona Pellucida/*metabolism
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  • 11
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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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  • 12
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    Translational suppression by trinucleotide repeat expansion at FMR1 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-05
    Description: Fragile X syndrome is the result of the unstable expansion of a trinucleotide repeat in the 5'-untranslated region of the FMR1 gene. Fibroblast subclones from a mildly affected patient, each containing stable FMR1 alleles with 57 to 285 CGG repeats, were shown to exhibit normal steady-state levels of FMR1 messenger RNA. However, FMR protein was markedly diminished from transcript with more than 200 repeats. Such transcripts were associated with stalled 40S ribosomal subunits. These results suggest that a structural RNA transition beyond 200 repeats impedes the linear 40S migration along the 5'-untranslated region. This results in translational inhibition by trinucleotide repeat expansion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, Y -- Zhang, F -- Lokey, L K -- Chastain, J L -- Lakkis, L -- Eberhart, D -- Warren, S T -- HD20521/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1995 May 5;268(5211):731-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7732383" target="_blank"〉PubMed〈/a〉
    Keywords: Centrifugation, Density Gradient ; Clone Cells ; Down-Regulation/genetics ; Female ; Fibroblasts/chemistry ; Fragile X Mental Retardation Protein ; Fragile X Syndrome/*genetics ; Humans ; Infant ; Male ; Nerve Tissue Proteins/*genetics ; Polymerase Chain Reaction ; Protein Biosynthesis/*genetics ; RNA, Messenger/analysis ; *RNA-Binding Proteins ; Repetitive Sequences, Nucleic Acid/*genetics
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  • 13
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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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  • 14
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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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    Immune system impairment and hepatic fibrosis in mice lacking the dioxin-binding Ah receptor (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-05-05
    Description: The aryl hydrocarbon (Ah) receptor (AHR) mediates many carcinogenic and teratogenic effects of environmentally toxic chemicals such as dioxin. An AHR-deficient (Ahr-/-) mouse line was constructed by homologous recombination in embryonic stem cells. Almost half of the mice died shortly after birth, whereas survivors reached maturity and were fertile. The Ahr-/- mice showed decreased accumulation of lymphocytes in the spleen and lymph nodes, but not in the thymus. The livers of Ahr-/- mice were reduced in size by 50 percent and showed bile duct fibrosis Ahr-/- mice were also nonresponsive with regard to dioxin-mediated induction of genes encoding enzymes that catalyze the metabolism of foreign compounds. Thus, the AHR plays an important role in the development of the liver and the immune system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez-Salguero, P -- Pineau, T -- Hilbert, D M -- McPhail, T -- Lee, S S -- Kimura, S -- Nebert, D W -- Rudikoff, S -- Ward, J M -- Gonzalez, F J -- P30 ES06096/ES/NIEHS NIH HHS/ -- R01 ES06811/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1995 May 5;268(5211):722-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Carcinogenesis, 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/7732381" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Female ; Gene Expression Regulation/physiology ; Immunity/*physiology ; Liver/*physiology ; Liver Cirrhosis, Experimental/genetics/pathology ; Lymphoid Tissue/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Receptors, Aryl Hydrocarbon/genetics/*physiology
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  • 16
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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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  • 17
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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)
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    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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  • 18
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    Global approaches to the promotion of women's health (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mongella, G -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):789-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fourth World Conference on Women, United Nations, New York, NY 10017, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638591" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/epidemiology/transmission ; Aging ; Biomedical Research ; Female ; *Global Health ; Health Promotion ; Humans ; *Internationality ; Life Expectancy ; Male ; Neoplasms/epidemiology ; Poverty ; Research ; Research Support as Topic ; Resource Allocation ; Sex Characteristics ; Violence ; *Women's Health ; Women's Health Services ; World Health Organization
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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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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  • 20
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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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  • 21
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    Genetic feminization of brain structures and changed sexual orientation in male Drosophila (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-10
    Description: The neural basis of sexual orientation in Drosophila was studied by the production of males with regionally feminized brains. Such flies express the female form of the sex determination gene transformer in a limited number of neurons under the control of GAL4 enhancer trap inserts. This method facilitated the creation of lines with a stable pattern of feminization. In tests of sexual preferences, flies that were feminized in a portion of the antennal lobes or in a subset of the corpora pedunculata (mushroom bodies) courted both males and females. These two brain structures, both of which are involved in olfactory processing, may function in the recognition of sex-specific pheromones, in the control of sex-specific behaviors, or both.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferveur, J F -- Stortkuhl, K F -- Stocker, R F -- Greenspan, R J -- New York, N.Y. -- Science. 1995 Feb 10;267(5199):902-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, New York University, NY 10003.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7846534" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bisexuality ; Brain/physiology ; Drosophila melanogaster/genetics/*physiology ; Female ; *Genes, Insect ; Male ; Sex Attractants/physiology ; Sexual Behavior, Animal ; Smell
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  • 22
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    Ethylene insensitivity conferred by Arabidopsis ERS gene (1995)
    American Association for the Advancement of Science (AAAS)
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    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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  • 23
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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)
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    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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  • 24
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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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  • 25
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    Attacking the causes of "silent" infertility (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):775-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638588" target="_blank"〉PubMed〈/a〉
    Keywords: Adolescent ; Adult ; Chlamydia Infections/complications/immunology ; Endometriosis/*complications/genetics ; Female ; Genetic Predisposition to Disease ; Humans ; Infertility, Female/*etiology/genetics ; Infertility, Male/etiology ; Leiomyoma/*complications/genetics ; Male ; Sexually Transmitted Diseases/*complications/epidemiology/immunology ; Uterine Neoplasms/*complications/genetics
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  • 26
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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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    PER protein interactions and temperature compensation of a circadian clock in Drosophila (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 28
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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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  • 29
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    Mutations of keratinocyte transglutaminase in lamellar ichthyosis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-27
    Description: Lamellar ichthyosis is a severe congenital skin disorder characterized by generalized large scales and variable redness. Affected individuals in three families exhibited drastically reduced keratinocyte transglutaminase (TGK) activity. In two of these families, expression of TGK transcripts was diminished or abnormal and no TGK protein was detected. Homozygous or compound heterozygous mutations of the TGK gene were identified in all families. These data suggest that defects in TGK cause lamellar ichthyosis and that intact cross-linkage of cornified cell envelopes is required for epidermal tissue homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, M -- Rettler, I -- Bernasconi, K -- Frenk, E -- Lavrijsen, S P -- Ponec, M -- Bon, A -- Lautenschlager, S -- Schorderet, D F -- Hohl, D -- New York, N.Y. -- Science. 1995 Jan 27;267(5197):525-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Dermatology, Centre Hospitalier Universitaire Vandois (CHUV), Hopital de Beaumont, Lausanne, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824952" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Membrane/metabolism ; Cells, Cultured ; Codon ; Female ; Gene Deletion ; Genetic Linkage ; Heterozygote ; Homozygote ; Humans ; Ichthyosis, Lamellar/enzymology/*genetics ; Introns ; Keratinocytes/*enzymology/ultrastructure ; Male ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Mutation ; Pedigree ; Point Mutation ; Protein Precursors/metabolism ; Transglutaminases/*genetics/metabolism
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    Zeroing in on how hormones affect the immune system (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):773-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638587" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoimmune Diseases/etiology ; Clinical Trials as Topic ; Estrogens/*physiology ; Female ; Genetic Predisposition to Disease ; Genitalia, Female/physiology ; Gonadal Steroid Hormones/*physiology ; Humans ; Immune System/*physiology ; Infection/immunology ; Male ; Menopause ; *Menstrual Cycle
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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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    Unraveling immune privilege (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Streilein, J W -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1158-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Schepens Eye Research Institute, Harvard Medical School, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502038" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anterior Chamber/immunology ; Fas Ligand Protein ; Graft Rejection ; Graft Survival ; *Immune Tolerance ; Male ; Membrane Glycoproteins/*physiology ; Mice ; Mice, Inbred Strains ; Sertoli Cells/immunology ; T-Lymphocytes/immunology ; *Transplantation Immunology
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    Aggression in mice and men? (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rose, S P -- New York, N.Y. -- Science. 1995 Oct 20;270(5235):362-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569986" target="_blank"〉PubMed〈/a〉
    Keywords: *Aggression ; Animals ; *Behavior, Animal ; Humans ; Male ; Mice ; Mice, Transgenic ; Monoamine Oxidase/*deficiency/genetics
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    U.S.-Russian space science. Joint mission gets off to slow start (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-01-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lawler, A -- New York, N.Y. -- Science. 1995 Jan 20;267(5196):323.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824926" target="_blank"〉PubMed〈/a〉
    Keywords: *Astronauts ; Humans ; International Cooperation ; Male ; Russia ; *Space Flight ; *Spacecraft ; United States
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  • 35
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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)
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    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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    Scope of the AIDS epidemic in the United States (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-24
    Description: Two-dimensional deconvolution techniques are used here to reconstruct age-specific human immunodeficiency virus (HIV) infection rates in the United States from surveillance data on acquired immunodeficiency syndrome (AIDS). This approach suggests that 630,000 to 897,000 adults and adolescents in the United States were living with HIV infection as of January 1993, including 107,000 to 150,000 women. The estimated incidence of HIV infection declined markedly over time among white males, especially those older than 30 years. In contrast, HIV incidence appears to have remained relatively constant among women and minorities. As of January 1993, prevalence was highest among young adults in their late twenties and thirties and among minorities. An estimated 3 percent of black men and 1 percent of black women in their thirties were living with HIV infection as of that date. If infection rates remain at these levels, HIV must be considered as endemic in the United States.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rosenberg, P S -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1372-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Cancer Institute, Rockville, MD 20852-4910, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481828" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/*epidemiology ; Adolescent ; Adult ; African Americans/statistics & numerical data ; Age Distribution ; *Disease Outbreaks ; European Continental Ancestry Group/statistics & numerical data ; Female ; HIV Infections/*epidemiology ; Hispanic Americans/statistics & numerical data ; Humans ; Incidence ; Male ; Middle Aged ; Models, Statistical ; Prevalence ; Sex Distribution ; United States/epidemiology
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    Anthropologists overturn old ideas about new developments (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fischman, J -- Gibbons, A -- Culotta, E -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):364-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716536" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Anthropology ; Behavior ; Female ; Fossils ; Genetic Variation ; Haplorhini/physiology ; Hominidae/anatomy & histology ; Humans ; Humerus/anatomy & histology ; Labor, Obstetric ; Male ; Melanesia ; Pregnancy
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    Primate genetics. Getting the poop on baboon DNA (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1995 Feb 3;267(5198):615-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7839135" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/analysis/*genetics ; DNA Primers ; DNA, Satellite ; Feces/*chemistry ; Male ; Papio/*genetics ; Polymerase Chain Reaction ; Sequence Analysis, DNA
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    Possible exceptions to rules for alpha-helix termination by glycine (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Herpes-like sequences in HIV-infected and uninfected Kaposi's sarcoma patients (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-04-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ambroziak, J A -- Blackbourn, D J -- Herndier, B G -- Glogau, R G -- Gullett, J H -- McDonald, A R -- Lennette, E T -- Levy, J A -- New York, N.Y. -- Science. 1995 Apr 28;268(5210):582-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7725108" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocyte Subsets/virology ; DNA, Viral/*analysis ; HIV Infections/*complications ; Herpesviridae/*genetics ; Humans ; Leukocytes, Mononuclear/virology ; Male ; Saliva/virology ; Sarcoma, Kaposi/etiology/*virology ; Semen/virology ; Tumor Cells, Cultured
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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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  • 42
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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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    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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    A simple genetic basis for a complex psychological trait in laboratory mice (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: Psychological traits are commonly inferred from covariation in sets of behavioral measures that otherwise appear to have little in common. Emotionality in mice is such a trait, defined here by covariation in activity and defecation in a novel environment and emergence into the open arms of an elevated plus maze. Behavioral and quantitative trait analyses were conducted on four measures obtained from 879 mice from an F2 intercross. Three loci, on murine chromosomes 1, 12, and 15, were mapped that influence emotionality. This trait, inferred from studies of strain, sex, and individual differences in rodents, may be related to human susceptibility to anxiety or neuroticism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flint, J -- Corley, R -- DeFries, J C -- Fulker, D W -- Gray, J A -- Miller, S -- Collins, A C -- DA-00197/DA/NIDA NIH HHS/ -- DA-05131/DA/NIDA NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1432-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660127" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior, Animal ; *Chromosome Mapping ; Defecation ; *Emotions ; Female ; Genes ; *Genetic Linkage ; Genetic Variation ; Lod Score ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Phenotype ; Regression Analysis
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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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    Arguing over why Johnny can't read (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1896-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701312" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Child ; Chromosomes, Human, Pair 6 ; Dyslexia/diagnosis/epidemiology/*etiology ; Female ; Humans ; Learning Disorders/diagnosis/epidemiology/*etiology ; Magnetic Resonance Imaging ; Male ; National Institutes of Health (U.S.) ; Thalamus/*pathology/physiopathology/*radionuclide imaging ; Tomography, Emission-Computed ; United States/epidemiology
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    A role for CD5 in TCR-mediated signal transduction and thymocyte selection (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-28
    Description: CD5 is a transmembrane protein that is expressed on the surface of T cells and a subset of B cells. The absence of CD5 rendered thymocytes hyperresponsive to stimulation through the T cell antigen receptor (TCR) in vitro. Selection of T cells expressing three distinct transgenic TCRs was also abnormal in CD5-deficient mice. These observations indicate that CD5 can influence the fate of developing thymocytes by acting as a negative regulator of TCR-mediated signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tarakhovsky, A -- Kanner, S B -- Hombach, J -- Ledbetter, J A -- Muller, W -- Killeen, N -- Rajewsky, K -- New York, N.Y. -- Science. 1995 Jul 28;269(5223):535-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542801" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/*immunology ; Antigens, CD3/metabolism ; Antigens, CD5 ; Female ; *Lymphocyte Activation ; Male ; Mice ; Mice, Transgenic ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Receptors, Antigen, T-Cell/*immunology ; *Signal Transduction ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes/*immunology ; Thymus Gland/immunology ; ZAP-70 Protein-Tyrosine Kinase
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    "The Duesberg phenomenon": Duesberg and other voices (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cline, F A Jr -- New York, N.Y. -- Science. 1995 Jan 20;267(5196):314-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7824921" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/drug therapy/*virology ; HIV/pathogenicity ; Homosexuality, Male ; Humans ; Male ; Research ; Zidovudine/*therapeutic use
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    AIDS-associated Kaposi's sarcoma. "Duesberg phenomenon' (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ascher, M S -- Sheppard, H W -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7726989" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/chemically induced/*etiology ; Humans ; Male ; Street Drugs/*adverse effects ; Zidovudine/adverse effects/therapeutic use
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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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    Selective opioid inhibition of small nociceptive neurons (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-11-24
    Description: Opioid analgesia, the selective suppression of pain without effects on other sensations, also distinguishes between different types of pain: severe, persistent pain is potently inhibited by opioids, but they fail to cohceal the sensation of a pinprick. The cellular basis for this specificity was analyzed by means of patch-clamp experiments performed on fluorescently labeled nociceptive neurons (nociceptors) that innervate rat tooth pulp. Activation of the mu opioid receptor inhibited calcium channels on almost all small nociceptors but had minimal effect on large nociceptors. Somatostatin had the opposite specificity, preferentially inhibiting calcium channels on the large cells. Because persistent pain is mediated by slow-conducting, small nociceptors, opioids are thus likely to inhibit neurotransmitter release only at those primary synapses specialized for persistent pain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Taddese, A -- Nah, S Y -- McCleskey, E W -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1366-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481826" target="_blank"〉PubMed〈/a〉
    Keywords: Analgesics/*pharmacology ; Animals ; Calcium Channels/drug effects ; Cells, Cultured ; Dental Pulp/innervation ; Enkephalin, Ala(2)-MePhe(4)-Gly(5)- ; Enkephalins/*pharmacology ; Male ; Neurons, Afferent/*drug effects/physiology ; Neurotransmitter Agents/metabolism ; Nociceptors/*drug effects/physiology ; Patch-Clamp Techniques ; Presynaptic Terminals/drug effects/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Opioid, mu/*physiology ; Receptors, Somatostatin/physiology ; Sodium Channel Blockers ; Somatostatin/pharmacology
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    A morbillivirus that caused fatal disease in horses and humans (1995)
    American Association for the Advancement of Science (AAAS)
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    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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    T cell awareness of paternal alloantigens during pregnancy (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-27
    Description: During pregnancy a semiallogeneic fetus survives despite the presence of maternal T cells specific for paternally inherited histocompatibility antigens. A mouse transgenic for a T cell receptor recognizing the major histocompatibility (MHC) antigen H-2Kb was used to follow the fate of T cells reactive to paternal alloantigens. In contrast to syngeneic and third-party allogeneic pregnancies, mice bearing a Kb-positive conceptus had reduced numbers of Kb-reactive T cells and accepted Kb-positive tumor grafts. T cell phenotype and responsiveness were restored after delivery. Thus, during pregnancy maternal T cells acquire a transient state of tolerance specific for paternal alloantigens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tafuri, A -- Alferink, J -- Moller, P -- Hammerling, G J -- Arnold, B -- New York, N.Y. -- Science. 1995 Oct 27;270(5236):630-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tumor Immunology Program, Deutsches Krebsforschungszentrum (DKFZ), Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7570020" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CD4-Positive T-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/immunology ; Fathers ; Female ; Fetus/*immunology ; Graft Rejection ; H-2 Antigens/*immunology ; *Immune Tolerance ; Male ; Mice ; Mice, Inbred C57BL ; Mice, SCID ; Mice, Transgenic ; Neoplasm Transplantation ; Phenotype ; Placenta/immunology ; Pregnancy ; Pregnancy, Animal/*immunology ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/*immunology
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    Thailand weighs AIDS vaccine tests (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):904-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481784" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines/immunology ; Acquired Immunodeficiency Syndrome/*prevention & control ; Animals ; *Clinical Trials as Topic/economics ; Cohort Studies ; Costs and Cost Analysis ; Female ; HIV/classification ; HIV Antibodies/biosynthesis ; *HIV Envelope Protein gp120/immunology ; HIV Infections/*prevention & control ; Humans ; International Cooperation ; Male ; Pan troglodytes ; Patient Selection ; Thailand ; United States
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    AIDS-associated Kaposi's sarcoma (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, J L -- Hanson, D L -- Chu, S Y -- Ward, J W -- Jaffe, H W -- New York, N.Y. -- Science. 1995 Feb 24;267(5201):1078-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7855583" target="_blank"〉PubMed〈/a〉
    Keywords: AIDS-Related Opportunistic Infections/drug therapy/virology ; Acquired Immunodeficiency Syndrome/*complications/drug therapy ; Acyclovir/therapeutic use ; Female ; Foscarnet/*therapeutic use ; Ganciclovir/therapeutic use ; Herpesviridae Infections/drug therapy/virology ; Humans ; Male ; Retrospective Studies ; Risk Factors ; Sarcoma, Kaposi/*complications/drug therapy/virology
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    Differences in HIV strains may underlie disease patterns (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-10-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1995 Oct 6;270(5233):30-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7569947" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Developed Countries ; Developing Countries ; Female ; HIV Infections/epidemiology/transmission/*virology ; HIV-1/classification/growth & development/*pathogenicity ; Humans ; Langerhans Cells/*virology ; Male ; Thailand/epidemiology ; Vagina/virology
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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)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Neurobiology. Brain center linked to perfect pitch (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-02-03
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, R -- New York, N.Y. -- Science. 1995 Feb 3;267(5198):616.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7839136" target="_blank"〉PubMed〈/a〉
    Keywords: Female ; *Functional Laterality ; Humans ; Magnetic Resonance Imaging ; Male ; *Music ; *Pitch Discrimination ; Temporal Lobe/*anatomy & histology
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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)
    Details
    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)
    Details
    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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    Women in clinical trials: an FDA perspective (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sherman, L A -- Temple, R -- Merkatz, R B -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):793-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Drug Evaluation and Research, FDA, Rockville, MD 20857, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638593" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; *Clinical Trials as Topic ; Drug Approval ; Federal Government ; Female ; *Guidelines as Topic ; Humans ; Male ; Paternalism ; *Patient Selection ; Pregnant Women ; Research Design ; *Research Subjects ; Sex Characteristics ; United States ; *United States Food and Drug Administration
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    Steroid hormone--and neurotransmitter-induced rat sexual behavior: addendum (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mani, S K -- Allen, J M -- Clark, J H -- Blaustein, J D -- O'Malley, B W -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1833.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604251" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Estradiol/*pharmacology ; Female ; Male ; Neurotransmitter Agents/*physiology ; Rats ; Sexual Behavior, Animal/drug effects/*physiology
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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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    Women's health research blossoms (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mann, C -- New York, N.Y. -- Science. 1995 Aug 11;269(5225):766-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638586" target="_blank"〉PubMed〈/a〉
    Keywords: *Biomedical Research ; Clinical Trials as Topic ; Cultural Characteristics ; Developing Countries ; Female ; Humans ; *Internationality ; Male ; Maternal Health Services ; *Patient Selection ; Poverty ; *Research ; Research Design ; *Research Subjects ; Resource Allocation ; Sex Characteristics ; *Women's Health
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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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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  • 72
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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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  • 73
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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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  • 74
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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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  • 75
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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)
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    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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  • 77
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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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    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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    Inducible gene targeting in mice (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-09-08
    Description: A method of gene targeting that allows the inducible inactivation of a target gene in mice is presented. The method uses an interferon-responsive promoter to control the expression of Cre recombinase. Here, Cre was used to delete a segment of the DNA polymerase beta gene flanked by IoxP recombinase recognition sites. Deletion was complete in liver and nearly complete in lymphocytes within a few days, whereas partial deletion was obtained in other tissues. This method can be used for the inducible inactivation of any other gene in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhn, R -- Schwenk, F -- Aguet, M -- Rajewsky, K -- New York, N.Y. -- Science. 1995 Sep 8;269(5229):1427-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7660125" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Crosses, Genetic ; DNA Nucleotidyltransferases/genetics ; DNA Polymerase I/genetics ; Female ; *GTP-Binding Proteins ; Gene Targeting/*methods ; Genetic Vectors ; *Integrases ; Interferon-alpha/pharmacology ; Interferon-beta/pharmacology ; Liver/drug effects/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Inbred CBA ; Mice, Transgenic ; Myxovirus Resistance Proteins ; Poly I-C/pharmacology ; Promoter Regions, Genetic ; Proteins/genetics ; Recombination, Genetic ; Sequence Deletion ; *Viral Proteins
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    Evolution made visible (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiner, J -- New York, N.Y. -- Science. 1995 Jan 6;267(5194):30-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7809606" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Birds ; Female ; Fishes ; Genetic Variation ; Male ; Reproduction ; Reproduction, Asexual ; *Selection, Genetic
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  • 81
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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)
    Details
    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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  • 82
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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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  • 83
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    Patterns of human growth (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heinrichs, C -- Munson, P J -- Counts, D R -- Cutler, G B Jr -- Baron, J -- New York, N.Y. -- Science. 1995 Apr 21;268(5209):442-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716552" target="_blank"〉PubMed〈/a〉
    Keywords: Body Height ; Body Weight ; Cephalometry ; Female ; *Growth ; Humans ; Infant ; Kinetics ; Male ; Regression Analysis
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  • 84
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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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  • 85
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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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  • 86
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    Common virulence factors for bacterial pathogenicity in plants and animals (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-06-30
    Description: A Pseudomonas aeruginosa strain (UCBPP-PA14) is infectious both in an Arabidopsis thaliana leaf infiltration model and in a mouse full-thickness skin burn model. UCBPP-PA14 exhibits ecotype specificity for Arabidopsis, causing a range of symptoms from none to severe in four different ecotypes. In the mouse model, UCBPP-PA14 is as lethal as other well-studied P. aeruginosa strains. Mutations in the UCBPP-PA14 toxA, plcS, and gacA genes resulted in a significant reduction in pathogenicity in both hosts, indicating that these genes encode virulence factors required for the full expression of pathogenicity in both plants and animals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rahme, L G -- Stevens, E J -- Wolfort, S F -- Shao, J -- Tompkins, R G -- Ausubel, F M -- New York, N.Y. -- Science. 1995 Jun 30;268(5219):1899-902.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7604262" target="_blank"〉PubMed〈/a〉
    Keywords: *ADP Ribose Transferases ; Animals ; Arabidopsis/*microbiology ; Bacterial Proteins/genetics ; *Bacterial Toxins ; Base Sequence ; Burns/complications ; Exotoxins/genetics ; Male ; Mice ; Molecular Sequence Data ; Mutation ; Phospholipases/genetics ; Plant Diseases/*microbiology ; Pseudomonas Infections/*microbiology ; Pseudomonas aeruginosa/genetics/growth & development/*pathogenicity ; Virulence/genetics ; *Virulence Factors
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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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    Getting a grip on G protein function in C. elegans (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1596-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7886445" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal ; Caenorhabditis elegans/genetics/*physiology ; GTP-Binding Proteins/genetics/*physiology ; Genes, Helminth ; Male ; Mutation ; *Signal Transduction
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  • 88
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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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  • 89
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    Inactivation of the mouse Huntington's disease gene homolog Hdh (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-07-21
    Description: Huntington's disease (HD) is a dominant neurodegenerative disorder caused by expansion of a CAG repeat in the gene encoding huntingtin, a protein of unknown function. To distinguish between "loss of function" and "gain of function" models of HD, the murine HD homolog Hdh was inactivated by gene targeting. Mice heterozygous for Hdh inactivation were phenotypically normal, whereas homozygosity resulted in embryonic death. Homozygotes displayed abnormal gastrulation at embryonic day 7.5 and were resorbing by day 8.5. Thus, huntingtin is critical early in embryonic development, before the emergence of the nervous system. That Hdh inactivation does not mimic adult HD neuropathology suggests that the human disease involves a gain of function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duyao, M P -- Auerbach, A B -- Ryan, A -- Persichetti, F -- Barnes, G T -- McNeil, S M -- Ge, P -- Vonsattel, J P -- Gusella, J F -- Joyner, A L -- NS16367/NS/NINDS NIH HHS/ -- NS32765/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1995 Jul 21;269(5222):407-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Neurogenetics Unit, Massachusetts General Hospital, Charlestown 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7618107" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Line ; Ectoderm/cytology ; Embryonic and Fetal Development ; Female ; Gene Targeting ; Genotype ; Heterozygote ; Homozygote ; Humans ; Huntington Disease/*genetics ; Male ; Mesoderm/cytology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Nerve Tissue Proteins/*genetics/physiology ; Nuclear Proteins/*genetics/physiology ; Phenotype ; Stem Cells/metabolism
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  • 90
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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)
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    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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  • 91
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    Detecting Alzheimer's disease (1995)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1995-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- Kumar, S R -- Thach, A B -- Kiat-Winarko, T -- Frambach, D A -- New York, N.Y. -- Science. 1995 Mar 17;267(5204):1577; author reply 1580-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7741897" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Alzheimer Disease/*diagnosis ; Female ; Humans ; Male ; Pupil/*drug effects ; *Tropicamide
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  • 92
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    Attenuated retrovirus vaccines and AIDS (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, P A -- New York, N.Y. -- Science. 1995 Nov 17;270(5239):1219-20; author reply 1220-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7502054" target="_blank"〉PubMed〈/a〉
    Keywords: *AIDS Vaccines ; Animals ; Animals, Newborn ; Female ; HIV Infections/*prevention & control/transmission ; Humans ; Macaca mulatta ; Male ; Simian Immunodeficiency Virus/pathogenicity ; Vaccination ; Vaccines, Attenuated
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  • 93
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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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  • 94
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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)
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    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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  • 95
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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)
    Details
    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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  • 96
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    Rescue of the En-1 mutant phenotype by replacement of En-1 with En-2 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-04
    Description: The related mouse Engrailed genes En-1 and En-2 are expressed from the one- and approximately five-somite stages, respectively, in a similar presumptive mid-hindbrain domain. However, mutations in En-1 and En-2 produce different phenotypes. En-1 mutant mice die at birth with a large mid-hindbrain deletion, whereas En-2 mutants are viable, with cerebellar defects. To determine whether these contrasting phenotypes reflect differences in temporal expression or biochemical activity of the En proteins, En-1 coding sequences were replaced with En-2 sequences by gene targeting. This rescued all En-1 mutant defects, demonstrating that the difference between En-1 and En-2 stems from their divergent expression patterns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanks, M -- Wurst, W -- Anson-Cartwright, L -- Auerbach, A B -- Joyner, A L -- New York, N.Y. -- Science. 1995 Aug 4;269(5224):679-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mt. Sinai Hospital, Toronto, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7624797" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/abnormalities/embryology ; Chimera ; Crosses, Genetic ; Female ; *Gene Expression Regulation, Developmental ; *Gene Targeting ; *Genes, Homeobox ; Homeodomain Proteins/*genetics/physiology ; Limb Deformities, Congenital ; Male ; Mice ; Mutation ; Nerve Tissue Proteins/*genetics/physiology ; Phenotype ; Promoter Regions, Genetic ; Recombination, Genetic ; Stem Cells ; Sternum/abnormalities
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  • 97
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    Structure-based design of transcription factors (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 98
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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)
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    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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  • 99
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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
    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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    Great transitions (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abelson, P H -- New York, N.Y. -- Science. 1995 Nov 10;270(5238):895.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481778" target="_blank"〉PubMed〈/a〉
    Keywords: *Adolescent ; Adolescent Behavior ; Female ; Health Education ; Humans ; Life Style ; Male ; Peer Group ; Television
    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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