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  • Mutation  (141)
  • American Association for the Advancement of Science (AAAS)  (141)
  • American Meteorological Society
  • 1995-1999  (141)
  • 1996  (141)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (141)
  • American Meteorological Society
  • Springer  (4)
  • Wiley-Blackwell  (1)
Years
  • 1995-1999  (141)
Year
  • 1
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    Estimating the age of the common ancestor of men from the ZFY intron (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, Y X -- Li, W H -- New York, N.Y. -- Science. 1996 May 31;272(5266):1356-7; author reply 1361-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650550" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bayes Theorem ; Biological Evolution ; Confidence Intervals ; DNA-Binding Proteins/*genetics ; *Genetics, Population ; Hominidae/*genetics ; Humans ; Introns/*genetics ; Kruppel-Like Transcription Factors ; Male ; Mutation ; Population Density ; Probability ; Time Factors ; Transcription Factors/*genetics ; Y Chromosome/*genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Identification of BIME as a subunit of the anaphase-promoting complex (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: The initiation of anaphase and exit from mitosis require the activation of a proteolytic system that ubiquitinates and degrades cyclin B. The regulated component of this system is a large ubiquitin ligase complex, termed the anaphase-promoting complex (APC) or cyclosome. Purified Xenopus laevis APC was found to be composed of eight major subunits, at least four of which became phosphorylated in mitosis. In addition to CDC27, CDC16, and CDC23, APC contained a homolog of Aspergillus nidulans BIME, a protein essential for anaphase. Because mutation of bimE can bypass the interphase arrest induced by either nimA mutation or unreplicated DNA, it appears that ubiquitination catalyzed by APC may also negatively regulate entry into mitosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peters, J M -- King, R W -- Hoog, C -- Kirschner, M W -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1199-201.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895470" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Anaphase ; Animals ; Aspergillus/chemistry/cytology/metabolism ; Cell Cycle Proteins/*chemistry/metabolism ; Cyclins/metabolism ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins/analysis/*chemistry/genetics/metabolism ; Ligases/*chemistry/metabolism ; *Mitosis ; Molecular Sequence Data ; Mutation ; Ovum ; Phosphorylation ; Ubiquitin-Protein Ligases ; Xenopus laevis
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  • 3
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    Stimulation of membrane ruffling and MAP kinase activation by distinct effectors of RAS (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-09
    Description: The RAS guanine nucleotide binding proteins activate multiple signaling events that regulate cell growth and differentiation. In quiescent fibroblasts, ectopic expression of activated H-RAS (H-RASV12, where V12 indicates valine-12) induces membrane ruffling, mitogen-activated protein (MAP) kinase activation, and stimulation of DNA synthesis. A mutant of activated H-RAS, H-RASV12C40 (where C40 indicates cysteine-40), was identified that was defective for MAP kinase activation and stimulation of DNA synthesis, but retained the ability to induce membrane ruffling. Another mutant of activated H-RAS, H-RASV12S35 (where S35 indicates serine-35), which activates MAP kinase, was defective for stimulation of membrane ruffling and induction of DNA synthesis. Expression of both mutants resulted in a stimulation of DNA synthesis that was comparable to that induced by H-RASV12. These results indicate that membrane ruffling and activation of MAP kinase represent distinct RAS effector pathways and that input from both pathways is required for the mitogenic activity of RAS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joneson, T -- White, M A -- Wigler, M H -- Bar-Sagi, D -- CA 55360/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):810-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, State University of New York at Stony Brook 11794, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8628998" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Division ; Cell Line ; Cell Membrane/*ultrastructure ; DNA/biosynthesis ; Enzyme Activation ; GTP-Binding Proteins/genetics/metabolism ; Microinjections ; Mutation ; Plasmids ; Protein-Serine-Threonine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-raf ; Rats ; Signal Transduction ; rac GTP-Binding Proteins ; ras Proteins/genetics/*metabolism
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  • 4
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    Antigen presentation and T cell development in H2-M-deficient mice (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-01
    Description: HLA-DM (DM) facilitates peptide loading of major histocompatibility complex class II molecules in human cell lines. Mice lacking functional H2-M, the mouse equivalent of DM, have normal amounts of class II molecules at the cell surface, but most of these are associated with invariant chain-derived CLIP peptides. These mice contain large numbers of CD4+ T cells, which is indicative of positive selection in the thymus. Their CD4+ cells were unresponsive to self H2-M-deficient antigen-presenting cells (APCs) but were hyperreactive to wild-type APCs. H2-M-deficient APCs failed to elicit proliferative responses from wild-type T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fung-Leung, W P -- Surh, C D -- Liljedahl, M -- Pang, J -- Leturcq, D -- Peterson, P A -- Webb, S R -- Karlsson, L -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1278-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉R. W. Johnson Pharmaceutical Research Institute, San Diego, CA 92121, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638109" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigen Presentation ; Antigen-Presenting Cells/*immunology ; Antigens, Differentiation, B-Lymphocyte/immunology/metabolism ; Base Sequence ; CD4-Positive T-Lymphocytes/*immunology ; Cells, Cultured ; Gene Targeting ; Histocompatibility Antigens Class II/genetics/*immunology/metabolism ; Isoantigens/immunology ; Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Mutation
    Print ISSN: 0036-8075
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  • 5
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    Modulation of virulence factor expression by pathogen target cell contact (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: Upon contact with the eukaryotic cell, Yersinia pseudotuberculosis increased the rate of transcription of virulence genes (yop), as determined by in situ monitoring of light emission from individual bacteria expressing luciferase under the control of the yopE promoter. The microbe-host interaction triggered export of LcrQ, a negative regulator of Yop expression, via the Yop-type III secretion system. The intracellular concentration of LcrQ was thereby lowered, resulting in increased expression of Yops. These results suggest a key role for the type III secretion system of pathogenic bacteria to coordinate secretion with expression of virulence factors after physical contact with the target cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pettersson, J -- Nordfelth, R -- Dubinina, E -- Bergman, T -- Gustafsson, M -- Magnusson, K E -- Wolf-Watz, H -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1231-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Molecular Biology, University of Umea, S-901 87 Umea, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703058" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Adhesion ; Bacterial Outer Membrane Proteins/biosynthesis/*genetics/secretion ; Bacterial Proteins/genetics/*secretion ; Calcium/metabolism ; Culture Media ; Cytosol/metabolism ; *Gene Expression Regulation, Bacterial ; HeLa Cells ; Humans ; Mutation ; Up-Regulation ; Virulence/*genetics ; Yersinia pseudotuberculosis/genetics/metabolism/*pathogenicity
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  • 6
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    Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-09
    Description: STAT proteins (signal transducers and activators of transcription) activate distinct target genes despite having similar DNA binding preferences. The transcriptional specificity of STAT proteins was investigated on natural STAT binding sites near the interferon-gamma gene. These sites are arranged in multiple copies and required cooperative interactions for STAT binding. The conserved amino-terminal domain of STAT proteins was required for cooperative DNA binding, although this domain was not essential for dimerization or binding to a single site. Cooperative binding interactions enabled the STAT proteins to recognize variations of the consensus site. These sites can be specific for the different STAT proteins and may function to direct selective transcriptional activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, X -- Sun, Y L -- Hoey, T -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):794-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik, Two Corporate Drive, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670419" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Line ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/immunology/*metabolism ; Interferon-gamma/genetics ; Introns ; Molecular Sequence Data ; Mutation ; Oligodeoxyribonucleotides/metabolism ; Promoter Regions, Genetic ; STAT1 Transcription Factor ; STAT4 Transcription Factor ; Sequence Deletion ; Signal Transduction ; Trans-Activators/chemistry/immunology/*metabolism ; *Transcriptional Activation
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  • 7
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    Functional evidence for indirect recognition of G.U in tRNA(Ala) by alanyl-tRNA synthetase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: The structural features of the G.U wobble pair in Escherichia coli alanine transfer RNA (tRNA(Ala)) that are associated with aminoacylation by alanyl-tRNA synthetase (AlaRS) were investigated in vivo for wild-type tRNA(Ala) and mutant tRNAs with G.U substitutions. tRNA(Ala) with G.U, C.A, or G.A gave similar amounts of charged tRNA(Ala) and supported viability of E. coli lacking chromosomal tRNA(Ala) genes. tRNA(Ala) with G.C was inactive. Recognition of G.U by AlaRS thus requires more than the functional groups on G.U in a regular helix and may involve detection of a helical distortion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabriel, K -- Schneider, J -- McClain, W H -- GM42123/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):195-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bacteriology, University of Wisconsin, Madison 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539617" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine-tRNA Ligase/*metabolism ; Anticodon ; Base Composition ; Base Sequence ; Escherichia coli/genetics/growth & development ; Genes, Bacterial ; Guanine/chemistry ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Plasmids ; RNA, Transfer, Ala/chemistry/genetics/*metabolism ; Uracil/chemistry
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  • 8
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    G protein-mediated neuronal DNA fragmentation induced by familial Alzheimer's disease-associated mutants of APP (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: Missense mutations in the 695-amino acid form of the amyloid precursor protein (APP695) cosegregate with disease phenotype in families with dominantly inherited Alzheimer's disease. These mutations convert valine at position 642 to isoleucine, phenylalanine, or glycine. Expression of these mutant proteins, but not of normal APP695, was shown to induce nucleosomal DNA fragmentation in neuronal cells. Induction of DNA fragmentation required the cytoplasmic domain of the mutants and appeared to be mediated by heterotrimeric guanosine triphosphate-binding proteins (G proteins).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamatsuji, T -- Matsui, T -- Okamoto, T -- Komatsuzaki, K -- Takeda, S -- Fukumoto, H -- Iwatsubo, T -- Suzuki, N -- Asami-Odaka, A -- Ireland, S -- Kinane, T B -- Giambarella, U -- Nishimoto, I -- New York, N.Y. -- Science. 1996 May 31;272(5266):1349-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cardiovascular Research Center, Massachusetts General Hospital, Department of Medicine, Harvard Medical School, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650548" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/chemistry/genetics/*physiology ; Animals ; Apoptosis ; Base Sequence ; Culture Media, Conditioned ; DNA/*metabolism ; GTP-Binding Proteins/*physiology ; Humans ; Hybrid Cells ; Mice ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Neurons/cytology/*metabolism ; Nucleosomes/*metabolism ; Peptide Fragments/metabolism ; Rats ; Transfection
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  • 9
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    Checkpoints take the next step (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carr, A M -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):314-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Research Council Cell Mutation Unit, Sussex University, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553064" target="_blank"〉PubMed〈/a〉
    Keywords: Ataxia Telangiectasia Mutated Proteins ; *Cell Cycle ; *Cell Cycle Proteins ; Checkpoint Kinase 2 ; *DNA Damage ; DNA Replication ; DNA-Binding Proteins ; Humans ; *Mitosis ; Mutation ; Phosphorylation ; Protein Kinases/genetics/*metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/genetics/metabolism ; Saccharomyces cerevisiae/cytology/metabolism ; *Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/cytology/metabolism ; Signal Transduction ; Tumor Suppressor Proteins
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  • 10
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    Sterol esterification in yeast: a two-gene process (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: Unesterified sterol modulates the function of eukaryotic membranes. In human cells, sterol is esterified to a storage form by acyl-coenzyme A (CoA): cholesterol acyl transferase (ACAT). Here, two genes are identified, ARE1 and ARE2, that encode ACAT-related enzymes in yeast. The yeast enzymes are 49 percent identical to each other and exhibit 23 percent identity to human ACAT. Deletion of ARE2 reduced sterol ester levels to approximately 25 percent of normal levels, whereas disruption of ARE1 did not affect sterol ester biosynthesis. Deletion of both genes resulted in a viable cell with undetectable esterified sterol. Measurements of [14C]acetate incorporation into saponified lipids indicated down-regulation of sterol biosynthesis in the are1 are2 mutant cells. With the use of a consensus sequence to the yeast and human genes, an additional number of the ACAT gene family was identified in humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, H -- Bard, M -- Bruner, D A -- Gleeson, A -- Deckelbaum, R J -- Aljinovic, G -- Pohl, T M -- Rothstein, R -- Sturley, S L -- GM 50237/GM/NIGMS NIH HHS/ -- HG00861/HG/NHGRI NIH HHS/ -- R01 AI38598/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 May 31;272(5266):1353-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Human Nutrition, Columbia University College of Physicians and Surgeons, New York, 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650549" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/metabolism ; Acyltransferases/chemistry/*genetics/metabolism ; Amino Acid Sequence ; Base Sequence ; Cell Membrane/metabolism ; Cholesterol Esters/metabolism ; Cyclin-Dependent Kinase 8 ; *Cyclin-Dependent Kinases ; DNA, Complementary/genetics ; Ergosterol/metabolism ; Esterification ; *Genes, Fungal ; Homeostasis ; Humans ; Molecular Sequence Data ; Mutation ; Oleic Acid ; Oleic Acids/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; Saccharomyces cerevisiae Proteins ; Sterol O-Acyltransferase/*genetics/metabolism ; Sterols/*metabolism ; Transformation, Genetic
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  • 11
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    A permease-oxidase complex involved in high-affinity iron uptake in yeast (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Iron must cross biological membranes to reach essential intracellular enzymes. Two proteins in the plasma membrane of yeast--a multicopper oxidase, encoded by the FET3 gene, and a permease, encoded by the FTR1 gene--were shown to mediate high-affinity iron uptake. FET3 expression was required for FTR1 protein to be transported to the plasma membrane. FTR1 expression was required for apo-FET3 protein to be loaded with copper and thus acquire oxidase activity. FTR1 protein also played a direct role in iron transport. Mutations in a conserved sequence motif of FTR1 specifically blocked iron transport.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stearman, R -- Yuan, D S -- Yamaguchi-Iwai, Y -- Klausner, R D -- Dancis, A -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1552-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institutes of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599111" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biological Transport ; Carrier Proteins/chemistry/*genetics/*metabolism ; Cell Membrane/metabolism ; *Ceruloplasmin ; Copper/metabolism/pharmacology ; Endoplasmic Reticulum/metabolism ; Ferric Compounds/metabolism ; Ferritins/chemistry/metabolism ; Ferrous Compounds/metabolism ; Genes, Fungal ; Golgi Apparatus/metabolism ; Iron/*metabolism ; Membrane Transport Proteins/chemistry/*genetics/*metabolism ; Models, Biological ; Molecular Sequence Data ; Multienzyme Complexes/*metabolism ; Mutation ; Open Reading Frames ; Oxidation-Reduction ; Oxidoreductases/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transformation, Genetic
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  • 12
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    Structural basis of ligand discrimination by two related RNA aptamers resolved by NMR spectroscopy (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: In a previous study, an RNA aptamer for the specific recognition of arginine was evolved from a parent sequence that bound citrulline specifically. The two RNAs differ at only 3 positions out of 44. The solution structures of the two aptamers complexed to their cognate amino acids have now been determined by two-dimensional nuclear magnetic resonance spectroscopy. Both aptamers contain two asymmetrical internal loops that are not well ordered in the free RNA but that fold into a compact structure upon ligand binding. Those nucleotides common to both RNAs include a conserved cluster of purine residues, three of which form an uneven plane containing a G:G pair, and two other residues nearly perpendicular to that surface. Two of the three variant nucleotides are stacked on the cluster of purines and form a triple contact to the amino acid side chain, whereas the edge of the third variant nucleotide is capping the binding pocket.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, Y -- Kochoyan, M -- Burgstaller, P -- Westhof, E -- Famulok, M -- New York, N.Y. -- Science. 1996 May 31;272(5266):1343-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Biochimie Structurale (CBS), Unite Mixte de Recherche, CNRS 9955, Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650546" target="_blank"〉PubMed〈/a〉
    Keywords: Arginine/chemistry/*metabolism ; Base Composition ; Base Sequence ; Citrulline/chemistry/*metabolism ; Crystallography, X-Ray ; Hydrogen Bonding ; Ligands ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Mutation ; *Nucleic Acid Conformation ; RNA/*chemistry/genetics/*metabolism
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  • 13
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    Molecular genetic insights into cardiovascular disease (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: The recent application of molecular genetic tools to inherited forms of cardiovascular disease has provided important insight into the molecular mechanisms underlying cardiac arrhythmias, cardiomyopathies, and vascular diseases. These studies point to defects in ion channels, contractile proteins, structural proteins, and signaling molecules as key players in disease pathogenesis. Genetic testing is now available for a subset of inherited cardiovascular diseases, and new mechanism-based therapies may be available in the near future. This remarkable progress and the implications it may have for more common forms of cardiovascular disease are reviewed here.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keating, M T -- Sanguinetti, M C -- New York, N.Y. -- Science. 1996 May 3;272(5262):681-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Utah, Salt Lake City, 84112, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614827" target="_blank"〉PubMed〈/a〉
    Keywords: Arrhythmias, Cardiac/diagnosis/*genetics ; Cardiomyopathies/diagnosis/*genetics ; Contractile Proteins/genetics ; Genetic Predisposition to Disease ; Genetic Testing ; Humans ; Ion Channels/genetics ; Mutation ; Myocardium/metabolism ; Prognosis ; Risk Factors ; Vascular Diseases/diagnosis/*genetics
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  • 14
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    Control of C. elegans larval development by neuronal expression of a TGF-beta homolog (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: The Caenorhabditis elegans dauer larva is specialized for dispersal without growth and is formed under conditions of overcrowding and limited food. The daf-7 gene, required for transducing environmental cues that support continuous development with plentiful food, encodes a transforming growth factor-beta (TGF-beta) superfamily member. A daf-7 reporter construct is expressed in the ASI chemosensory neurons. Dauer-inducing pheromone inhibits daf-7 expression and promotes dauer formation, whereas food reactivates daf-7 expression and promotes recovery from the dauer state. When the food/pheromone ratio is high, the level of daf-7 mRNA peaks during the L1 larval stage, when commitment to non-dauer development is made.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ren, P -- Lim, C S -- Johnsen, R -- Albert, P S -- Pilgrim, D -- Riddle, D L -- HD11239/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1389-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Program and Division of Biological Sciences, 311 Tucker Hall, University of Missouri, Columbia, MO 65211, USA. riddle@biosci.mbp.missouri.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910282" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Animals, Genetically Modified ; Caenorhabditis elegans/genetics/*growth & development/metabolism ; *Caenorhabditis elegans Proteins ; Genes, Helminth ; Genes, Reporter ; Green Fluorescent Proteins ; Helminth Proteins/chemistry/genetics/*physiology ; Humans ; Larva/growth & development/metabolism ; Ligands ; Luminescent Proteins/genetics ; Molecular Sequence Data ; Mutation ; Neurons, Afferent/*metabolism ; Phenotype ; Pheromones/pharmacology ; Temperature ; Transforming Growth Factor beta/chemistry/genetics/*physiology ; Transgenes
    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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  • 15
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    Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: A cytosolic yeast karyopherin, Kap104p, was isolated and shown to function in the nuclear import of a specific class of proteins. The protein bound directly to repeat-containing nucleoporins and to a cytosolic pool of two nuclear messenger RNA (mRNA) binding proteins, Nab2p and Nab4p. Depletion of Kap104p resulted in a rapid shift of Nab2p from the nucleus to the cytoplasm without affecting the localization of other nuclear proteins tested. This finding suggests that the major function of Kap104p lies in returning mRNA binding proteins to the nucleus after mRNA export.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aitchison, J D -- Blobel, G -- Rout, M P -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):624-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. blobel@rockvax.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849456" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Biological Transport ; Carrier Proteins/chemistry/isolation & purification/*metabolism ; Cell Nucleus/*metabolism ; Cytosol/chemistry/metabolism ; Fungal Proteins/*metabolism ; *Karyopherins ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Mutation ; Nuclear Envelope/metabolism ; *Nuclear Pore Complex Proteins ; Nuclear Proteins/*metabolism ; *Nucleocytoplasmic Transport Proteins ; RNA, Messenger/genetics/metabolism ; RNA-Binding Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*metabolism ; *Saccharomyces cerevisiae Proteins ; Temperature ; beta Karyopherins
    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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  • 16
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    New 'Alzheimer's mouse' produced (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):177-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8927978" target="_blank"〉PubMed〈/a〉
    Keywords: *Alzheimer Disease/genetics/metabolism/pathology ; Amyloid beta-Peptides/blood/metabolism ; Amyloid beta-Protein Precursor/*genetics ; Animals ; Brain/pathology ; Brain Chemistry ; *Disease Models, Animal ; Learning Disorders/etiology ; Memory Disorders/etiology ; Mice ; Mice, Inbred C57BL ; *Mice, Transgenic ; Mutation ; Peptide Fragments/blood/metabolism ; Transgenes
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: During neurogenesis in Drosophila both neurons and nonneuronal cells are produced from a population of initially equivalent cells. The kuzbanian (kuz) gene described here is essential for the partitioning of neural and nonneuronal cells during development of both the central and peripheral nervous systems in Drosophila. Mosaic analyses indicated that kuz is required for cells to receive signals inhibiting the neural fate. These analyses further revealed that the development of a neuron requires a kuz-mediated positive signal from neighboring cells. The kuz gene encodes a metalloprotease-disintegrin protein with a highly conserved bovine homolog, raising the possibility that kuz homologs may act in similar processes during mammalian neurogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rooke, J -- Pan, D -- Xu, T -- Rubin, G M -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1227-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Boyer Center for Molecular Medicine, Yale University School of Medicine, New Haven, CT 06536, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703057" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Disintegrins/chemistry/genetics/*physiology ; Drosophila/cytology/embryology/*genetics/physiology ; *Drosophila Proteins ; *Genes, Insect ; Metalloendopeptidases/chemistry/genetics/*physiology ; Molecular Sequence Data ; Mosaicism ; Mutation ; Nervous System/embryology ; Neurons/*cytology ; Photoreceptor Cells, Invertebrate/cytology/embryology
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  • 18
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    Control of the gene optomotor-blind in Drosophila wing development by decapentaplegic and wingless (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Diffusible factors of several protein families control appendage outgrowth and patterning in both insects and vertebrates. In Drosophila wing development, the gene decapentaplegic (dpp) is expressed along the anteroposterior compartment boundary. Early wingless (wg) expression is involved in setting up the dorsoventral boundary. Interaction between dpp- and wg-expressing cells promotes appendage outgrowth. Here, it is shown that optomotor-blind (omb) expression is required for distal wing development and is controlled by both dpp and wg. Ectopic omb expression can lead to the growth of additional wings. Thus, omb is essential for wing development and is controlled by two signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grimm, S -- Pflugfelder, G O -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1601-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Theodor-Boveri-Institut (Biozentrum), Lehrstuhl fur Genetik, Universitat Wurzburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599120" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA-Binding Proteins/*genetics/physiology ; Drosophila/*genetics/growth & development ; *Drosophila Proteins ; *Gene Expression Regulation, Developmental ; Genes, Insect ; Insect Hormones/*genetics/physiology ; Larva/genetics/growth & development ; Mutation ; Nerve Tissue Proteins/*genetics/physiology ; Phenotype ; Proto-Oncogene Proteins/*genetics/physiology ; Signal Transduction ; *T-Box Domain Proteins ; Wings, Animal/*growth & development ; Wnt1 Protein
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  • 19
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    Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: Rapamycin, a potent immunosuppressive agent, binds two proteins: the FK506-binding protein (FKBP12) and the FKBP-rapamycin-associated protein (FRAP). A crystal structure of the ternary complex of human FKBP12, rapamycin, and the FKBP12-rapamycin-binding (FRB) domain of human FRAP at a resolution of 2.7 angstroms revealed the two proteins bound together as a result of the ability of rapamycin to occupy two different hydrophobic binding pockets simultaneously. The structure shows extensive interactions between rapamycin and both proteins, but fewer interactions between the proteins. The structure of the FRB domain of FRAP clarifies both rapamycin-independent and -dependent effects observed for mutants of FRAP and its homologs in the family of proteins related to the ataxia-telangiectasia mutant gene product, and it illustrates how a small cell-permeable molecule can mediate protein dimerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Choi, J -- Chen, J -- Schreiber, S L -- Clardy, J -- CA59021/CA/NCI NIH HHS/ -- GM38625/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):239-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Baker Laboratory, Cornell University, Ithaca, NY 14853-1301, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662507" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carrier Proteins/chemistry/genetics/*metabolism ; Crystallography, X-Ray ; DNA-Binding Proteins/chemistry/*metabolism ; Heat-Shock Proteins/chemistry/*metabolism ; Humans ; *Immunophilins ; Models, Molecular ; Mutation ; *Phosphotransferases (Alcohol Group Acceptor) ; Polyenes/*chemistry/*metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/chemistry/metabolism ; Sirolimus ; TOR Serine-Threonine Kinases ; Tacrolimus Binding Proteins
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  • 20
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    Circadian rhythms in cultured mammalian retina (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-19
    Description: Many retinal functions are circadian, but in most instances the location of the clock that drives the rhythm is not known. Cultured neural retinas of the golden hamster (Mesocricetus auratus) exhibited circadian rhythms of melatonin synthesis for at least 5 days at 27 degrees celsius. The rhythms were entrained by light cycles applied in vitro and were free-running in constant darkness. Retinas from hamsters homozygous for the circadian mutation tau, which shortens the free-running period of the circadian activity rhythm by 4 hours, showed a shortened free-running period of melatonin synthesis. The mammalian retina contains a genetically programmed circadian oscillator that regulates its synthesis of melatonin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tosini, G -- Menaker, M -- HD13162/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):419-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Virginia, Charlottesville, VA 22903, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602533" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks ; *Circadian Rhythm/genetics ; Cricetinae ; Culture Techniques ; Darkness ; Genes ; Light ; Melatonin/*biosynthesis ; Mesocricetus ; Mutation ; Retina/metabolism/*physiology ; Temperature
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
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    Flies unmask evolutionary warfare between the sexes (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1996 May 17;272(5264):953-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638139" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Drosophila/genetics/*physiology ; Female ; Genes, Insect ; Male ; Mutation ; Reproduction ; Sex Characteristics ; Sexual Behavior, Animal
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  • 22
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    Sperm protein makes its mark upon the worm embryo (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539595" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*embryology/genetics ; *Caenorhabditis elegans Proteins ; *Embryonic Development ; Female ; Fertilization ; Genes, Helminth ; Helminth Proteins/genetics/*physiology ; Male ; Mutation ; *Nuclear Proteins ; Oocytes/physiology ; Spermatozoa/*chemistry/physiology
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  • 23
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    HERG sequence correction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Trudeau, M C -- Warmke, J W -- Ganetzky, B -- Robertson, G A -- New York, N.Y. -- Science. 1996 May 24;272(5265):1087.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638148" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Humans ; Mutation ; Potassium Channels/*genetics ; *Potassium Channels, Inwardly Rectifying
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  • 24
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    Cell killing by the Drosophila gene reaper (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-09
    Description: The reaper gene (rpr) is important for the activation of apoptosis in Drosophila. To investigate whether rpr expression is sufficient to induce apoptosis, transgenic flies were generated that express rpr complementary DNA or the rpr open reading frame in cells that normally live. Transcription of rpr from a heat-inducible promoter rapidly caused wide-spread ectopic apoptosis and organismal death. Ectopic overexpression of rpr in the developing retina resulted in eye ablation. The occurrence of cell death was highly sensitive to the dosage of the transgene. Because cell death induced by the protein encoded by rpr (RPR) could be blocked by the baculovirus p35 protein, RPR appears to activate a death program mediated by a ced-3/ICE (interleukin-1 converting enzyme)-like protease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉White, K -- Tahaoglu, E -- Steller, H -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):805-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cutaneous Biology Research Center, Massachusetts General Hospital, Charlestown 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8628996" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; *Apoptosis ; Caspase 1 ; Cysteine Endopeptidases/metabolism ; DNA, Complementary/genetics ; Drosophila/cytology/embryology/*genetics ; *Drosophila Proteins ; Gene Dosage ; Gene Expression ; *Genes, Insect ; Hot Temperature ; Inhibitor of Apoptosis Proteins ; Mutation ; Open Reading Frames ; Peptides/*genetics/physiology ; Photoreceptor Cells, Invertebrate/cytology ; Transgenes ; Viral Proteins/genetics/physiology
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  • 25
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    Evidence that Spt6p controls chromatin structure by a direct interaction with histones (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-07
    Description: Genetic analysis has implicated SPT6, an essential gene of Saccharomyces cerevisiae, in the control of chromatin structure. Mutations in SPT6 and particular mutations in histone genes are able to overcome transcriptional defects in strains lacking the Snf/Swi protein complex. Here it is shown that an spt6 mutation causes changes in chromatin structure in vivo. In addition, both in vivo and in vitro experiments provide evidence that Spt6p interacts directly with histones and primarily with histone H3. Consistent with these findings, Spt6p is capable of nucleosome assembly in vitro.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bortvin, A -- Winston, F -- GM32967/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 7;272(5267):1473-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8633238" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/chemistry/genetics/metabolism/*ultrastructure ; DNA, Fungal/metabolism ; Fungal Proteins/genetics/metabolism/*physiology ; Histones/chemistry/genetics/*metabolism ; Humans ; Mutation ; Nuclear Proteins/genetics/metabolism/*physiology ; Nucleosomes/metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Transcription, Genetic ; Transcriptional Elongation Factors
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  • 26
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    Gene perplexes epilepsy researchers (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-03-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, C -- New York, N.Y. -- Science. 1996 Mar 22;271(5256):1672.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596927" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Chromosome Mapping ; Chromosomes, Human, Pair 21/*genetics ; Cystatin B ; Cystatins/*genetics ; Cysteine Proteinase Inhibitors/*genetics ; Epilepsies, Myoclonic/*genetics ; Female ; Humans ; Male ; Mutation ; Pedigree ; RNA, Messenger/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 27
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    Evidence for physical and functional association between EMB-5 and LIN-12 in Caenorhabditis elegans (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-05
    Description: The Caenorhabditis elegans LIN-12 and GLP-1 proteins are members of the LIN-12/Notch family of receptors for intercellular signals that specify cell fate. Evidence presented here suggests that the intracellular domains of LIN-12 and GLP-1 interact with the C. elegans EMB-5 protein and that the emb-5 gene functions in the same pathway as the lin-12 and glp-1 genes. EMB-5 is similar in sequence to a yeast protein that controls chromatin structure. Hence, a direct consequence of LIN-12 or GLP-1 activation may be an alteration of chromatin structure that produces changes in transcriptional activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hubbard, E J -- Dong, Q -- Greenwald, I -- GM37602/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jul 5;273(5271):112-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*cytology/embryology/genetics/*metabolism ; *Caenorhabditis elegans Proteins ; Cell Lineage ; Chromatin/metabolism ; Gene Expression Regulation, Developmental ; Genes, Helminth ; Helminth Proteins/genetics/*metabolism ; Meiosis ; Membrane Proteins/genetics/*metabolism ; Mitosis ; Mutation ; Receptors, Notch ; *Signal Transduction ; Temperature ; Transcription Factors/genetics/*metabolism
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  • 28
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    Initiation of runaway cell death in an Arabidopsis mutant by extracellular superoxide (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-27
    Description: Reactive oxygen intermediates (ROIs) regulate apoptosis during normal development and disease in animals. ROIs are also implicated in hypersensitive resistance responses of plants against pathogens. Arabidopsis lsd1 mutants exhibited impaired control of cell death in the absence of pathogen and could not control the spread of cell death once it was initiated. Superoxide was necessary and sufficient to initiate lesion formation; it accumulated before the onset of cell death and subsequently in live cells adjacent to spreading lsd1 lesions. Thus, runaway cell death seen in lsd1 plants reflected abnormal accumulation of superoxide and lack of responsiveness to signals derived from it.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jabs, T -- Dietrich, R A -- Dangl, J L -- New York, N.Y. -- Science. 1996 Sep 27;273(5283):1853-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Delbruck Laboratory, Carl von Linne Weg 10, 50829 Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8791589" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Arabidopsis/*cytology/genetics/metabolism ; Cell Membrane/enzymology ; Enzyme Inhibitors/pharmacology ; Gene Expression Regulation, Plant ; Genes, Plant ; Glutathione Transferase/genetics/metabolism ; Mutation ; NADH, NADPH Oxidoreductases/antagonists & inhibitors/metabolism ; NADPH Oxidase ; Onium Compounds/pharmacology ; Peroxidases/genetics/metabolism ; Plant Leaves/cytology/metabolism ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Reactive Oxygen Species/metabolism ; Superoxide Dismutase/genetics ; Superoxides/*metabolism
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  • 29
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    Streetcar carries evolution modelers around roadblocks (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1365-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596907" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Game Theory ; Genes ; Genetics, Population ; Humans ; *Models, Biological ; Models, Genetic ; Mutation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Will a twist of viral fate lead to a new cancer treatment? (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1996 Oct 18;274(5286):342-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8927990" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1B Proteins/*genetics/metabolism ; Adenoviruses, Human/genetics/*physiology ; Animals ; Clinical Trials, Phase I as Topic ; Cytopathogenic Effect, Viral ; Genes, Viral ; *Genes, p53 ; Head and Neck Neoplasms/*therapy/virology ; Humans ; Mice ; Mutation ; Neoplasm Transplantation ; Neoplasms, Experimental/*therapy/virology ; Tumor Suppressor Protein p53/metabolism ; Virus Replication
    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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  • 31
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    Identification of an asymmetrically localized sensor histidine kinase responsible for temporally and spatially regulated transcription (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: Caulobacter crescentus undergoes asymmetric cell division, resulting in a stalked cell and a motile swarmer cell. The genes encoding external components of the flagellum are expressed in the swarmer compartment of the predivisional cell through the localized activation of the transcription factor FlbD. The mechanisms responsible for the temporal and spatial activation of FlbD were determined through identification of FlbE, a histidine kinase required for FlbD activity. FlbE is asymmetrically distributed in the predivisional cell. It is located at the pole of the stalked compartment and at the site of cell division in the swarmer compartment. These findings suggest that FlbE and FlbD are activated in response to a morphological change in the cell resulting from cell division events.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wingrove, J A -- Gober, J W -- GM-07104/GM/NIGMS NIH HHS/ -- GM48417/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):597-601.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry and the Molecular Biology Institute, University of California, Los Angeles, CA 90095-1569, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849449" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/genetics/*metabolism ; Caulobacter crescentus/cytology/*genetics/physiology ; Cell Division ; DNA-Binding Proteins/genetics/*metabolism ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; Mutation ; Phosphorylation ; Promoter Regions, Genetic ; Protein Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic
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    Molecular pathways controlling heart development (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: Heart formation requires complex interactions among cells from multiple embryonic origins. Recent studies have begun to reveal the genetic pathways that control cardiac morphogenesis. Many of the genes within these pathways are conserved across vast phylogenetic distances, which has allowed cardiac development to be dissected in organisms ranging from flies to mammals. Studies of cardiac development have also revealed the molecular defects underlying several congenital cardiac malformations in humans and may ultimately provide opportunities for genetic testing and intervention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, E N -- Srivastava, D -- New York, N.Y. -- Science. 1996 May 3;272(5262):671-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Oncology, University of Texas Southwestern Medical Center, Dallas, 75235-9148, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614825" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; *Gene Expression Regulation, Developmental ; Genes ; Genes, Regulator ; Heart/*embryology ; Heart Conduction System/embryology ; Heart Defects, Congenital/embryology/*genetics/pathology ; Humans ; Morphogenesis ; Mutation ; Myocardium/cytology ; Neural Crest/cytology ; Transcription Factors/physiology ; Transcription, Genetic
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    Worm genes imply a master clock (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1996 May 17;272(5264):949-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638138" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Animals ; Biological Clocks/*genetics ; Caenorhabditis elegans/*genetics/physiology ; *Genes, Helminth ; Longevity/genetics ; Mutation
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  • 34
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    Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-09
    Description: Bruton's tyrosine kinase (BTK) is pivotal in B cell activation and development through its participation in the signaling pathways of multiple hematopoietic receptors. The mechanisms controlling BTK activation were studied here by examination of the biochemical consequences of an interaction between BTK and SRC family kinases. This interaction of BTK with SRC kinases transphosphorylated BTK on tyrosine at residue 551, which led to BTK activation. BTK then autophosphorylated at a second site. The same two sites were phosphorylated upon B cell antigen receptor cross-linking. The activated BTK was predominantly membrane-associated, which suggests that BTK integrates distinct receptor signals resulting in SRC kinase activation and BTK membrane targeting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rawlings, D J -- Scharenberg, A M -- Park, H -- Wahl, M I -- Lin, S -- Kato, R M -- Fluckiger, A C -- Witte, O N -- Kinet, J P -- AR01912/AR/NIAMS NIH HHS/ -- AR36834/AR/NIAMS NIH HHS/ -- CA09120-20/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Feb 9;271(5250):822-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90095-1662, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8629002" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; B-Lymphocytes/*enzymology ; Cell Line, Transformed ; Cell Membrane/enzymology ; Enzyme Activation ; Immunoglobulin M/immunology ; Lymphocyte Activation ; Mice ; Mutation ; Phosphopeptides/analysis ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptors, Antigen, B-Cell/metabolism ; Signal Transduction ; src-Family Kinases/*metabolism
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    Selector genes, polymorphisms, and evolution (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tautz, D -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):160-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zoologisches Institut, Universitat Munchen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539613" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA-Binding Proteins/*genetics ; Drosophila/drug effects/*genetics ; *Drosophila Proteins ; Ether/pharmacology ; *Genes, Homeobox ; Genes, Insect ; *Genes, Regulator ; Homeodomain Proteins/*genetics ; Homeostasis ; Mutation ; *Polymorphism, Genetic ; *Transcription Factors
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  • 36
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    Regulation of an early developmental checkpoint in the B cell pathway by Ig beta (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-19
    Description: Many of the cell fate decisions in precursor B cells and more mature B cells are controlled by membrane immunoglobulin (Ig)M heavy chain (mu) and the Ig alpha-Ig beta signal transducers. The role of Ig beta in regulating early B cell development was examined in mice that lack Ig beta (Ig beta-/-). These mice had a complete block in B cell development at the immature CD43+B220+ stage. Immunoglobulin heavy chain diversity (DH) and joining (JH) segments rearranged, but variable (VH) to DJH recombination and immunoglobulin messenger RNA expression were compromised. These experiments define an unexpected, early requirement for Ig(beta) to produce B cells that can complete VDJH recombination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gong, S -- Nussenzweig, M C -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):411-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602530" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/genetics/*physiology ; Antigens, CD79 ; B-Lymphocytes/cytology/*immunology ; Gene Expression ; *Gene Rearrangement, B-Lymphocyte, Heavy Chain ; Gene Targeting ; Genes, Immunoglobulin ; Immunoglobulin Heavy Chains/*genetics ; Immunoglobulin Joining Region/genetics ; Immunoglobulin Light Chains/*genetics ; Immunoglobulin Variable Region/genetics ; Immunoglobulin mu-Chains/biosynthesis/genetics/physiology ; Lymph Nodes ; Mice ; Mice, Inbred C57BL ; Mutation ; RNA, Messenger/genetics ; Receptors, Antigen, B-Cell/physiology ; *Recombination, Genetic ; Signal Transduction
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  • 37
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    Diffusional mobility of Golgi proteins in membranes of living cells (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-09
    Description: The mechanism by which Golgi membrane proteins are retained within the Golgi complex in the midst of a continuous flow of protein and lipid is not yet understood. The diffusional mobilities of mammalian Golgi membrane proteins fused with green fluorescent protein from Aequorea victoria were measured in living HeLa cells with the fluorescence photobleaching recovery technique. The diffusion coefficients ranged from 3 x 10(-9) square centimeters per second to 5 x 10(-9) square centimeters per second, with greater than 90 percent of the chimeric proteins mobile. Extensive lateral diffusion of the chimeric proteins occurred between Golgi stacks. Thus, the chimeras diffuse rapidly and freely in Golgi membranes, which suggests that Golgi targeting and retention of these molecules does not depend on protein immobilization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cole, N B -- Smith, C L -- Sciaky, N -- Terasaki, M -- Edidin, M -- Lippincott-Schwartz, J -- R37 AI14584/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):797-801.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Building 18T, 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/8670420" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Compounds/pharmacology ; Diffusion ; Endoplasmic Reticulum/metabolism ; Fluorides/pharmacology ; Golgi Apparatus/*metabolism ; Green Fluorescent Proteins ; HeLa Cells ; Humans ; Intracellular Membranes/metabolism ; Luminescent Proteins ; Mannosidases/*metabolism ; Membrane Proteins/*metabolism ; Microscopy, Confocal ; Mutation ; N-Acetyllactosamine Synthase/*metabolism ; Receptors, Peptide/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism
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    Mechanosensation and the DEG/ENaC ion channels (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corey, D P -- Garcia-Anoveros, J -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):323-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8685718" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Caenorhabditis elegans/genetics/*physiology ; Genes, Helminth ; Helminth Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Muscle Contraction ; Mutation ; Phenotype ; Sensation/genetics/*physiology ; Sodium Channels/chemistry/genetics/*physiology ; Touch/genetics/physiology
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  • 39
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    Uncoupling of GTP binding from target stimulation by a single mutation in the transducin alpha subunit (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-08
    Description: Glutamic acid-203 of the alpha subunit of transducin (alphaT) resides within a domain that undergoes a guanosine triphosphate (GTP)-induced conformational change that is essential for effector recognition. Changing the glutamic acid to an alanine in bovine alpha(T) yielded an alpha subunit (alpha(T)E203A) that was fully dependent on rhodopsin for GTP-guanosine diphosphate (GDP) exchange and showed GTP hydrolytic activity similar to that measured for wild-type alpha(T). However, unlike the wild-type protein, the GDP-bound form of alpha(T)E203A was constitutively active toward the effector of transducin, the cyclic guanosine monophosphate phosphodiesterase. Thus, the alpha(T)E203A mutant represents a short-circuited protein switch that no longer requires GTP for the activation of the effector target phosphodiesterase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mittal, R -- Erickson, J W -- Cerione, R A -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1413-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Cornell University, Ithaca, NY 14853-6401, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596913" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-GMP Phosphodiesterases/*metabolism ; Adenosine Diphosphate Ribose/metabolism ; Alanine/chemistry ; Animals ; Base Sequence ; Cattle ; Enzyme Activation ; Glutamic Acid/chemistry ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/*metabolism ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins ; Rhodopsin/metabolism ; Transducin/chemistry/genetics/*metabolism
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    Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-08
    Description: Mutations in the p53 tumor suppressor are among the most frequently observed genetic alterations in human cancer and map to the 200-amino acid core domain of the protein. The core domain contains the sequence-specific DNA binding activity and the in vitro 53BP2 protein binding activity of p53. The crystal structure of the p53 core domain bound to the 53BP2 protein, which contains an SH3 (Src homology 3) domain and four ankyrin repeats, revealed that (i) the SH3 domain binds the L3 loop of p53 in a manner distinct from that of previously characterized SH3-polyproline peptide complexes, and (ii) an ankyrin repeat, which forms an L-shaped structure consisting of a beta hairpin and two alpha helices, binds the L2 loop of p53. The structure of the complex shows that the 53BP2 binding site on the p53 core domain consists of evolutionarily conserved regions that are frequently mutated in cancer and that it overlaps the site of DNA binding. The six most frequently observed p53 mutations disrupt 53BP2 binding in vitro. The structure provides evidence that the 53BP2-p53 complex forms in vivo and may have a critical role in the p53 pathway of tumor suppression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorina, S -- Pavletich, N P -- CA65698/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):1001-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875926" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ankyrins/*chemistry ; Apoptosis Regulatory Proteins ; Binding Sites ; Carrier Proteins/*chemistry/metabolism ; Crystallography, X-Ray ; DNA/metabolism ; Humans ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Neoplasms/genetics ; Protein Binding ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Tumor Suppressor Protein p53/*chemistry/genetics/metabolism ; *src Homology Domains
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    A mouse model of familial hypertrophic cardiomyopathy (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: A mouse model of familial hypertrophic cardiomyopathy (FHC) was generated by the introduction of an Arg 403 --〉 Gln mutation into the alpha cardiac myosin heavy chain (MHC) gene. Homozygous alpha MHC 403/403 mice died 7 days after birth, and sedentary heterozygous alpha MHC 403/+ mice survived for 1 year. Cardiac histopathology and dysfunction in the alpha MHC 403/+ mice resembled human FHC. Cardiac dysfunction preceded histopathologic changes, and myocyte disarray, hypertrophy, and fibrosis increased with age. Young male alpha MHC 403/+ mice showed more evidence of disease than did their female counterparts. Preliminary results suggested that exercise capacity may have been compromised in the alpha MHC 403/+ mice. This mouse model may help to define the natural history of FHC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geisterfer-Lowrance, A A -- Christe, M -- Conner, D A -- Ingwall, J S -- Schoen, F J -- Seidman, C E -- Seidman, J G -- New York, N.Y. -- Science. 1996 May 3;272(5262):731-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614836" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cardiac Output ; Cardiomyopathy, Hypertrophic/*genetics/pathology/physiopathology ; *Disease Models, Animal ; Female ; Gene Transfer Techniques ; Heart/*physiopathology ; Heterozygote ; Homozygote ; Humans ; Male ; Mice ; Mice, Mutant Strains ; Molecular Sequence Data ; Mutation ; Myocardium/chemistry/*pathology ; Myosin Heavy Chains/*genetics ; Physical Exertion ; Sex Characteristics ; Ventricular Function, Left
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    Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: Pycnodysostosis, an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature, maps to chromosome 1q21. Cathepsin K, a cysteine protease gene that is highly expressed in osteoclasts, localized to the pycnodysostosis region. Nonsense, missense, and stop codon mutations in the gene encoding cathepsin K were identified in patients. Transient expression of complementary DNA containing the stop codon mutation resulted in messenger RNA but no immunologically detectable protein. Thus, pycnodysostosis results from gene defects in a lysosomal protease with highest expression in osteoclasts. These findings suggest that cathepsin K is a major protease in bone resorption, providing a possible rationale for the treatment of disorders such as osteoporosis and certain forms of arthritis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gelb, B D -- Shi, G P -- Chapman, H A -- Desnick, R J -- R01 DK31775/DK/NIDDK NIH HHS/ -- R01 HL44816/HL/NHLBI NIH HHS/ -- R37 DK34045/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1236-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Human Genetics and Division of Pediatric Cardiology, 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/8703060" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Bone Matrix/metabolism ; Bone Resorption ; Cathepsin K ; Cathepsins/deficiency/*genetics/metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 1 ; Codon, Terminator ; Dinucleoside Phosphates/genetics ; Humans ; Lysosomal Storage Diseases/enzymology/*genetics ; Lysosomes/*enzymology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Osteochondrodysplasias/enzymology/*genetics ; Osteoclasts/*enzymology ; Transfection
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    CKI1, a histidine kinase homolog implicated in cytokinin signal transduction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-08
    Description: Although cytokinin plays a central role in plant development, little is known about cytokinin signal transduction. Five Arabidopsis thaliana mutants that exhibit typical cytokinin responses, including rapid cell division and shoot formation in tissue culture in the absence of exogenous cytokinin, were isolated by activation transferred DNA tagging. A gene, CKI1, which was tagged in four of the five mutants and induced typical cytokinin responses after introduction and overexpression in plants, was cloned. CKI1 encodes a protein similar to the two-component regulators. These results suggest that CKI1 is involved in cytokinin signal transduction, possibly as a cytokinin receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kakimoto, T -- New York, N.Y. -- Science. 1996 Nov 8;274(5289):982-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8875940" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics/*physiology ; *Arabidopsis Proteins ; Cloning, Molecular ; Cytokinins/pharmacology/*physiology ; DNA, Bacterial/genetics ; DNA, Complementary/genetics ; DNA, Plant/genetics ; Ethylenes/metabolism ; Genes, Plant ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Plant Proteins/chemistry/metabolism ; Polymorphism, Restriction Fragment Length ; Protein Kinases/chemistry/genetics/*physiology ; *Receptors, Cell Surface ; Sequence Homology, Amino Acid ; *Signal Transduction ; Transformation, Genetic
    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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    PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: A second gene for autosomal dominant polycystic kidney disease was identified by positional cloning. Nonsense mutations in this gene (PKD2) segregated with the disease in three PKD2 families. The predicted 968-amino acid sequence of the PKD2 gene product has six transmembrane spans with intracellular amino- and carboxyl-termini. The PKD2 protein has amino acid similarity with PKD1, the Caenorhabditis elegans homolog of PKD1, and the family of voltage-activated calcium (and sodium) channels, and it contains a potential calcium-binding domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mochizuki, T -- Wu, G -- Hayashi, T -- Xenophontos, S L -- Veldhuisen, B -- Saris, J J -- Reynolds, D M -- Cai, Y -- Gabow, P A -- Pierides, A -- Kimberling, W J -- Breuning, M H -- Deltas, C C -- Peters, D J -- Somlo, S -- DK02015/DK/NIDDK NIH HHS/ -- DK48383/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 May 31;272(5266):1339-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Renal Division, Department of Medicine and Molecular Genetics, Albert Einstein College of Medicine, Bronx, NY 10461, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650545" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis elegans/chemistry/genetics ; Calcium Channels/chemistry/genetics ; Chromosome Mapping ; Chromosomes, Human, Pair 4 ; Cloning, Molecular ; Consensus Sequence ; Crystallography, X-Ray ; Female ; Glycosylation ; Humans ; Male ; Membrane Proteins/chemistry/*genetics/physiology ; Molecular Sequence Data ; Mutation ; Pedigree ; Phenotype ; Polycystic Kidney, Autosomal Dominant/*genetics ; Polymorphism, Single-Stranded Conformational ; Proteins/chemistry/genetics ; Sodium Channels/chemistry/genetics ; TRPP Cation Channels
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Fly gene discovery gets at root of branching structures (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2011.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984660" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Body Patterning ; *Drosophila Proteins ; Drosophila melanogaster/embryology/*genetics ; Fibroblast Growth Factors/chemistry ; Gene Expression Regulation, Developmental ; *Genes, Insect ; Insect Proteins/chemistry/*genetics/metabolism/physiology ; Larva/growth & development ; Morphogenesis ; Mutation ; *Protein-Tyrosine Kinases ; Receptors, Fibroblast Growth Factor/genetics/metabolism ; Trachea/embryology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Hedgehog's patterning call is patched through, smoothly (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1304-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8966601" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Body Patterning ; Carcinoma, Basal Cell/genetics/therapy ; Hedgehog Proteins ; Humans ; Membrane Proteins/genetics/*metabolism ; Mutation ; Proteins/*metabolism ; Receptors, Cell Surface/*metabolism/physiology ; *Receptors, G-Protein-Coupled ; Signal Transduction ; Skin Neoplasms/genetics/therapy ; *Trans-Activators
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  • 47
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    Interaction between Wingless and Notch signaling pathways mediated by dishevelled (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-29
    Description: In Drosophila, the Wingless and Notch signaling pathways function in m any of the same developmental patterning events. Genetic analysis demonstrates that the dishevelled gene, which encodes a molecule previously implicated in implementation of the Winglass signal, interacts antagonistically with Notch and one of its known ligands, Delta. A direct physical interaction between Dishevelled and the Notch carboxyl terminus, distal to the cdc10/ankyrin repeats, suggests a mechanism for this interaction. It is proposed that Dishevelled, in addition to transducing the Wingless signal, blocks Notch signaling directly, thus providing a molecular mechanism for the inhibitory cross talk observed between these pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Axelrod, J D -- Matsuno, K -- Artavanis-Tsakonas, S -- Perrimon, N -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1826-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596950" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Clone Cells ; Drosophila/genetics/growth & development/*metabolism ; *Drosophila Proteins ; Genes, Insect ; Intracellular Signaling Peptides and Proteins ; Membrane Proteins/antagonists & inhibitors/genetics/*metabolism ; Molecular Sequence Data ; Mutation ; Phenotype ; *Phosphoproteins ; Proteins/genetics/*metabolism ; Proto-Oncogene Proteins/genetics/*metabolism ; Pupa/metabolism ; Receptors, Notch ; *Signal Transduction ; Wings, Animal/cytology/growth & development ; Wnt1 Protein
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    Liver failure and defective hepatocyte regeneration in interleukin-6-deficient mice (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: Liver regeneration stimulated by a loss of liver mass leads to hepatocyte and nonparenchymal cell proliferation and rapid restoration of liver parenchyma. Mice with targeted disruption of the interleukin-6 (IL-6) gene had impaired liver regeneration characterized by liver necrosis and failure. There was a blunted DNA synthetic response in hepatocytes of these mice but not in nonparenchymal liver cells. Furthermore, there were discrete G1 phase (prereplicative stage in the cell cycle) abnormalities including absence of STAT3 (signal transducer and activator of transcription protein 3) activation and depressed AP-1, Myc, and cyclin D1 expression. Treatment of IL-6-deficient mice with a single preoperative dose of IL-6 returned STAT3 binding, gene expression, and hepatocyte proliferation to near normal and prevented liver damage, establishing that IL-6 is a critical component of the regenerative response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cressman, D E -- Greenbaum, L E -- DeAngelis, R A -- Ciliberto, G -- Furth, E E -- Poli, V -- Taub, R -- DK44237/DK/NIDDK NIH HHS/ -- DK49210/DK/NIDDK NIH HHS/ -- DK49629/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1379-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Medicine, University of Pennsylvania School of Medicine, 705a Stellar-Chance, 422 Curie Boulevard, Philadelphia, PA 19104-6145, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910279" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cyclin D1 ; Cyclins/biosynthesis ; DNA/biosynthesis/metabolism ; DNA-Binding Proteins/metabolism ; G1 Phase ; Gene Expression Regulation ; Gene Targeting ; Genes, Immediate-Early ; Hepatectomy ; Interleukin-6/deficiency/genetics/pharmacology/*physiology ; Liver/*cytology/metabolism/pathology ; Liver Failure/*etiology/pathology ; *Liver Regeneration ; Mice ; Mice, Inbred C57BL ; Mitosis ; Mutation ; Necrosis ; Oncogene Proteins/biosynthesis ; Proto-Oncogene Proteins c-myc/biosynthesis ; STAT3 Transcription Factor ; Trans-Activators/metabolism ; Transcription Factor AP-1/biosynthesis
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 49
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    A neural tetraspanin, encoded by late bloomer, that facilitates synapse formation (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-29
    Description: Upon contacting its postsynaptic target, a neuronal growth cone transforms into a presynaptic terminal. A membrane component on the growth cone that facilitates synapse formation was identified by means of a complementary DNA-based screen followed by genetic analysis. The late bloomer (lbl) gene in Drosophila encodes a member of the tetraspanin family of cell surface proteins. LBL protein is transiently expressed on motor axons, growth cones, and terminal arbors. In lbl mutant embryos, the growth cone of the RP3 motoneuron contacts its target muscles, but synapse formation is delayed and neighboring motoneurons display an increase in ectopic sprouting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kopczynski, C C -- Davis, G W -- Goodman, C S -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1867-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, Berkeley 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596956" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Axons/metabolism/ultrastructure ; Cloning, Molecular ; Drosophila/embryology/genetics/physiology ; *Drosophila Proteins ; *Genes, Insect ; Membrane Proteins/chemistry/genetics/*physiology ; Molecular Sequence Data ; Motor Neurons/cytology/metabolism/*physiology ; Muscles/innervation ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*physiology ; Neuromuscular Junction/*physiology ; Presynaptic Terminals/*physiology/ultrastructure ; Signal Transduction
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    New virus variant killed Serengeti cats (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morell, V -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):596.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571120" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Distemper/transmission/*virology ; Distemper Virus, Canine/classification/*genetics ; Dogs ; *Genome, Viral ; Humans ; Lions/*virology ; Mutation ; Species Specificity ; Tanzania
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    DPC4, a candidate tumor suppressor gene at human chromosome 18q21.1 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: About 90 percent of human pancreatic carcinomas show allelic loss at chromosome 18q. To identify candidate tumor suppressor genes on 18q, a panel of pancreatic carcinomas were analyzed for convergent sites of homozygous deletion. Twenty-five of 84 tumors had homozygous deletions at 18q21.1, a site that excludes DCC (a candidate suppressor gene for colorectal cancer) and includes DPC4, a gene similar in sequence to a Drosophila melanogaster gene (Mad) implicated in a transforming growth factor-beta (TGF-beta)-like signaling pathway. Potentially inactivating mutations in DPC4 were identified in six of 27 pancreatic carcinomas that did not have homozygous deletions at 18q21.1. These results identify DPC4 as a candidate tumor suppressor gene whose inactivation may play a role in pancreatic and possibly other human cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hahn, S A -- Schutte, M -- Hoque, A T -- Moskaluk, C A -- da Costa, L T -- Rozenblum, E -- Weinstein, C L -- Fischer, A -- Yeo, C J -- Hruban, R H -- Kern, S E -- CA62924/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):350-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553070" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Division ; Chromosome Mapping ; *Chromosomes, Human, Pair 18 ; *DNA-Binding Proteins ; Gene Deletion ; Gene Expression ; *Genes, Tumor Suppressor ; Genetic Markers ; Humans ; Mice ; Molecular Sequence Data ; Mutation ; Neoplasm Transplantation ; Pancreatic Neoplasms/*genetics/pathology ; Proteins/chemistry/*genetics/physiology ; Signal Transduction ; Smad4 Protein ; *Trans-Activators ; Transforming Growth Factor beta/physiology ; Transplantation, Heterologous ; Tumor Cells, Cultured
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    Rapid degradation of the G1 cyclin Cln2 induced by CDK-dependent phosphorylation (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: Cyclins regulate the major cell cycle transitions in eukaryotes through association with cyclin-dependent protein kinases (CDKs). In yeast, G1 cyclins are essential, rate-limiting activators of cell cycle initiation. G1-specific accumulation of one G1 cyclin, Cln2, results from periodic gene expression coupled with rapid protein turnover. Site-directed mutagenesis of CLN2 revealed that its phosphorylation provides a signal that promotes rapid degradation. Cln2 phosphorylation is dependent on the Cdc28 protein kinase, the CDK that it activates. These findings suggest that Cln2 is rendered self-limiting by virtue of its ability to activate its cognate CDK subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lanker, S -- Valdivieso, M H -- Wittenberg, C -- GM43487/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1597-601.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599119" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; CDC28 Protein Kinase, S cerevisiae/*metabolism ; Cyclins/genetics/*metabolism ; Enzyme Activation ; Fungal Proteins/genetics/metabolism ; *G1 Phase ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Phenotype ; Phosphorylation ; Saccharomyces cerevisiae/cytology/metabolism ; Saccharomyces cerevisiae Proteins
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    Green light for steroid hormones (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, D W -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):370-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235-9046, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602524" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxo-5-alpha-Steroid 4-Dehydrogenase/chemistry ; Arabidopsis/genetics/*growth & development/metabolism ; *Arabidopsis Proteins ; Brassinosteroids ; Cholestanols/*metabolism ; Cytochrome P-450 Enzyme System/genetics/metabolism ; *Genes, Plant ; Light ; Mutation ; Plant Growth Regulators/biosynthesis/*metabolism ; Plant Proteins/chemistry/*genetics/metabolism ; Steroids, Heterocyclic/*metabolism
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    Mutant mice and worms help solve mysteries of olfaction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):500-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8928002" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/genetics/physiology ; Cyclic AMP/*physiology ; Inositol Phosphates/physiology ; Ion Channels/genetics/*physiology ; Mice ; Mice, Knockout ; Mutation ; Neurons, Afferent/physiology ; Odors ; Olfactory Receptor Neurons/*physiology ; Sensation/*physiology ; Sexual Behavior, Animal ; Signal Transduction ; Smell/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 55
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    AT-AC introns: an ATtACk on dogma (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mount, S M -- New York, N.Y. -- Science. 1996 Mar 22;271(5256):1690-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Maryland, College Park 20742-4415, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596928" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; Consensus Sequence ; Humans ; *Introns ; Molecular Sequence Data ; Mutation ; RNA Precursors/*genetics/metabolism ; *RNA Splicing ; RNA, Small Nuclear/metabolism ; Spliceosomes/metabolism
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    Altered growth and branching patterns in synpolydactyly caused by mutations in HOXD13 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-26
    Description: Hox genes regulate patterning during limb development. It is believed that they function in the determination of the timing and extent of local growth rates. Here, it is demonstrated that synpolydactyly, an inherited human abnormality of the hands and feet, is caused by expansions of a polyalanine stretch in the amino-terminal region of HOXD13. The homozygous phenotype includes the transformation of metacarpal and metatarsal bones to short carpal- and tarsal-like bones. The mutations identify the polyalanine stretch outside of the DNA binding domain of HOXD13 as a region necessary for proper protein function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Muragaki, Y -- Mundlos, S -- Upton, J -- Olsen, B R -- AR36819/AR/NIAMS NIH HHS/ -- AR36820/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Apr 26;272(5261):548-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614804" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 2 ; Cloning, Molecular ; Female ; Fingers/*abnormalities/embryology ; *Genes, Homeobox ; Genetic Linkage ; Homeodomain Proteins/chemistry/*genetics/physiology ; Humans ; Male ; Molecular Sequence Data ; Morphogenesis ; Multigene Family ; Mutation ; Pedigree ; Peptides/chemistry ; Polydactyly/embryology/*genetics/radiography ; Polymerase Chain Reaction ; Syndactyly/embryology/*genetics/radiography ; Toes/*abnormalities/embryology ; *Transcription Factors
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  • 57
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    Genetic clues to Alzheimer's disease (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dewji, N N -- Singer, S J -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):159-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Medicine, University of California at San Diego, La Jolla 92093-0322, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539612" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/metabolism ; Amyloid beta-Peptides/biosynthesis ; Amyloid beta-Protein Precursor/*genetics/metabolism ; Animals ; Brain/metabolism ; Caenorhabditis elegans/growth & development ; *Caenorhabditis elegans Proteins ; Drosophila/genetics/growth & development ; *Drosophila Proteins ; Eye Proteins/metabolism ; Female ; Helminth Proteins/genetics/metabolism ; Humans ; Membrane Glycoproteins/metabolism ; Membrane Proteins/*genetics/metabolism ; Mutation ; Neurons/metabolism ; Photoreceptor Cells, Invertebrate/growth & development/metabolism ; Presenilin-1 ; Presenilin-2 ; *Receptor Protein-Tyrosine Kinases ; Receptors, Notch ; *Receptors, Peptide ; Signal Transduction ; Vulva/growth & development/metabolism
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    An intriguing new lead on Huntington's disease (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1233-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638101" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*metabolism ; Glyceraldehyde-3-Phosphate Dehydrogenases/antagonists & inhibitors/*metabolism ; Glycolysis ; Humans ; Huntington Disease/genetics/*metabolism ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Nervous System Diseases/metabolism ; Nuclear Proteins/chemistry/genetics/*metabolism ; Peptides/metabolism ; Repetitive Sequences, Nucleic Acid
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Regulation of RAD53 by the ATM-like kinases MEC1 and TEL1 in yeast cell cycle checkpoint pathways (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: Mutants of the Saccharomyces cerevisiae ataxia telangiectasia mutated (ATM) homolog MEC1/SAD3/ESR1 were identified that could live only if the RAD53/SAD1 checkpoint kinase was overproduced. MEC1 and a structurally related gene, TEL1, have overlapping functions in response to DNA damage and replication blocks that in mutants can be provided by overproduction of RAD53. Both MEC1 and TEL1 were found to control phosphorylation of Rad53p in response to DNA damage. These results indicate that RAD53 is a signal transducer in the DNA damage and replication checkpoint pathways and functions downstream of two members of the ATM lipid kinase family. Because several members of this pathway are conserved among eukaryotes, it is likely that a RAD53-related kinase will function downstream of the human ATM gene product and play an important role in the mammalian response to DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez, Y -- Desany, B A -- Jones, W J -- Liu, Q -- Wang, B -- Elledge, S J -- DK07696/DK/NIDDK NIH HHS/ -- GM44664/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):357-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Mars McLean Department of Biochemistry, Department of Molecular and Human Genetics, Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553072" target="_blank"〉PubMed〈/a〉
    Keywords: Ataxia Telangiectasia Mutated Proteins ; Base Sequence ; *Cell Cycle ; *Cell Cycle Proteins ; Checkpoint Kinase 2 ; *DNA Damage ; DNA Replication ; DNA-Binding Proteins ; Fungal Proteins/*genetics/metabolism ; Gene Expression Regulation, Fungal ; *Genes, Fungal ; Intracellular Signaling Peptides and Proteins ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/*genetics/metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/genetics/metabolism ; Saccharomyces cerevisiae/cytology/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Tumor Suppressor Proteins
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    Researchers nail down leptin receptor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1996 Feb 16;271(5251):913.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8584929" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carrier Proteins/biosynthesis/chemistry/*genetics ; Chromosome Mapping ; Cloning, Molecular ; Diabetes Mellitus/*genetics ; Humans ; Leptin ; Mice ; Mutation ; Obesity/*genetics ; Proteins/genetics ; RNA, Messenger/genetics ; Rats ; *Receptors, Cell Surface ; Receptors, Cytokine/biosynthesis/chemistry/*genetics ; Receptors, Leptin
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    Dating the cenancester of organisms (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hasegawa, M -- Fitch, W M -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1750; author reply 1751-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8984636" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Evolution, Molecular ; Models, Statistical ; Mutation ; Proteins/*chemistry/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Estimating the age of the common ancestor of men from the ZFY intron (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Donnelly, P -- Tavare, S -- Balding, D J -- Griffiths, R C -- GM36232/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 May 31;272(5266):1357-9; author reply 1361-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650551" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA-Binding Proteins/*genetics ; *Genetics, Population ; Hominidae/*genetics ; Humans ; Introns/*genetics ; Kruppel-Like Transcription Factors ; Male ; Mutation ; Polymorphism, Genetic ; Population Density ; Probability ; Time Factors ; Transcription Factors/*genetics ; Y Chromosome/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Change of a catalytic reaction carried out by a DNA replication protein (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-01
    Description: The RepA protein of plasmid pC194 initiates and terminates rolling circle replication. At initiation, it forms a 5'-phosphotyrosyl DNA link, whereas at termination, a glutamate residue directs hydrolytic cleavage of the newly synthesized origin, and the resulting 3'-hydroxyl group undergoes transesterification with the phosphotyrosine link. The protein is thus released from DNA, and the termination is uncoupled from reinitiation of replication. Replacement of the glutamate with tyrosine in RepA altered this mechanism, so that termination occurred by two successive transesterifications and became coupled to reinitiation. This result suggests that various enzymes involved in DNA cleavage and rejoining may have similar mechanistic and evolutionary roots.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noirot-Gros, M F -- Ehrlich, S D -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):777-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetique Microbienne, Institut National de la Recherche Agronomique, Domaine de Vilvert, 78352 Jouy en Josas Cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864116" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage phi X 174 ; Binding Sites ; *DNA Helicases ; *DNA Replication ; DNA, Bacterial/*metabolism ; DNA, Single-Stranded/metabolism ; DNA, Viral/metabolism ; *DNA-Binding Proteins ; Esterification ; Evolution, Molecular ; Glutamic Acid/metabolism ; Hydrolysis ; Mutation ; Plasmids ; Proteins/chemistry/genetics/*metabolism ; *Trans-Activators ; Tyrosine/metabolism ; Viral Proteins/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Rho1p, a yeast protein at the interface between cell polarization and morphogenesis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-12
    Description: The enzyme that catalyzes the synthesis of the major structural component of the yeast cell wall, beta(1--〉3)-D-glucan synthase (also known as 1,3-beta-glucan synthase), requires a guanosine triphosphate (GTP) binding protein for activity. The GTP binding protein was identified as Rho1p. The rho1 mutants were defective in GTP stimulation of glucan synthase, and the defect was corrected by addition of purified or recombinant Rho1p. A protein missing in purified preparations from a rho1 strain was identified as Rho1p. Rho1p also regulates protein kinase C, which controls a mitogen-activated protein kinase cascade. Experiments with a dominant positive PKC1 gene showed that the two effects of Rho1p are independent of each other. The colocalization of Rho1p with actin patches at the site of bud emergence and the role of Rho1p in cell wall synthesis emphasize the importance of Rho1p in polarized growth and morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drgonova, J -- Drgon, T -- Tanaka, K -- Kollar, R -- Chen, G C -- Ford, R A -- Chan, C S -- Takai, Y -- Cabib, E -- New York, N.Y. -- Science. 1996 Apr 12;272(5259):277-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory od Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602514" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Polarity ; Cell Wall/metabolism ; GTP Phosphohydrolases/*metabolism ; GTP-Binding Proteins/genetics/*metabolism ; Glucans/biosynthesis ; Glucosyltransferases/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Triphosphate/metabolism ; *Membrane Proteins ; Morphogenesis ; Mutation ; Protein Kinase C/metabolism ; Recombinant Proteins/pharmacology ; Saccharomyces cerevisiae/cytology/genetics/growth & development/*metabolism ; Saccharomyces cerevisiae Proteins ; *Schizosaccharomyces pombe Proteins ; Temperature ; *beta-Glucans ; *rho GTP-Binding Proteins
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    A cyclophilin function in Hsp90-dependent signal transduction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: Cpr6 and Cpr7, the Saccharomyces cerevisiae homologs of cyclophilin-40 (CyP-40), were shown to form complexes with Hsp90, a protein chaperone that functions in several signal transduction pathways. Deletion of CPR7 caused severe growth defects when combined with mutations that decrease the amount of Hsp90 or Sti1, another component of the Hsp90 chaperone machinery. The activities of two heterologous Hsp90-dependent signal transducers expressed in yeast, glucocorticoid receptor and pp60(v-src) kinase, were adversely affected by cpr7 null mutations. These results suggest that CyP-40 cyclophilins play a general role in Hsp90-dependent signal transduction pathways under normal growth conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duina, A A -- Chang, H C -- Marsh, J A -- Lindquist, S -- Gaber, R F -- GM25874/GM/NIGMS NIH HHS/ -- GM45739/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1713-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2153 Sheridan Road, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939862" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/genetics/metabolism/*physiology ; Carrier Proteins/genetics/metabolism/*physiology ; *Cyclophilins ; Fungal Proteins/genetics/metabolism/*physiology ; HSP90 Heat-Shock Proteins/genetics/metabolism/*physiology ; Heat-Shock Proteins ; Molecular Chaperones/genetics/metabolism/*physiology ; Mutation ; Oncogene Protein pp60(v-src)/metabolism ; *Peptidylprolyl Isomerase ; Proto-Oncogene Proteins pp60(c-src)/metabolism ; Receptors, Glucocorticoid/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/metabolism/*physiology ; Saccharomyces cerevisiae Proteins ; *Signal Transduction
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    Conditional circadian dysfunction of the Arabidopsis early-flowering 3 mutant (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-01
    Description: Photoperiodic responses, such as the daylength-dependent control of reproductive development, are associated with a circadian biological clock. The photoperiod-insensitive early-flowering 3 (elf3) mutant of Arabidopsis thaliana lacks rhythmicity in two distinct circadian-regulated processes. This defect was apparent only when plants were assayed under constant light conditions. elf3 mutants retain rhythmicity in constant dark and anticipate light/dark transitions under most light/dark regimes. The conditional arrhythmic phenotype suggests that the circadian pacemaker is intact in darkness in elf3 mutant plants, but the transduction of light signals to the circadian clock is impaired.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hicks, K A -- Millar, A J -- Carre, I A -- Somers, D E -- Straume, M -- Meeks-Wagner, D R -- Kay, S A -- 1R01GM46006/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 1;274(5288):790-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8864121" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/growth & development/*physiology ; *Circadian Rhythm ; Darkness ; Gene Expression Regulation, Plant ; Genes, Plant ; *Light ; Movement ; Mutation ; Phenotype ; *Photoperiod ; Photosynthetic Reaction Center Complex Proteins/genetics ; Plant Leaves/physiology ; Plants, Genetically Modified
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    Enhanced fidelity of 3TC-selected mutant HIV-1 reverse transcriptase (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-01
    Description: Monotherapy with (-)2',3'-dideoxy-3'-thiacytidine (3TC) leads to the appearance of a drug-resistant variant of human immunodeficiency virus-type 1 (HIV-1) with the methionine-184 --〉 valine (M184V) substitution in the reverse transcriptase (RT). Despite resulting drug resistance, treatment for more than 48 weeks is associated with a lower plasma viral burden than that at baseline. Studies to investigate this apparent contradiction revealed the following. (i) Titers of HIV-neutralizing antibodies remained stable in 3TC-treated individuals in contrast to rapid declines in those treated with azidothymidine (AZT). (ii) Unlike wild-type HIV, growth of M184V HIV in cell culture in the presence of d4T, AZT, Nevirapine, Delavirdine, or Saquinavir did not select for variants displaying drug resistance. (iii) There was an increase in fidelity of nucleotide insertion by the M184V mutant compared with wild-type enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wainberg, M A -- Drosopoulos, W C -- Salomon, H -- Hsu, M -- Borkow, G -- Parniak, M -- Gu, Z -- Song, Q -- Manne, J -- Islam, S -- Castriota, G -- Prasad, V R -- P30 AI-27741/AI/NIAID NIH HHS/ -- R01 AI0-30861/AI/NIAID NIH HHS/ -- UO1AI-24845/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Mar 1;271(5253):1282-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉McGill AIDS Centre, Jewish General Hospital, Montreal, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638110" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/*pharmacology/therapeutic use ; Base Composition ; Base Sequence ; Deoxyribonucleotides/metabolism ; Drug Resistance, Microbial ; HIV Antibodies/blood/immunology ; HIV Infections/drug therapy/*virology ; HIV Protease Inhibitors/pharmacology ; HIV Reverse Transcriptase ; HIV-1/drug effects/*enzymology/genetics/immunology/physiology ; Humans ; Isoquinolines/pharmacology ; Lamivudine ; Molecular Sequence Data ; Mutation ; Neutralization Tests ; Quinolines/pharmacology ; RNA-Directed DNA Polymerase/drug effects/*genetics/metabolism ; Reverse Transcriptase Inhibitors/*pharmacology/therapeutic use ; Saquinavir ; Virus Replication/drug effects ; Zalcitabine/*analogs & derivatives/pharmacology/therapeutic use
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    Population dynamics of immune responses to persistent viruses (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-05
    Description: Mathematical models, which are based on a firm understanding of biological interactions, can provide nonintuitive insights into the dynamics of host responses to infectious agents and can suggest new avenues for experimentation. Here, a simple mathematical approach is developed to explore the relation between antiviral immune responses, virus load, and virus diversity. The model results are compared to data on cytotoxic T cell responses and viral diversity in infections with the human T cell leukemia virus (HTLV-1) and the human immunodeficiency virus (HIV-1).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nowak, M A -- Bangham, C R -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):74-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Oxford, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600540" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Viral/immunology ; Antigenic Variation ; Antigens, Viral/immunology ; Cytokines/immunology ; Cytotoxicity, Immunologic ; Epitopes/immunology ; Genetic Variation ; HIV Infections/immunology/virology ; HIV-1/immunology/physiology ; HTLV-I Infections/immunology/virology ; Human T-lymphotropic virus 1/genetics/immunology/physiology ; Humans ; *Models, Biological ; Mutation ; Population Dynamics ; T-Lymphocytes, Cytotoxic/*immunology ; Virus Diseases/*immunology/virology ; Virus Physiological Phenomena ; Virus Replication ; Viruses/genetics/*immunology
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    Lysogenic conversion by a filamentous phage encoding cholera toxin (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-28
    Description: Vibrio cholerae, the causative agent of cholera, requires two coordinately regulated factors for full virulence: cholera toxin (CT), a potent enterotoxin, and toxin-coregulated pili (TCP), surface organelles required for intestinal colonization. The structural genes for CT are shown here to be encoded by a filamentous bacteriophage (designated CTXphi), which is related to coliphage M13. The CTXphi genome chromosomally integrated or replicated as a plasmid. CTXphi used TCP as its receptor and infected V. cholerae cells within the gastrointestinal tracts of mice more efficiently than under laboratory conditions. Thus, the emergence of toxigenic V. cholerae involves horizontal gene transfer that may depend on in vivo gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waldor, M K -- Mekalanos, J J -- AI01321/AI/NIAID NIH HHS/ -- AI18045/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 28;272(5270):1910-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Shipley Institute of Medicine, Harvard Medical School, Boston, Massachusetts 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658163" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacteriophages/*genetics/physiology ; Base Sequence ; Cholera/*microbiology ; Cholera Toxin/*genetics ; DNA Primers ; Digestive System/microbiology ; Fimbriae, Bacterial/physiology/virology ; Gene Expression ; Genes, Bacterial ; *Lysogeny ; Mice ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Transduction, Genetic ; Vibrio cholerae/genetics/*pathogenicity/*virology ; Virulence/genetics
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    Arabidopsis AUX1 gene: a permease-like regulator of root gravitropism (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-16
    Description: The plant hormone auxin regulates various developmental processes including root formation, vascular development, and gravitropism. Mutations within the AUX1 gene confer an auxin-resistant root growth phenotype and abolish root gravitropic curvature. Polypeptide sequence similarity to amino acid permeases suggests that AUX1 mediates the transport of an amino acid-like signaling molecule. Indole-3-acetic acid, the major form of auxin in higher plants, is structurally similar to tryptophan and is a likely substrate for the AUX1 gene product. The cloned AUX1 gene can restore the auxin-responsiveness of transgenic aux1 roots. Spatially, AUX1 is expressed in root apical tissues that regulate root gravitropic curvature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bennett, M J -- Marchant, A -- Green, H G -- May, S T -- Ward, S P -- Millner, P A -- Walker, A R -- Schulz, B -- Feldmann, K A -- New York, N.Y. -- Science. 1996 Aug 16;273(5277):948-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8688077" target="_blank"〉PubMed〈/a〉
    Keywords: 2,4-Dichlorophenoxyacetic Acid/pharmacology ; Amino Acid Sequence ; Amino Acid Transport Systems ; Amino Acids/metabolism ; Arabidopsis/chemistry/*genetics/growth & development/metabolism ; *Arabidopsis Proteins ; Biological Transport ; Cloning, Molecular ; DNA, Bacterial/genetics ; *Genes, Plant ; Genetic Complementation Test ; *Gravitropism ; Indoleacetic Acids/metabolism/pharmacology ; Membrane Transport Proteins/chemistry ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Plant Proteins/chemistry/*genetics/metabolism ; Plant Roots/*growth & development/metabolism ; Sequence Alignment ; Signal Transduction
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    rad-dependent response of the chk1-encoded protein kinase at the DNA damage checkpoint (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: Exposure of eukaryotic cells to agents that generate DNA damage results in transient arrest of progression through the cell cycle. In fission yeast, the DNA damage checkpoint associated with cell cycle arrest before mitosis requires the protein kinase p56chk1. DNA damage induced by ultraviolet light, gamma radiation, or a DNA-alkylating agent has now been shown to result in phosphorylation of p56chk1. This phosphorylation decreased the mobility of p56chk1 on SDS-polyacrylamide gel electrophoresis and was abolished by a mutation in the p56chk1 catalytic domain, suggesting that it might represent autophosphorylation. Phosphorylation of p56chk1 did not occur when other checkpoint genes were inactive. Thus, p56chk1 appears to function downstream of several of the known Schizosaccharomyces pombe checkpoint gene products, including that encoded by rad3+, a gene with sequence similarity to the ATM gene mutated in patients with ataxia telangiectasia. The phosphorylation of p56chk1 provides an assayable biochemical response to activation of the DNA damage checkpoint in the G2 phase of the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walworth, N C -- Bernards, R -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):353-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Carcinogenesis, Netherlands Cancer Institute, Amsterdam.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553071" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/genetics ; Ataxia Telangiectasia Mutated Proteins ; Base Sequence ; Cell Cycle Proteins ; *DNA Damage ; DNA Helicases/genetics ; DNA Replication ; DNA, Fungal/metabolism/radiation effects ; DNA-Binding Proteins ; Electrophoresis, Polyacrylamide Gel ; *G2 Phase ; Genes, Fungal ; Humans ; *Mitosis ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/chemistry/genetics/*metabolism ; *Protein-Serine-Threonine Kinases ; Proteins/genetics ; Recombinant Fusion Proteins/chemistry/metabolism ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/*cytology/genetics/radiation effects ; Tumor Suppressor Proteins ; Ultraviolet Rays
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    Cdc13p: a single-strand telomeric DNA-binding protein with a dual role in yeast telomere maintenance (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-11
    Description: The CDC13 gene has previously been implicated in the maintenance of telomere integrity in Saccharomyces cerevisiae. With the use of two classes of mutations, here it is shown that CDC13 has two discrete roles at the telomere. The cdc13-2est mutation perturbs a function required in vivo for telomerase regulation but not in vitro for enzyme activity, whereas cdc13-1ts defines a separate essential role at the telomere. In vitro, purified Cdc13p binds to single-strand yeast telomeric DNA. Therefore, Cdc13p is a telomere-binding protein required to protect the telomere and mediate access of telomerase to the chromosomal terminus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nugent, C I -- Hughes, T R -- Lue, N F -- Lundblad, V -- New York, N.Y. -- Science. 1996 Oct 11;274(5285):249-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Human Genetics and Cell and Molecular Biology Program, Baylor College of Medicine, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8824190" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Base Sequence ; Cloning, Molecular ; Cyclin B ; Cyclins/genetics/*metabolism ; DNA, Fungal/metabolism ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/*metabolism ; Fungal Proteins/genetics ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Phenotype ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Telomerase/genetics/*metabolism ; Telomere/*metabolism
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    Role of the Yersinia pestis hemin storage (hms) locus in the transmission of plague by fleas (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-19
    Description: Yersinia pestis, the cause of bubonic plague, is transmitted by the bites of infected fleas. Biological transmission of plague depends on blockage of the foregut of the flea by a mass of plague bacilli. Blockage was found to be dependent on the hemin storage (hms) locus. Yersinia pestis hms mutants established long-term infection of the flea's midgut but failed to colonize the proventriculus, the site in the foregut where blockage normally develops. Thus, the hms locus markedly alters the course of Y. pestis infection in its insect vector, leading to a change in blood-feeding behavior and to efficient transmission of plague.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hinnebusch, B J -- Perry, R D -- Schwan, T G -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):367-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Microbial Structure and Function, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662526" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Adhesion ; Digestive System/microbiology ; Female ; *Genes, Bacterial ; Hemin/*metabolism ; Insect Vectors/*microbiology ; Male ; Mutation ; Plague/*transmission ; Proventriculus/microbiology ; Siphonaptera/*microbiology ; Virulence ; Yersinia pestis/genetics/growth & development/metabolism/*pathogenicity
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    Emergence of preferred structures in a simple model of protein folding (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-02
    Description: Protein structures in nature often exhibit a high degree of regularity (for example, secondary structure and tertiary symmetries) that is absent from random compact conformations. With the use of a simple lattice model of protein folding, it was demonstrated that structural regularities are related to high "designability" and evolutionary stability. The designability of each compact structure is measured by the number of sequences that can design the structure-that is, sequences that possess the structure as their nondegenerate ground state. Compact structures differ markedly in terms of their designability; highly designable structures emerge with a number of associated sequences much larger than the average. These highly designable structures possess "proteinlike" secondary structure and even tertiary symmetries. In addition, they are thermodynamically more stable than other structures. These results suggest that protein structures are selected in nature because they are readily designed and stable against mutations, and that such a selection simultaneously leads to thermodynamic stability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, H -- Helling, R -- Tang, C -- Wingreen, N -- New York, N.Y. -- Science. 1996 Aug 2;273(5275):666-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NEC Research Institute, 4 Independence Way, Princeton, NJ 08540, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662562" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acid Sequence ; Evolution, Molecular ; *Models, Molecular ; Mutation ; *Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*chemistry/genetics ; Thermodynamics
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    A role for brassinosteroids in light-dependent development of Arabidopsis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-19
    Description: Although steroid hormones are important for animal development, the physiological role of plant steroids is unknown. The Arabidopsis DET2 gene encodes a protein that shares significant sequence identity with mammalian steroid 5 alpha-reductases. A mutation of glutamate 204, which is absolutely required for the activity of human steroid reductase, abolishes the in vivo activity of DET2 and leads to defects in light-regulated development that can be ameliorated by application of a plant steroid, brassinolide. Thus, DET2 may encode a reductase in the brassinolide biosynthetic pathway, and brassinosteroids may constitute a distinct class of phytohormones with an important role in light-regulated development of higher plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, J -- Nagpal, P -- Vitart, V -- McMorris, T C -- Chory, J -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):398-401.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Biology Laboratory, Salk Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602526" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxo-5-alpha-Steroid 4-Dehydrogenase/chemistry ; Amino Acid Sequence ; Animals ; Arabidopsis/genetics/*growth & development/metabolism ; *Arabidopsis Proteins ; Brassinosteroids ; Cholestanols/*metabolism/pharmacology ; Chromosome Mapping ; *Genes, Plant ; Humans ; Light ; Molecular Sequence Data ; Mutation ; Oxidation-Reduction ; Phenotype ; Plant Growth Regulators/biosynthesis/*metabolism ; Plant Proteins/*genetics ; Rats ; Sequence Alignment ; Signal Transduction ; Steroids, Heterocyclic/*metabolism/pharmacology
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    RAG mutations in human B cell-negative SCID (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-04
    Description: Patients with human severe combined immunodeficiency (SCID) can be divided into those with B lymphocytes (B+ SCID) and those without (B- SCID). Although several genetic causes are known for B+ SCID, the etiology of B- SCID has not been defined. Six of 14 B- SCID patients tested were found to carry a mutation of the recombinase activating gene 1 (RAG-1), RAG-2, or both. This mutation resulted in a functional inability to form antigen receptors through genetic recombination and links a defect in one of the site-specific recombination systems to a human disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwarz, K -- Gauss, G H -- Ludwig, L -- Pannicke, U -- Li, Z -- Lindner, D -- Friedrich, W -- Seger, R A -- Hansen-Hagge, T E -- Desiderio, S -- Lieber, M R -- Bartram, C R -- New York, N.Y. -- Science. 1996 Oct 4;274(5284):97-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Molecular Biology, University of Ulm, D-89070 Ulm, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8810255" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/immunology ; Cell Line ; Consanguinity ; *DNA-Binding Proteins ; Female ; Genes, Immunoglobulin ; Genes, Recessive ; *Homeodomain Proteins ; Humans ; Immunophenotyping ; Male ; Mutation ; Nuclear Proteins ; Polymorphism, Single-Stranded Conformational ; Proteins/*genetics ; Receptors, Antigen, T-Cell/genetics ; Recombination, Genetic ; Sequence Deletion ; Severe Combined Immunodeficiency/*genetics/immunology ; Transfection
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    The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-02-23
    Description: The alpha subunit of p21(RAS) farnesyltransferase (FNTA), which is also shared by geranylgeranyltransferase, was isolated as a specific cytoplasmic interactor of the transforming growth factor-beta (TGF-beta) and activin type I receptors with the use of the yeast two-hybrid system. FNTA interacts specifically with ligand-free TGF-beta type l receptor but is phosphorylated and released upon ligand binding. Furthermore, the release is dependent on the kinase activity of the TGF-beta type II receptor. Thus, the growth inhibitory and differentiative pathways activated by TGF-beta and activin involve novel mechanisms of serine-threonine receptor phosphorylation-dependent release of cytoplasmic interactors and regulation of the activation of small G proteins, such as p21(RAS).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, T -- Danielson, P D -- Li, B Y -- Shah, P C -- Kim, S D -- Donahoe, P K -- HD28138/HD/NICHD NIH HHS/ -- R01 HD3081/HD/NICHD NIH HHS/ -- R01 HD32112/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1996 Feb 23;271(5252):1120-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pediatric Surgical Research Laboratories, Massachusetts General Hospital, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599089" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors ; *Activin Receptors, Type I ; Activins ; *Alkyl and Aryl Transferases ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Humans ; Inhibins/*metabolism ; Ligands ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Receptors, Growth Factor/metabolism ; Receptors, Transforming Growth Factor beta/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transferases/*metabolism ; Transforming Growth Factor beta/*metabolism
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    Mad cow disease. Scant data cause widespread concern (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, C -- New York, N.Y. -- Science. 1996 Mar 29;271(5257):1798.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596943" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Animals ; Brain/pathology ; Cattle ; Creutzfeldt-Jakob Syndrome/genetics/pathology/*transmission ; Encephalopathy, Bovine Spongiform/*transmission ; Food Contamination ; Humans ; *Meat ; Mutation ; Prions/genetics ; Zoonoses
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    CD5-mediated negative regulation of antigen receptor-induced growth signals in B-1 B cells (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-13
    Description: A subset of B lymphocytes present primarily in the peritoneal and pleural cavities is defined by the expression of CD5 and is elevated in autoimmune diseases. Upon signaling through membrane immunoglobulin M (mIgM), splenic B lymphocytes (B-2) proliferate, whereas peritoneal B cells (B-1) undergo apoptosis. However, in CD5-deficient mice, B-1 cells responded to mIgM crosslinking by developing a resistance to apoptosis and entering the cell cycle. In wild-type B-1 cells, prevention of association between CD5 and mIgM rescued their growth response to mIgM crosslinking. Thus the B cell receptor-mediated signaling is negatively regulated by CD5 in normal B-1 cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bikah, G -- Carey, J -- Ciallella, J R -- Tarakhovsky, A -- Bondada, S -- AG05731/AG/NIA NIH HHS/ -- AI21490/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 13;274(5294):1906-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology and Center on Aging, University of Kentucky, Lexington, KY 40536, USA. sbonda@pop.uky.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8943203" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD5/*physiology ; Apoptosis ; B-Lymphocyte Subsets/*cytology/*immunology/metabolism ; Calcium/metabolism ; Cell Division ; Cell Nucleus/metabolism ; Cross-Linking Reagents ; Female ; Immunoglobulin M/immunology/metabolism ; *Lymphocyte Activation ; Male ; Mice ; Mice, Inbred C57BL ; Mutation ; NF-kappa B/metabolism ; Peritoneal Cavity/cytology ; Receptors, Antigen, B-Cell/immunology/metabolism/*physiology ; *Signal Transduction
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    Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARgamma (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-20
    Description: Adipocyte differentiation is an important component of obesity and other metabolic diseases. This process is strongly inhibited by many mitogens and oncogenes. Several growth factors that inhibit fat cell differentiation caused mitogen-activated protein (MAP) kinase-mediated phosphorylation of the dominant adipogenic transcription factor peroxisome proliferator-activated receptor gamma (PPARgamma) and reduction of its transcriptional activity. Expression of PPARgamma with a nonphosphorylatable mutation at this site (serine-112) yielded cells with increased sensitivity to ligand-induced adipogenesis and resistance to inhibition of differentiation by mitogens. These results indicate that covalent modification of PPARgamma by serum and growth factors is a major regulator of the balance between cell growth and differentiation in the adipose cell lineage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hu, E -- Kim, J B -- Sarraf, P -- Spiegelman, B M -- R37DK31405/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 20;274(5295):2100-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute and Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8953045" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adipocytes/*cytology/metabolism ; Animals ; Blood ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism ; Cell Differentiation ; Cell Line ; Enzyme Inhibitors/pharmacology ; Epidermal Growth Factor/pharmacology ; Flavonoids/pharmacology ; Insulin/pharmacology ; Ligands ; Mice ; Mitogens/pharmacology ; Mutation ; Phosphorylation ; Rats ; Receptors, Cytoplasmic and Nuclear/chemistry/genetics/*metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription Factors/chemistry/genetics/*metabolism ; Transcription, Genetic/drug effects ; Transfection
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    Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-26
    Description: A subset of individuals with familial amyotrophic lateral sclerosis (FALS) possesses dominantly inherited mutations in the gene that encodes copper-zinc superoxide dismutase (CuZnSOD). A4V and G93A, two of the mutant enzymes associated with FALS, were shown to catalyze the oxidation of a model substrate (spin trap 5,5'-dimethyl-1-pyrroline N-oxide) by hydrogen peroxide at a higher rate than that seen with the wild-type enzyme. Catalysis of this reaction by A4V and G93A was more sensitive to inhibition by the copper chelators diethyldithiocarbamate and penicillamine than was catalysis by wild-type CuZnSOD. The same two chelators reversed the apoptosis-inducing effect of mutant enzymes expressed in a neural cell line. These results suggest that oxidative reactions catalyzed by mutant CuZnSOD enzymes initiate the neuropathologic changes in FALS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wiedau-Pazos, M -- Goto, J J -- Rabizadeh, S -- Gralla, E B -- Roe, J A -- Lee, M K -- Valentine, J S -- Bredesen, D E -- AG12282/AG/NIA NIH HHS/ -- DK46828/DK/NIDDK NIH HHS/ -- GM28222/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):515-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of California, Los Angeles 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560268" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*enzymology/genetics ; Animals ; Apoptosis/drug effects ; Binding Sites ; Catalysis ; Cell Line ; Chelating Agents/pharmacology ; Copper/metabolism ; Cyclic N-Oxides/metabolism ; Ditiocarb/pharmacology ; Humans ; Hydrogen Peroxide/metabolism ; Mutation ; Oxidation-Reduction ; Penicillamine/pharmacology ; Rats ; Superoxide Dismutase/genetics/*metabolism
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    Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Mutations that eliminate KatG catalase-peroxidase activity prevent activation of isoniazid and are a major mechanism of resistance to this principal drug for the treatment of Mycobacterium tuberculosis infections. However, the loss of KatG activity in clinical isolates seemed paradoxical because KatG is considered an important factor for the survival of the organism. Expression of either KatG or the recently identified alkyl hydroperoxidase AhpC was sufficient to protect bacilli against the toxic effects of organic peroxides. To survive during infection, isoniazid-resistant KatG mutants have apparently compensated for the loss of KatG catalase-peroxidase activity by a second mutation, resulting in hyperexpression of AhpC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sherman, D R -- Mdluli, K -- Hickey, M J -- Arain, T M -- Morris, S L -- Barry, C E 3rd -- Stover, C K -- Z01 AI000783-11/Intramural NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1641-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Tuberculosis and Molecular Microbiology, PathoGenesis Corporation, Seattle, Washington 98119, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658136" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antitubercular Agents/*pharmacology ; *Bacterial Proteins ; Base Sequence ; Cloning, Molecular ; DNA, Bacterial ; Drug Resistance, Microbial/genetics ; Drug Synergism ; Enzyme Induction ; Gene Expression Regulation, Bacterial ; Hydrogen Peroxide/pharmacology ; Isoniazid/*pharmacology ; Molecular Sequence Data ; Mutation ; Mycobacterium bovis/drug effects/genetics ; Mycobacterium tuberculosis/*drug effects/*genetics ; Oxidoreductases/*genetics ; Peroxidases/biosynthesis/genetics/metabolism ; Peroxiredoxins ; Promoter Regions, Genetic
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  • 83
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    Organization of diphtheria toxin T domain in bilayers: a site-directed spin labeling study (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-09
    Description: The diphtheria toxin transmembrane (T) domain was spin-labeled at consecutive residues in a helical segment, TH9. After binding of the T domain to membranes at low pH, the nitroxide side chains generated by spin labeling were measured with respect to their frequency of collision with polar and nonpolar reagents. The data showed that the helical structure of TH9 in solution is conserved, with one face exposed to water and the other to the hydrophobic interior of the bilayer. Measurement of the depth of the nitroxide side chains from the membrane surfaces revealed an incremental change of about 5 angstroms per turn, which is consistent with a transmembrane orientation of an alpha helix. These results indicate that the helix forms the lining of a transmembrane water-filled channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oh, K J -- Zhan, H -- Cui, C -- Hideg, K -- Collier, R J -- Hubbell, W L -- AI-22021/AI/NIAID NIH HHS/ -- AI-22848/AI/NIAID NIH HHS/ -- EY-05216/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1996 Aug 9;273(5276):810-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-7008, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8670424" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Diphtheria Toxin/*chemistry/genetics ; Edetic Acid/analogs & derivatives ; Electron Spin Resonance Spectroscopy ; Hydrogen-Ion Concentration ; *Lipid Bilayers ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nickel ; Oxygen ; Phospholipids ; *Protein Structure, Secondary ; *Protein Structure, Tertiary ; Spin Labels
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  • 84
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    DPY-26, a link between dosage compensation and meiotic chromosome segregation in the nematode (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: The DPY-26 protein is required in the nematode Caenorhabditis elegans for X-chromosome dosage compensation as well as for proper meiotic chromosome segregation. DPY-26 was shown to mediate both processes through its association with chromosomes. In somatic cells, DPY-26 associates specifically with hermaphrodite X chromosomes to reduce their transcript levels. In germ cells, DPY-26 associates with all meiotic chromosomes to mediate its role in chromosome segregation. The X-specific localization of DPY-26 requires two dosage compensation proteins (DPY-27 and DPY-30) and two proteins that coordinately control both sex determination and dosage compensation (SDC-2 and SDC-3).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lieb, J D -- Capowski, E E -- Meneely, P -- Meyer, B J -- GM30702/GM/NIGMS NIH HHS/ -- HD24324/HD/NICHD NIH HHS/ -- T32 GM07127/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1732-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939869" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/embryology/genetics/*physiology ; *Caenorhabditis elegans Proteins ; Carrier Proteins/physiology ; Cell Nucleus/chemistry ; Chromosomes/*physiology ; Disorders of Sex Development ; *Dosage Compensation, Genetic ; Embryonic Development ; Female ; Gene Expression ; Genes, Helminth ; Germ Cells/physiology ; Helminth Proteins/analysis/genetics/*physiology ; Male ; *Meiosis ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/physiology ; X Chromosome/physiology
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  • 85
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    Molecular genetics of human blood pressure variation (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: Hypertension is a common multifactorial vascular disorder of largely unknown cause. Recognition that hypertension is in part genetically determined has motivated studies to identify mutations that confer susceptibility. Thus far, mutations in at least 10 genes have been shown to alter blood pressure; most of these are rare mutations imparting large quantitative effects that either raise or lower blood pressure. These mutations alter blood pressure through a common pathway, changing salt and water reabsorption in the kidney. These findings demonstrate the utility of molecular genetic approaches to the understanding of blood pressure variation and may provide insight into the physiologic mechanisms underlying common forms of hypertension.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lifton, R P -- New York, N.Y. -- Science. 1996 May 3;272(5262):676-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614826" target="_blank"〉PubMed〈/a〉
    Keywords: Absorption ; Animals ; Blood Pressure/*genetics ; Chromosome Mapping ; Genetic Variation ; Humans ; Hypertension/*genetics/metabolism/physiopathology ; Hypotension/*genetics/metabolism/physiopathology ; Kidney/metabolism ; Mutation ; Renin-Angiotensin System/physiology ; Sodium/metabolism
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  • 86
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    Premature aging gene discovered (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1996 Apr 12;272(5259):193-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602501" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Chromosome Mapping ; Chromosomes, Human, Pair 8/*genetics ; DNA Damage ; DNA Helicases/*genetics/metabolism ; Exodeoxyribonucleases ; Female ; Humans ; Male ; Mutation ; Neoplasms/etiology ; RecQ Helicases ; Sequence Analysis, DNA ; Werner Syndrome/complications/*genetics
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  • 87
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    Mechanisms and evolution of aging (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lithgow, G J -- Kirkwood, T B -- New York, N.Y. -- Science. 1996 Jul 5;273(5271):80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biologicag Gerontology Group, University of Manchester, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658201" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Animals ; *Biological Evolution ; Caenorhabditis elegans/*genetics/*physiology ; *Genes, Helminth ; Longevity/genetics ; Mutation ; Oxidative Stress ; Temperature ; Ultraviolet Rays
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  • 88
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    Effect of polymorphism in the Drosophila regulatory gene Ultrabithorax on homeotic stability (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-12
    Description: Development is buffered against unpredictable environmental and genetic effects. Here, a molecular genetic analysis of one type of developmental homeostasis, the establishment of thoracic segmental identity under the control of the Ultrabithorax (Ubx) gene in Drosophila melanogaster, is presented. Flies were artificially selected for differential sensitivity to the induction of bithorax phenocopies by ether vapor. The experiments demonstrated that increased sensitivity to ether correlated with a loss of expression of UBX in the third thoracic imaginal discs and that a significant proportion of the genetic variation for transcriptional stability can be attributed to polymorphism in the Ubx gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibson, G -- Hogness, D S -- New York, N.Y. -- Science. 1996 Jan 12;271(5246):200-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of Michigan, Ann Arbor 48109-1048, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539619" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Base Sequence ; DNA-Binding Proteins/*genetics ; *Drosophila Proteins ; Drosophila melanogaster/drug effects/*genetics ; Ether/pharmacology ; Female ; *Genes, Homeobox ; *Genes, Regulator ; Homeodomain Proteins/*genetics ; Homeostasis ; Linkage Disequilibrium ; Male ; Molecular Sequence Data ; Mutation ; Nucleic Acid Heteroduplexes ; Phenotype ; Polymerase Chain Reaction ; *Polymorphism, Genetic ; Selection, Genetic ; *Transcription Factors
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  • 89
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    Polar overdominance at the ovine callipyge locus (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-12
    Description: An inheritable muscular hypertrophy was recently described in sheep and shown to be determined by the callipyge gene mapped to ovine chromosome 18. Here, the callipyge phenotype was found to be characterized by a nonmendelian inheritance pattern, referred to as polar overdominance, where only heterozygous individuals having inherited the callipyge mutation from their sire express the phenotype. The possible role of parental imprinting in the determinism of polar overdominance is envisaged.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cockett, N E -- Jackson, S P -- Shay, T L -- Farnir, F -- Berghmans, S -- Snowder, G D -- Nielsen, D M -- Georges, M -- New York, N.Y. -- Science. 1996 Jul 12;273(5272):236-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Animal, Dairy and Veterinary Sciences, Utah State University, Logan, UT 84322-4700, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662506" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosome Mapping ; Crosses, Genetic ; Female ; *Genes, Dominant ; *Genomic Imprinting ; Genotype ; Heterozygote ; Lod Score ; Male ; Models, Genetic ; Muscle, Skeletal/*anatomy & histology ; Mutation ; Phenotype ; Sheep/*anatomy & histology/*genetics
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  • 90
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    Similarity of a chromatic adaptation sensor to phytochrome and ethylene receptors (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-09-06
    Description: Complementary chromatic adaptation in cyanobacteria acts through photoreceptors to control the biosynthesis of light-harvesting complexes. The mutant FdBk, which appears black, cannot chromatically adapt and may contain a lesion in the apparatus that senses light quality. The complementing gene identified here, rcaE, encodes a deduced protein in which the amino-terminal region resembles the chromophore attachment domain of phytochrome photoreceptors and regions of plant ethylene receptors; the carboxyl- terminal half is similar to the histidine kinase domain of two-component sensor kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kehoe, D M -- Grossman, A R -- New York, N.Y. -- Science. 1996 Sep 6;273(5280):1409-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Carnegie Institution of Washington, 290 Panama Street, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703080" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Physiological ; Amino Acid Sequence ; Apoproteins/*chemistry ; *Arabidopsis Proteins ; Bacterial Proteins/chemistry ; Cyanobacteria/*chemistry/genetics/physiology ; Genetic Complementation Test ; Light ; *Light-Harvesting Protein Complexes ; Molecular Sequence Data ; Mutation ; Open Reading Frames ; Photosynthetic Reaction Center Complex Proteins/*chemistry/genetics/metabolism ; Phytochrome/*chemistry ; *Plant Proteins ; Protein Kinases/chemistry ; Receptors, Cell Surface/*chemistry ; Sequence Alignment
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  • 91
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    Direct regulation of ZAP-70 by SHP-1 in T cell antigen receptor signaling (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-24
    Description: The threshold at which antigen triggers lymphocyte activation is set by the enzymes that regulate tyrosine phosphorylation. Upon T cell activation, the protein tyrosine phosphatase SHP-1 was found to bind to the protein tyrosine kinase ZAP-70. This interaction resulted in an increase in SHP-1 phosphatase activity and a decrease in ZAP-70 kinase activity. Expression of a dominant negative mutant of SHP-1 in T cells increased the sensitivity of the antigen receptor. Thus, SHP-1 functions as a negative regulator of the T cell antigen receptor and in setting the threshold of activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Plas, D R -- Johnson, R -- Pingel, J T -- Matthews, R J -- Dalton, M -- Roy, G -- Chan, A C -- Thomas, M L -- New York, N.Y. -- Science. 1996 May 24;272(5265):1173-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Center for Immunology, Washington University Medical School, St Louis, Missouri 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638162" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins ; Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Mutation ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/immunology/*metabolism ; Transfection ; Tumor Cells, Cultured ; ZAP-70 Protein-Tyrosine Kinase ; src-Family Kinases/metabolism
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  • 92
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    Substitution of L-fucose by L-galactose in cell walls of Arabidopsis mur1 (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-21
    Description: An Arabidopsis thaliana mutant (mur1) has less than 2 percent of the normal amounts of L-fucose in the primary cell walls of aerial portions of the plant. The survival of mur1 plants challenged the hypothesis that fucose is a required component of biologically active oligosaccharides derived from cell wall xyloglucan. However, the replacement of L-fucose (that is, 6-deoxy-L-galactose) by L-galactose does not detectably alter the biological activity of the oligosaccharides derived from xyloglucan. Thus, essential structural and conformational features of xyloglucan and xyloglucan-derived oligosaccharides are retained when L-galactose replaces L-fucose.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zablackis, E -- York, W S -- Pauly, M -- Hantus, S -- Reiter, W D -- Chapple, C C -- Albersheim, P -- Darvill, A -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1808-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Complex Carbohydrate Research Center, University of Georgia, Athens 30602-4712, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650583" target="_blank"〉PubMed〈/a〉
    Keywords: 2,4-Dichlorophenoxyacetic Acid/pharmacology ; Arabidopsis/*chemistry/genetics/physiology ; Carbohydrate Conformation ; Carbohydrate Sequence ; Cell Wall/*chemistry/physiology ; Fucose/*analysis/physiology ; Fucosyltransferases/metabolism ; Galactose/*analysis/physiology ; *Glucans ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Mutation ; Oligosaccharides/pharmacology ; Peas ; Plant Stems/drug effects/growth & development ; Polysaccharides/*chemistry ; Spectrometry, Mass, Fast Atom Bombardment ; *Xylans
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  • 93
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    Independent modes of natural killing distinguished in mice lacking Lag3 (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-04-19
    Description: The LAG3 protein has several features in common with CD4, suggesting that it may be important in controlling T cell reactivity. However, mice with a Lag3 null mutation have now been shown to exhibit a defect in the natural killer cell, rather than the T cell, compartment. Killing of certain tumor targets by natural killer cells from these mice was inhibited or even abolished, whereas lysis of cells displaying major histocompatibility complex class I disparities remained intact. It appears that LAG3 is a receptor or coreceptor that defines different modes of natural killing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyazaki, T -- Dierich, A -- Benoist, C -- Mathis, D -- New York, N.Y. -- Science. 1996 Apr 19;272(5260):405-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Genetique et de Biologie Moleculaire et Cellulaire (INSERM, CNRS, ULP), Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8602528" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; B-Lymphocytes/immunology ; Base Sequence ; *Cytotoxicity, Immunologic ; Female ; Histocompatibility Antigens Class I/immunology ; Killer Cells, Natural/*immunology ; Male ; Membrane Proteins/genetics/*physiology ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Phenotype ; T-Lymphocytes/immunology ; Tumor Cells, Cultured ; beta 2-Microglobulin/deficiency/physiology
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    Mutant enzyme provides new insights into the cause of ALS (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):446-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560253" target="_blank"〉PubMed〈/a〉
    Keywords: Amyotrophic Lateral Sclerosis/*enzymology/genetics/pathology ; Animals ; Apoptosis ; Cells, Cultured ; Free Radicals ; Humans ; Lipid Peroxidation ; Mice ; Mutation ; Neurons/cytology ; Nitrates/metabolism ; Peroxidases/metabolism ; Selenium/administration & dosage ; Superoxide Dismutase/genetics/*metabolism ; Vitamin E/administration & dosage/metabolism
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  • 95
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    A second breast cancer susceptibility gene is found (1996)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1996-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1996 Jan 5;271(5245):30-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8539592" target="_blank"〉PubMed〈/a〉
    Keywords: BRCA1 Protein ; BRCA2 Protein ; Breast Neoplasms/*genetics/metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 13 ; Computer Communication Networks ; Female ; Genetic Markers ; Genetic Predisposition to Disease ; Great Britain ; Humans ; Mutation ; Neoplasm Proteins/*genetics/physiology ; Patents as Topic ; Sequence Analysis, DNA ; Transcription Factors/*genetics/physiology ; United States
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  • 96
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    Role of type I myosins in receptor-mediated endocytosis in yeast (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-26
    Description: Type I myosins are thought to drive actin-dependent membrane motility, but the direct demonstration in vivo of their involvement in specific cellular processes has been difficult. Deletion of the genes MYO3 and MYO5, which encode the yeast type I myosins, almost abolished growth. A double-deleted mutant complemented with a MYO5 temperature-sensitive allele (myo5-1) showed a strong defect in the internalization step of receptor-mediated endocytosis, whereas the secretory pathway remained apparently unaffected. Thus, myosin I activity is required for a budding event in endocytosis but not for several other aspects of membrane traffic.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geli, M I -- Riezman, H -- New York, N.Y. -- Science. 1996 Apr 26;272(5261):533-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614799" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Endocytosis/*physiology ; Gene Deletion ; Molecular Sequence Data ; Mutation ; Myosins/genetics/*physiology ; Peptides/metabolism ; Receptors, Mating Factor ; Receptors, Peptide/metabolism ; Saccharomyces cerevisiae/genetics/*physiology ; Temperature ; *Transcription Factors
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  • 97
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    Activation of Gal4p by galactose-dependent interaction of galactokinase and Gal80p (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-14
    Description: Yeast galactokinase (Gal1p) is an enzyme and a regulator of transcription. In addition to phosphorylating galactose, Gal1p activates Gal4p, the activator of GAL genes, but the mechanism of this regulation has been unclear. Here, biochemical and genetic evidence is presented to show that Gal1p activates Gal4p by direct interaction with the Gal4p inhibitor Gal80p. Interaction requires galactose, adenosine triphosphate, and the regulatory function of Gal1p. These data indicate that Gal1p-Gal80p complex formation results in the inactivation of Gal80p, thereby transmitting the galactose signal to Gal4p.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zenke, F T -- Engles, R -- Vollenbroich, V -- Meyer, J -- Hollenberg, C P -- Breunig, K D -- New York, N.Y. -- Science. 1996 Jun 14;272(5268):1662-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Mikrobiologie, Heinrich-Heine-Universitat Dusseldorf, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8658143" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Coenzymes/metabolism ; DNA-Binding Proteins ; Fungal Proteins/*metabolism ; Galactokinase/genetics/*metabolism ; Galactose/*metabolism ; Kluyveromyces/genetics/metabolism ; Molecular Sequence Data ; Mutation ; Repressor Proteins/*metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Transcription Factors/*metabolism
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  • 98
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    CD2: an exception to the immunoglobulin superfamily concept? (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-08-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S J -- van der Merwe, P A -- New York, N.Y. -- Science. 1996 Aug 30;273(5279):1241-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8703062" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD2/*chemistry/genetics/metabolism ; Glycosylation ; Humans ; Immunoglobulins/chemistry ; Ligands ; Membrane Glycoproteins/*chemistry/genetics/metabolism ; Mutation ; Polysaccharides/chemistry ; *Protein Conformation ; Protein Folding ; Solubility
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 99
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    Determination of life-span in Caenorhabditis elegans by four clock genes (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-17
    Description: The nematode worm Caenorhabditis elegans is a model system for the study of the genetic basis of aging. Maternal-effect mutations in four genes--clk-1, clk-2, clk-3, and gro-1--interact genetically to determine both the duration of development and life-span. Analysis of the phenotypes of these mutants suggests the existence of a general physiological clock in the worm. Mutations in certain genes involved in dauer formation (an alternative larval stage induced by adverse conditions in which development is arrested) can also extend life-span, but the life extension of Clock mutants appears to be independent of these genes. The daf-2(e1370) clk-1(e2519) worms, which carry life-span-extending mutations from two different pathways, live nearly five times as long as wild-type worms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lakowski, B -- Hekimi, S -- New York, N.Y. -- Science. 1996 May 17;272(5264):1010-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, McGill University, Montreal, Quebec, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8638122" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/*genetics ; Animals ; Biological Clocks/*genetics ; Caenorhabditis elegans/*genetics/*physiology ; *Genes, Helminth ; Genotype ; Longevity/genetics ; Mutation ; Phenotype ; Temperature
    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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  • 100
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    Protein motors may drive cells on route to specialization (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1498-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599101" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/physiology ; Fungal Proteins/genetics/*physiology ; Genes, Fungal ; Mutation ; Saccharomyces cerevisiae/cytology/genetics/*physiology ; Spores, Bacterial/physiology
    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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