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  • Articles  (101)
  • Phosphorylation  (58)
  • Cloning, Molecular  (53)
  • American Association for the Advancement of Science (AAAS)  (101)
  • American Institute of Physics (AIP)
  • American Society of Hematology
  • EMBO Press
  • Essen : Verl. Glückauf
  • 2005-2009
  • 1995-1999  (101)
  • 1997  (101)
Collection
  • Articles  (101)
Source
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (101)
  • American Institute of Physics (AIP)
  • American Society of Hematology
  • EMBO Press
  • Essen : Verl. Glückauf
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Years
  • 2005-2009
  • 1995-1999  (101)
Year
Journal
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  • 1
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    STATs and gene regulation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-12
    Description: STATs (signal transducers and activators of transcription) are a family of latent cytoplasmic proteins that are activated to participate in gene control when cells encounter various extracellular polypeptides. Biochemical and molecular genetic explorations have defined a single tyrosine phosphorylation site and, in a dimeric partner molecule, an Src homology 2 (SH2) phosphotyrosine-binding domain, a DNA interaction domain, and a number of protein-protein interaction domains (with receptors, other transcription factors, the transcription machinery, and perhaps a tyrosine phosphatase). Mouse genetics experiments have defined crucial roles for each known mammalian STAT. The discovery of a STAT in Drosophila, and most recently in Dictyostelium discoideum, implies an ancient evolutionary origin for this dual-function set of proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Darnell, J E Jr -- AI32489/AI/NIAID NIH HHS/ -- AI34420/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 12;277(5332):1630-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Cell Biology, Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9287210" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; DNA/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Dimerization ; *Gene Expression Regulation ; Humans ; Nuclear Proteins/metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; *Signal Transduction ; Trans-Activators/chemistry/genetics/*metabolism ; *Transcriptional Activation ; src Homology Domains
    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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    Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: The nuclear factor of activated T cells (NFAT) group of transcription factors is retained in the cytoplasm of quiescent cells. NFAT activation is mediated in part by induced nuclear import. This process requires calcium-dependent dephosphorylation of NFAT caused by the phosphatase calcineurin. The c-Jun amino-terminal kinase (JNK) phosphorylates NFAT4 on two sites. Mutational removal of the JNK phosphorylation sites caused constitutive nuclear localization of NFAT4. In contrast, JNK activation in calcineurin-stimulated cells caused nuclear exclusion of NFAT4. These findings show that the nuclear accumulation of NFAT4 promoted by calcineurin is opposed by the JNK signal transduction pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chow, C W -- Rincon, M -- Cavanagh, J -- Dickens, M -- Davis, R J -- CA58396/CA/NCI NIH HHS/ -- CA65831/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1638-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9374467" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; COS Cells ; Calcineurin/metabolism ; Calcineurin Inhibitors ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cell Nucleus/*metabolism ; Cyclosporine/pharmacology ; Cytoplasm/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Humans ; JNK Mitogen-Activated Protein Kinases ; Jurkat Cells ; Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Mutation ; NFATC Transcription Factors ; *Nuclear Proteins ; Phosphorylation ; Protein Kinases/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Discrete determinants in transfer RNA for editing and aminoacylation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-23
    Description: During translation errors of aminoacylation are corrected in editing reactions which ensure that an amino acid is stably attached to its corresponding transfer RNA (tRNA). Previous studies have not shown whether the tRNA nucleotides needed for effecting translational editing are the same as or distinct from those required for aminoacylation, but several considerations have suggested that they are the same. Here, designed tRNAs that are highly active for aminoacylation but are not active in translational editing are presented. The editing reaction can be controlled by manipulation of nucleotides at the corner of the L-shaped tRNA. In contrast, these manipulations do not affect aminoacylation. These results demonstrate the segregation of nucleotide determinants for the editing and aminoacylation functions of tRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hale, S P -- Auld, D S -- Schmidt, E -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 May 23;276(5316):1250-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9157882" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Escherichia coli ; Molecular Sequence Data ; Nucleic Acid Conformation ; *RNA Editing ; RNA, Transfer/*metabolism ; RNA, Transfer, Ile/chemistry/metabolism ; RNA, Transfer, Val/chemistry/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Can cloning help save beleaguered species? (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, J -- New York, N.Y. -- Science. 1997 May 30;276(5317):1329-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9190674" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Zoo/genetics ; Cloning, Molecular ; *Conservation of Natural Resources ; Costs and Cost Analysis ; Cryopreservation ; Female ; Fibroblasts/cytology ; *Genetic Engineering/economics ; Genetic Variation ; Reproduction, Asexual ; Sheep ; Species Specificity
    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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  • 5
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    PtdIns(3,4,5)P3 gets its message across (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hemmings, B A -- New York, N.Y. -- Science. 1997 Jul 25;277(5325):534.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute, CH-4002 Basel, Switzerland. hemmings@fmi.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9254423" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Enzyme Activation ; Phosphatidylinositol Phosphates/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Proto-Oncogene Proteins/chemistry/*metabolism ; Proto-Oncogene Proteins c-akt ; Second Messenger Systems ; Signal Transduction
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  • 6
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    Mitochondrial and chloroplast phage-type RNA polymerases in Arabidopsis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-08
    Description: In addition to the RNA polymerases (RNAPs) transcribing the nuclear genes, eukaryotic cells also require RNAPs to transcribe the genes of the mitochondrial genome and, in plants, of the chloroplast genome. The plant Arabidopsis thaliana was found to contain two nuclear genes similar to genes encoding the mitochondrial RNAP from yeast and RNAPs of bacteriophages T7, T3, and SP6. The putative transit peptides of the two polymerases were capable of targeting fusion proteins to mitochondria and chloroplasts, respectively, in vitro. The results indicate that the mitochondrial RNAP in plants is a bacteriophage-type enzyme. A gene duplication event may have generated the second RNAP, which along with the plastid-encoded eubacteria-like RNAP could transcribe the chloroplast genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedtke, B -- Borner, T -- Weihe, A -- New York, N.Y. -- Science. 1997 Aug 8;277(5327):809-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Humboldt University Berlin, Institute of Biology, Chausseestrasse 117, D-10115 Berlin, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9242608" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*enzymology/genetics ; Cell Nucleus/genetics ; Chloroplasts/*enzymology ; Cloning, Molecular ; DNA-Directed RNA Polymerases/chemistry/*genetics ; Exons ; *Genes, Plant ; Introns ; Mitochondria/*enzymology ; Molecular Sequence Data ; Phylogeny ; Recombinant Fusion Proteins/metabolism ; Sequence Alignment ; T-Phages/enzymology
    Print ISSN: 0036-8075
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  • 7
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    Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo angiogenesis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-04
    Description: Angiogenesis is thought to depend on a precise balance of positive and negative regulation. Angiopoietin-1 (Ang1) is an angiogenic factor that signals through the endothelial cell-specific Tie2 receptor tyrosine kinase. Like vascular endothelial growth factor, Ang1 is essential for normal vascular development in the mouse. An Ang1 relative, termed angiopoietin-2 (Ang2), was identified by homology screening and shown to be a naturally occurring antagonist for Ang1 and Tie2. Transgenic overexpression of Ang2 disrupts blood vessel formation in the mouse embryo. In adult mice and humans, Ang2 is expressed only at sites of vascular remodeling. Natural antagonists for vertebrate receptor tyrosine kinases are atypical; thus, the discovery of a negative regulator acting on Tie2 emphasizes the need for exquisite regulation of this angiogenic receptor system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maisonpierre, P C -- Suri, C -- Jones, P F -- Bartunkova, S -- Wiegand, S J -- Radziejewski, C -- Compton, D -- McClain, J -- Aldrich, T H -- Papadopoulos, N -- Daly, T J -- Davis, S -- Sato, T N -- Yancopoulos, G D -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):55-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals Inc., 777 Old Saw Mill River Road, Tarrytown, NY 10591, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204896" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Angiopoietin-1 ; Angiopoietin-2 ; Animals ; Blood Vessels/embryology/*metabolism ; Cells, Cultured ; Cloning, Molecular ; Embryo, Mammalian/metabolism ; Endothelial Growth Factors/genetics/metabolism ; Endothelium, Vascular/*cytology/metabolism ; Female ; Humans ; Ligands ; Lymphokines/genetics/metabolism ; Membrane Glycoproteins/antagonists & inhibitors/metabolism ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; *Neovascularization, Physiologic ; Phosphorylation ; Proteins/chemistry/*metabolism ; Rats ; Rats, Sprague-Dawley ; Receptor Protein-Tyrosine Kinases/*antagonists & inhibitors/metabolism ; Receptor, TIE-2 ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors
    Print ISSN: 0036-8075
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  • 8
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    Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold role of Pbs2p MAPKK (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-13
    Description: Exposure of the yeast Saccharomyces cerevisiae to high extracellular osmolarity induces the Sln1p-Ypd1p-Ssk1p two-component osmosensor to activate a mitogen-activated protein (MAP) kinase cascade composed of the Ssk2p and Ssk22p MAP kinase kinase kinases (MAPKKKs), the Pbs2p MAPKK, and the Hog1p MAPK. A second osmosensor, Sho1p, also activated Pbs2p and Hog1p, but did so through the Ste11p MAPKKK. Although Ste11p also participates in the mating pheromone-responsive MAPK cascade, there was no detectable cross talk between these two pathways. The MAPKK Pbs2p bound to the Sho1p osmosensor, the MAPKKK Ste11p, and the MAPK Hog1p. Thus, Pbs2p may serve as a scaffold protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Posas, F -- Saito, H -- GM50909/GM/NIGMS NIH HHS/ -- GM53415/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1702-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Tumor Immunology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9180081" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Enzyme Activation ; Genes, Fungal ; Genetic Complementation Test ; MAP Kinase Kinase Kinases ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Mutation ; Osmolar Concentration ; Osmotic Pressure ; Peptides/metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; *Saccharomyces cerevisiae Proteins ; Signal Transduction
    Print ISSN: 0036-8075
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  • 9
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    Fluorescence-based isolation of bacterial genes expressed within host cells (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-26
    Description: A selection strategy was devised to identify bacterial genes preferentially expressed when a bacterium associates with its host cell. Fourteen Salmonella typhimurium genes, which were under the control of at least four independent regulatory circuits, were identified to be selectively induced in host macrophages. Four genes encode virulence factors, including a component of a type III secretory apparatus. This selection methodology should be generally applicable to the identification of genes from pathogenic organisms that are induced upon association with host cells or tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Valdivia, R H -- Falkow, S -- AI26195/AI/NIAID NIH HHS/ -- DK38707/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 26;277(5334):2007-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA. valdivia@cmgm.stanford.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9302299" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/genetics ; Cell Line ; Cloning, Molecular ; Female ; Flow Cytometry ; Fluorescence ; *Gene Expression Regulation, Bacterial ; Green Fluorescent Proteins ; HeLa Cells ; Humans ; Luminescent Proteins/genetics ; Macrophages/*microbiology ; Mice ; Mice, Inbred BALB C ; Microscopy, Fluorescence ; Molecular Sequence Data ; Open Reading Frames ; Promoter Regions, Genetic ; Recombinant Fusion Proteins ; Salmonella Infections, Animal/microbiology ; Salmonella typhimurium/*genetics/isolation & purification/*pathogenicity ; Spleen/microbiology ; Transcription Factors/genetics ; Virulence/genetics
    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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  • 10
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    Dictyostelium development in the absence of cAMP (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: Adenosine 3',5'-monophosphate (cAMP) and cAMP-dependent protein kinase (PKA) are regulators of development in many organisms. Dictyostelium uses cAMP as an extracellular chemoattractant and as an intracellular signal for differentiation. Cells that are mutant in adenylyl cyclase do not develop. Moderate expression of the catalytic subunit of PKA in adenylyl cyclase-null cells led to near-normal development without detectable accumulation of cAMP. These results suggest that all intracellular cAMP signaling is effected through PKA and that signals other than extracellular cAMP coordinate morphogenesis in Dictyostelium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, B -- Kuspa, A -- R01 GM052359/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):251-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Marrs McLean Department of Biochemistry, 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/9211856" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Animals ; Cloning, Molecular ; Cyclic AMP/*metabolism ; Cyclic AMP-Dependent Protein Kinases/*metabolism ; Dictyostelium/genetics/*growth & development/metabolism ; Enzyme Activation ; Gene Expression Regulation ; Genes, Protozoan ; Morphogenesis ; Signal Transduction ; Transformation, Genetic
    Print ISSN: 0036-8075
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  • 11
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    Chemical selection for catalysis in combinatorial antibody libraries (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-14
    Description: For the past decade the immune system has been exploited as a rich source of de novo catalysts. Catalytic antibodies have been shown to have chemoselectivity, enantioselectivity, large rate accelerations, and even an ability to reroute chemical reactions. In many instances catalysts have been made for reactions for which there are no known natural or man-made enzymes. Yet, the full power of this combinatorial system can only be exploited if there was a system that allows for the direct selection of a particular function. A method that allows for the direct chemical selection for catalysis from antibody libraries was so devised, whereby the positive aspects of hybridoma technology were preserved and re-formatted in the filamentous phage system to allow direct selection of catalysis. This methodology is based on a purely chemical selection process, making it more general than biologically based selection systems because it is not limited to reaction products that perturb cellular machinery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janda, K D -- Lo, L C -- Lo, C H -- Sim, M M -- Wang, R -- Wong, C H -- Lerner, R A -- GM-43858/GM/NIGMS NIH HHS/ -- GM-44154/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Feb 14;275(5302):945-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Scripps Research Institute, Department of Chemistry, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9020070" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies, Catalytic/genetics/metabolism ; Catalysis ; Cloning, Molecular ; Coliphages ; Dithiothreitol ; Enzyme-Linked Immunosorbent Assay ; Escherichia coli/genetics/metabolism ; Galactosides/metabolism ; Haptens ; Hybridomas ; Immunoglobulin Fab Fragments/genetics/metabolism ; Indoles/metabolism ; Isopropyl Thiogalactoside/metabolism ; Mice ; Nitrophenylgalactosides/metabolism ; *Peptide Library ; Polymerase Chain Reaction ; Serum Albumin, Bovine ; Transformation, Bacterial ; beta-Galactosidase/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 12
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    Receptor offers clues to how 'good' cholesterol works (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Husten, L -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1228.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411750" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenal Glands/metabolism ; Animals ; Antigens, CD36/genetics/*metabolism ; Arteriosclerosis/etiology/metabolism ; *Carrier Proteins ; Cholesterol/blood/metabolism ; Cloning, Molecular ; Humans ; Lipoproteins, HDL/blood/*metabolism ; Liver/metabolism ; *Membrane Proteins ; Mice ; Mice, Knockout ; *RNA-Binding Proteins ; *Receptors, Immunologic ; Receptors, Lipoprotein/genetics/*metabolism ; Receptors, Scavenger ; Scavenger Receptors, Class B
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 13
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    Mammalian genome debate heats up (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1997 Mar 21;275(5307):1733.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9122675" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; Animal Husbandry ; Animals ; Animals, Genetically Modified ; *Bioethics ; Cloning, Molecular ; Federal Government ; *Genetic Engineering ; Genetic Research ; Government Regulation ; Humans ; Public Policy ; Risk Assessment ; United States
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  • 14
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    Panel weighs a law against cloning (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-23
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1997 May 23;276(5316):1185-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9182324" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; Animals ; *Bioethics ; Cloning, Molecular ; Embryo Research ; Embryo, Mammalian ; *Ethics Committees ; Federal Government ; Financing, Government/legislation & jurisprudence ; Genetic Engineering/*legislation & jurisprudence ; *Government Regulation ; Humans ; Nuclear Transfer Techniques ; Private Sector/legislation & jurisprudence ; Public Policy ; Research Support as Topic/*legislation & jurisprudence ; Sheep
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  • 15
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    A euryarchaeal lysyl-tRNA synthetase: resemblance to class I synthetases (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-14
    Description: The sequencing of euryarchaeal genomes has suggested that the essential protein lysyl-transfer RNA (tRNA) synthetase (LysRS) is absent from such organisms. However, a single 62-kilodalton protein with canonical LysRS activity was purified from Methanococcus maripaludis, and the gene that encodes this protein was cloned. The predicted amino acid sequence of M. maripaludis LysRS is similar to open reading frames of unassigned function in both Methanobacterium thermoautotrophicum and Methanococcus jannaschii but is unrelated to canonical LysRS proteins reported in eubacteria, eukaryotes, and the crenarchaeote Sulfolobus solfataricus. The presence of amino acid motifs characteristic of the Rossmann dinucleotide-binding domain identifies M. maripaludis LysRS as a class I aminoacyl-tRNA synthetase, in contrast to the known examples of this enzyme, which are class II synthetases. These data question the concept that the classification of aminoacyl-tRNA synthetases does not vary throughout living systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ibba, M -- Morgan, S -- Curnow, A W -- Pridmore, D R -- Vothknecht, U C -- Gardner, W -- Lin, W -- Woese, C R -- Soll, D -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1119-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, Post Office Box 208114, 266 Whitney Avenue, New Haven, CT 06520-8114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9353192" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Animals ; Bacteria/enzymology ; Cloning, Molecular ; Electrophoresis, Polyacrylamide Gel ; Euryarchaeota/enzymology/genetics ; Evolution, Molecular ; Genes, Archaeal ; Humans ; Kinetics ; Lysine-tRNA Ligase/*chemistry/*classification/genetics/metabolism ; Methanococcus/*enzymology/genetics ; Molecular Sequence Data ; Phylogeny ; RNA, Transfer, Amino Acyl/biosynthesis ; Sequence Alignment ; Sulfolobus/enzymology
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  • 16
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    New clues found to circadian clocks--including mammals' (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1997 May 16;276(5315):1030-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9173537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Clocks/*genetics ; CLOCK Proteins ; Chromosome Mapping ; Circadian Rhythm/*genetics ; Cloning, Molecular ; Gene Expression Regulation ; Mice ; Mutation ; Trans-Activators/chemistry/*genetics/physiology
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  • 17
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    Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-01-17
    Description: The proto-oncogene-encoded transcription factor c-Jun activates genes in response to a number of inducers that act through mitogen-activated protein kinase (MAPK) signal transduction pathways. The activation of c-Jun after phosphorylation by MAPK is accompanied by a reduction in c-Jun ubiquitination and consequent stabilization of the protein. These results illustrate the relevance of regulated protein degradation in the signal-dependent control of gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Musti, A M -- Treier, M -- Bohmann, D -- New York, N.Y. -- Science. 1997 Jan 17;275(5298):400-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstr. 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8994040" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Cycle Proteins/metabolism ; GTP-Binding Proteins/metabolism ; Gene Expression Regulation ; JNK Mitogen-Activated Protein Kinases ; Mice ; *Mitogen-Activated Protein Kinases ; Phosphorylation ; Proto-Oncogene Proteins c-jun/*metabolism ; Signal Transduction ; Transfection ; Ubiquitins/*metabolism ; cdc42 GTP-Binding Protein, Saccharomyces cerevisiae
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  • 18
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    Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-06-27
    Description: Long-term potentiation (LTP), a cellular model of learning and memory, requires calcium-dependent protein kinases. Induction of LTP increased the phosphorus-32 labeling of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPA-Rs), which mediate rapid excitatory synaptic transmission. This AMPA-R phosphorylation appeared to be catalyzed by Ca2+- and calmodulin-dependent protein kinase II (CaM-KII): (i) it correlated with the activation and autophosphorylation of CaM-KII, (ii) it was blocked by the CaM-KII inhibitor KN-62, and (iii) its phosphorus-32 peptide map was the same as that of GluR1 coexpressed with activated CaM-KII in HEK-293 cells. This covalent modulation of AMPA-Rs in LTP provides a postsynaptic molecular mechanism for synaptic plasticity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barria, A -- Muller, D -- Derkach, V -- Griffith, L C -- Soderling, T R -- NS27037/NS/NINDS NIH HHS/ -- R01 GM054408/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):2042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland, OR 97201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9197267" target="_blank"〉PubMed〈/a〉
    Keywords: 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine/analogs & derivatives/pharmacology ; 2-Amino-5-phosphonovalerate/pharmacology ; Animals ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism ; Cell Line ; Enzyme Inhibitors/pharmacology ; Excitatory Amino Acid Antagonists/pharmacology ; Hippocampus/*metabolism ; Humans ; In Vitro Techniques ; *Long-Term Potentiation/drug effects ; Male ; Peptide Mapping ; Phosphorylation ; Rats ; Rats, Sprague-Dawley ; Receptors, AMPA/*metabolism ; Synaptic Transmission/drug effects
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  • 19
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    In situ activation pattern of Drosophila EGF receptor pathway during development (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-22
    Description: Signaling cascades triggered by receptor tyrosine kinases (RTKs) participate in diverse developmental processes. The active state of these signaling pathways was monitored by examination of the in situ distribution of the active, dual phosphorylated form of mitogen-activated protein kinase (ERK) with a specific monoclonal antibody. Detection of the active state of the Drosophila epidermal growth factor receptor (DER) pathway allowed the visualization of gradients and boundaries of receptor activation, assessment of the distribution of activating ligands, and analysis of interplay with the inhibitory ligand Argos. This in situ approach can be used to monitor other receptor-triggered pathways in a wide range of organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gabay, L -- Seger, R -- Shilo, B Z -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1103-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9262480" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Body Patterning ; Calcium-Calmodulin-Dependent Protein Kinases/immunology/*metabolism ; Cell Differentiation ; Drosophila/cytology/embryology/genetics/*metabolism ; *Drosophila Proteins ; *Epidermal Growth Factor ; Eye Proteins/metabolism ; Gene Expression Regulation, Developmental ; Genes, Insect ; Membrane Proteins/metabolism ; Mutation ; Nerve Tissue Proteins/metabolism ; Phosphorylation ; Photoreceptor Cells, Invertebrate/cytology/embryology ; Receptor, Epidermal Growth Factor/*metabolism ; *Signal Transduction
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  • 20
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    Transmission of hepatitis C by intrahepatic inoculation with transcribed RNA (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-25
    Description: More than 1% of the world's population is chronically infected with hepatitis C virus (HCV). HCV infection can result in acute hepatitis, chronic hepatitis, and cirrhosis, which is strongly associated with development of hepatocellular carcinoma. Genetic studies of HCV replication have been hampered by lack of a bona fide infectious molecular clone. Full-length functional clones of HCV complementary DNA were constructed. RNA transcripts from the clones were found to be infectious and to cause disease in chimpanzees after direct intrahepatic inoculation. This work defines the structure of a functional HCV genome RNA and proves that HCV alone is sufficient to cause disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolykhalov, A A -- Agapov, E V -- Blight, K J -- Mihalik, K -- Feinstone, S M -- Rice, C M -- AI40034/AI/NIAID NIH HHS/ -- CA57973/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 25;277(5325):570-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110-1093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9228008" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Consensus Sequence ; DNA, Complementary ; Hepacivirus/*genetics/physiology ; Hepatitis C/*transmission/*virology ; Liver/*virology ; Molecular Sequence Data ; Pan troglodytes ; Polymerase Chain Reaction ; RNA, Messenger/*genetics ; RNA, Viral/blood/*genetics ; Transfection ; Viremia ; Virus Replication
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  • 21
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    Inducible expression and phosphorylation of coactivator BOB.1/OBF.1 in T cells (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-11
    Description: BOB.1/OBF.1 is a transcriptional coactivator that is constitutively expressed in B cells and interacts with the Oct1 and Oct2 transcription factors. Upon activation of Jurkat T cells and primary murine thymocytes with phorbol esters and ionomycin, BOB.1/OBF.1 expression and transactivation function were induced. BOB.1/OBF.1 was phosphorylated at Ser184 both in vivo and in vitro, and this modification was required for inducible activation. Mutation of Ser184 also diminished transactivation function in B cells, suggesting that the activating phosphorylation that is inducible in T cells is constitutively present in B cells. Thus, BOB.1/OBF.1 is a transcriptional coactivator that is critically regulated by posttranslational modifications to mediate cell type-specific gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zwilling, S -- Dieckmann, A -- Pfisterer, P -- Angel, P -- Wirth, T -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):221-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MSZ, Institut fur Medizinische Strahlenkunde und Zellforschung, Universitat Wurzburg, Versbacher Strasse 5, 97078 Wurzburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9211847" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/metabolism ; Cells, Cultured ; *DNA-Binding Proteins ; *Gene Expression Regulation ; HeLa Cells ; Homeodomain Proteins/metabolism ; Host Cell Factor C1 ; Humans ; Immunosuppressive Agents/pharmacology ; Ionomycin/pharmacology ; Jurkat Cells ; *Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Octamer Transcription Factor-1 ; Phosphorylation ; Phosphoserine/metabolism ; Recombinant Fusion Proteins/metabolism ; T-Lymphocytes/immunology/*metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Trans-Activators/genetics/*metabolism ; Transcription Factors/metabolism ; *Transcriptional Activation
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  • 22
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    Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to Cdk regulation through Cdc25 (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-09-05
    Description: In response to DNA damage, mammalian cells prevent cell cycle progression through the control of critical cell cycle regulators. A human gene was identified that encodes the protein Chk1, a homolog of the Schizosaccharomyces pombe Chk1 protein kinase, which is required for the DNA damage checkpoint. Human Chk1 protein was modified in response to DNA damage. In vitro Chk1 bound to and phosphorylated the dual-specificity protein phosphatases Cdc25A, Cdc25B, and Cdc25C, which control cell cycle transitions by dephosphorylating cyclin-dependent kinases. Chk1 phosphorylates Cdc25C on serine-216. As shown in an accompanying paper by Peng et al. in this issue, serine-216 phosphorylation creates a binding site for 14-3-3 protein and inhibits function of the phosphatase. These results suggest a model whereby in response to DNA damage, Chk1 phosphorylates and inhibits Cdc25C, thus preventing activation of the Cdc2-cyclin B complex and mitotic entry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sanchez, Y -- Wong, C -- Thoma, R S -- Richman, R -- Wu, Z -- Piwnica-Worms, H -- Elledge, S J -- GM17763/GM/NIGMS NIH HHS/ -- GM44664/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1497-501.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Marrs McLean Department of Biochemistry, Howard Hughes Medical Institute, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278511" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; Amino Acid Sequence ; Animals ; CDC2 Protein Kinase/*metabolism ; Cell Cycle Proteins/antagonists & inhibitors/*metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 11 ; Cytoskeletal Proteins ; *DNA Damage ; *F-Box Proteins ; G2 Phase ; HeLa Cells ; Humans ; Mice ; *Mitosis ; Molecular Sequence Data ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Kinases/chemistry/genetics/*metabolism ; Protein Tyrosine Phosphatases/metabolism ; Proteins/metabolism ; Recombinant Fusion Proteins/metabolism ; Schizosaccharomyces pombe Proteins ; Signal Transduction ; Transfection ; *Tyrosine 3-Monooxygenase ; *Ubiquitin-Protein Ligases ; *cdc25 Phosphatases
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  • 23
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    Identification of a naturally occurring peroxidase-lipoxygenase fusion protein (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-09-26
    Description: A distant relative of catalase that is specialized for metabolism of a fatty acid hydroperoxide was identified. This heme peroxidase occurs in coral as part of a fusion protein, the other component of which is a lipoxygenase that forms the hydroperoxide substrate. The end product is an unstable epoxide (an allene oxide) that is a potential precursor of prostaglandin-like molecules. These results extend the known chemistry of catalase-like proteins and reveal a distinct type of enzymatic construct involved in the metabolism of polyunsaturated fatty acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koljak, R -- Boutaud, O -- Shieh, B H -- Samel, N -- Brash, A R -- GM49502/GM/NIGMS NIH HHS/ -- TW00404/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 26;277(5334):1994-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Vanderbilt University Medical Center, Nashville, TN 37232-6602, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9302294" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arachidonic Acid/metabolism ; Binding Sites ; Catalase/chemistry ; Catalysis ; Cloning, Molecular ; Cnidaria/*enzymology/genetics ; Hydrogen Peroxide/metabolism ; *Intramolecular Oxidoreductases ; Isomerases/chemistry ; Lipoxygenase/*chemistry/genetics/isolation & purification/metabolism ; Molecular Sequence Data ; Peroxidase/*chemistry/genetics/isolation & purification/metabolism ; Peroxidases/*chemistry/isolation & purification/metabolism ; Recombinant Proteins/metabolism ; Sequence Homology, Amino Acid
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  • 24
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    Constitutive transcriptional activation by a beta-catenin-Tcf complex in APC-/- colon carcinoma (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-21
    Description: The adenomatous polyposis coli (APC) tumor suppressor protein binds to beta-catenin, a protein recently shown to interact with Tcf and Lef transcription factors. The gene encoding hTcf-4, a Tcf family member that is expressed in colonic epithelium, was cloned and characterized. hTcf-4 transactivates transcription only when associated with beta-catenin. Nuclei of APC-/- colon carcinoma cells were found to contain a stable beta-catenin-hTcf-4 complex that was constitutively active, as measured by transcription of a Tcf reporter gene. Reintroduction of APC removed beta-catenin from hTcf-4 and abrogated the transcriptional transactivation. Constitutive transcription of Tcf target genes, caused by loss of APC function, may be a crucial event in the early transformation of colonic epithelium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korinek, V -- Barker, N -- Morin, P J -- van Wichen, D -- de Weger, R -- Kinzler, K W -- Vogelstein, B -- Clevers, H -- CA57345/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 21;275(5307):1784-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, University Hospital, Post Office Box 85500, 3508 GA Utrecht, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9065401" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Amino Acid Sequence ; Animals ; Cell Line ; Cell Transformation, Neoplastic ; Cloning, Molecular ; Colon/metabolism ; Colonic Neoplasms/*genetics/metabolism ; Cytoskeletal Proteins/genetics/*metabolism ; Gene Expression Regulation, Neoplastic ; *Genes, APC ; Genes, Reporter ; Humans ; Intestinal Mucosa/metabolism ; Mice ; Molecular Sequence Data ; Signal Transduction ; TCF Transcription Factors ; *Trans-Activators ; Transcription Factor 7-Like 2 Protein ; Transcription Factors/chemistry/genetics/*metabolism ; *Transcriptional Activation ; Transfection ; Tumor Cells, Cultured ; beta Catenin
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  • 25
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    Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-28
    Description: Signal transmission by many cell surface receptors results in the activation of phosphoinositide (PI) 3-kinases that phosphorylate the 3' position of polyphosphoinositides. From a screen for mouse proteins that bind phosphoinositides, the protein GRP1was identified. GRP1 binds phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4, 5)P3] through a pleckstrin homology (PH) domain and displays a region of high sequence similarity to the yeast Sec7 protein. The PH domain of the closely related protein cytohesin-1, which, through its Sec7 homology domain, regulates integrin beta2 and catalyzes guanine nucleotide exchange of the small guanine nucleotide-binding protein ARF1, was also found to specifically bind PtdIns(3,4,5)P3. GRP1 and cytohesin-1 appear to connect receptor-activated PI 3-kinase signaling pathways with proteins that mediate biological responses such as cell adhesion and membrane trafficking.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klarlund, J K -- Guilherme, A -- Holik, J J -- Virbasius, J V -- Chawla, A -- Czech, M P -- DK30648/DK/NIDDK NIH HHS/ -- DK30898/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 28;275(5308):1927-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Medicine and Department of Biochemistry and Molecular Biology, University of Massachusetts Medical Center, 373 Plantation Street, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072969" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factor 1 ; ADP-Ribosylation Factors ; Adipocytes/chemistry ; Amino Acid Sequence ; Animals ; Antigens, CD18/metabolism ; Blood Proteins/*chemistry ; Brain Chemistry ; Cell Adhesion Molecules/chemistry/*metabolism ; Cell Membrane/metabolism ; Cells, Cultured ; Cloning, Molecular ; DNA, Complementary ; Fungal Proteins/*chemistry ; GTP-Binding Proteins/metabolism ; *Guanine Nucleotide Exchange Factors ; Humans ; Mice ; Molecular Sequence Data ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/*metabolism ; *Phosphoproteins ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/*metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Sequence Homology, Amino Acid ; *Signal Transduction
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  • 26
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    Src structure crystallizes 20 years of oncogene research (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Featherstone, C -- New York, N.Y. -- Science. 1997 Feb 21;275(5303):1066.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9054006" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography, X-Ray ; Models, Molecular ; Phosphorylation ; *Protein Conformation ; Protein Structure, Secondary ; Protein-Tyrosine Kinases/chemistry ; Proto-Oncogene Proteins/chemistry ; Proto-Oncogene Proteins c-hck ; Proto-Oncogene Proteins pp60(c-src)/*chemistry/metabolism ; Tyrosine/chemistry/metabolism ; *src Homology Domains
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  • 27
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    Fyn-kinase as a determinant of ethanol sensitivity: relation to NMDA-receptor function (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-24
    Description: Animals vary in their sensitivity to ethanol, a trait at least partly determined by genetic factors. In order to identify possible responsible genes, mice lacking Fyn, a non-receptor type tyrosine kinase, were investigated. These mice were hypersensitive to the hypnotic effect of ethanol. The administration of ethanol enhanced tyrosine phosphorylation of the N-methyl-D-aspartate receptor (NMDAR) in the hippocampus of control mice but not in Fyn-deficient mice. An acute tolerance to ethanol inhibition of NMDAR-mediated excitatory postsynaptic potentials in hippocampal slices developed in control mice but not in Fyn-deficient mice. These results indicate that Fyn affects behavioral, biochemical, and physiological responses to ethanol.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyakawa, T -- Yagi, T -- Kitazawa, H -- Yasuda, M -- Kawai, N -- Tsuboi, K -- Niki, H -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):698-701.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Neurobiology of Emotion, Brain Science Institute, RIKEN, Hirosawa, Wako-shi, Saitama-ken 351-01, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Central Nervous System Depressants/*pharmacology ; Ethanol/*pharmacology ; Excitatory Postsynaptic Potentials/drug effects ; Flurazepam/pharmacology ; Hippocampus/metabolism ; Hypnotics and Sedatives/pharmacology ; In Vitro Techniques ; Male ; Mice ; Mice, Knockout ; Motor Activity/*drug effects ; N-Methylaspartate/pharmacology ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/deficiency/genetics/*metabolism ; Proto-Oncogene Proteins/deficiency/genetics/*metabolism ; Proto-Oncogene Proteins c-fyn ; Receptors, N-Methyl-D-Aspartate/*metabolism
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    Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-18
    Description: Most cases of early-onset familial Alzheimer's disease (FAD) are caused by mutations in the genes encoding the presenilin 1 (PS1) and PS2 proteins, both of which undergo regulated endoproteolytic processing. During apoptosis, PS1 and PS2 were shown to be cleaved at sites distal to their normal cleavage sites by a caspase-3 family protease. In cells expressing PS2 containing the asparagine-141 FAD mutant, the ratio of alternative to normal PS2 cleavage fragments was increased relative to wild-type PS2-expressing cells, suggesting a potential role for apoptosis-associated cleavage of presenilins in the pathogenesis of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, T W -- Pettingell, W H -- Jung, Y K -- Kovacs, D M -- Tanzi, R E -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):373-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetics and Aging Unit, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9219695" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/metabolism/pathology ; Amino Acid Chloromethyl Ketones/pharmacology ; Amino Acid Substitution ; Animals ; *Apoptosis ; Caspase 3 ; *Caspases ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Enzyme Activation ; Etoposide/pharmacology ; Membrane Proteins/chemistry/genetics/*metabolism ; Mutation ; Oligopeptides/pharmacology ; Phosphorylation ; Presenilin-1 ; Presenilin-2 ; Rats ; Staurosporine/pharmacology ; Tumor Cells, Cultured
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    daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-15
    Description: A C. elegans neurosecretory signaling system regulates whether animals enter the reproductive life cycle or arrest development at the long-lived dauer diapause stage. daf-2, a key gene in the genetic pathway that mediates this endocrine signaling, encodes an insulin receptor family member. Decreases in DAF-2 signaling induce metabolic and developmental changes, as in mammalian metabolic control by the insulin receptor. Decreased DAF-2 signaling also causes an increase in life-span. Life-span regulation by insulin-like metabolic control is analogous to mammalian longevity enhancement induced by caloric restriction, suggesting a general link between metabolism, diapause, and longevity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimura, K D -- Tissenbaum, H A -- Liu, Y -- Ruvkun, G -- R01AG14161/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):942-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Massachusetts General Hospital, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252323" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Amino Acid Sequence ; Animals ; Caenorhabditis elegans/chemistry/*genetics/growth & development/metabolism ; Caenorhabditis elegans Proteins ; Chromosome Mapping ; Conserved Sequence ; Energy Intake ; *Genes, Helminth ; Glucose/metabolism ; Humans ; Insulin/metabolism ; Larva/genetics/growth & development/metabolism ; Longevity/*genetics ; Molecular Sequence Data ; Mutation ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Receptor, IGF Type 1/chemistry/genetics ; Receptor, Insulin/chemistry/*genetics/metabolism ; Signal Transduction
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    Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-31
    Description: The regulation of the serine-threonine kinase Akt by lipid products of phosphoinositide 3-kinase (PI 3-kinase) was investigated. Akt activity was found to correlate with the amount of phosphatidylinositol-3,4-bisphosphate (PtdIns-3,4-P2) in vivo, and synthetic PtdIns-3,4-P2 activated Akt both in vitro and in vivo. Binding of PtdIns-3,4-P2 occurred within the Akt pleckstrin homology (PH) domain and facilitated dimerization of Akt. Akt mutated in the PH domain was not activated by PI 3-kinase in vivo or by PtdIns-3, 4-P2 in vitro, and it was impaired in binding to PtdIns-3,4-P2. Examination of the binding to other phosphoinositides revealed that they bound to the Akt PH domain with much lower affinity than did PtdIns-3,4-P2 and failed to increase Akt activity. Thus, Akt is apparently regulated by the direct interaction of PtdIns-3,4-P2 with the Akt PH domain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Franke, T F -- Kaplan, D R -- Cantley, L C -- Toker, A -- GM41890/GM/NIGMS NIH HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- R01 GM041890/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):665-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ABL-Basic Research Program, National Cancer Institute-Frederick Cancer Research Facility and Development Center (NCI-FCRFDC), Frederick, MD 21702, USA. tfranke@bidmc.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005852" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; COS Cells ; Dimerization ; Enzyme Activation ; Mice ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/*metabolism/pharmacology ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Platelet-Derived Growth Factor/pharmacology ; Point Mutation ; Protein-Serine-Threonine Kinases/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins c-akt ; Recombinant Fusion Proteins/chemistry/metabolism
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    NMDA channel regulation by channel-associated protein tyrosine kinase Src (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-31
    Description: The N-methyl-D-aspartate (NMDA) receptor mediates synaptic transmission and plasticity in the central nervous system (CNS) and is regulated by tyrosine phosphorylation. In membrane patches excised from mammalian central neurons, the endogenous tyrosine kinase Src was shown to regulate the activity of NMDA channels. The action of Src required a sequence [Src(40-58)] within the noncatalytic, unique domain of Src. In addition, Src coprecipitated with NMDA receptor proteins. Finally, endogenous Src regulated the function of NMDA receptors at synapses. Thus, NMDA receptor regulation by Src may be important in development, plasticity, and pathology in the CNS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, X M -- Askalan, R -- Keil, G J 2nd -- Salter, M W -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):674-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Hospital for Sick Children, Department of Physiology, University of Toronto, Toronto, Ontario, M5G 1X8 Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005855" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cells, Cultured ; Ion Channel Gating ; Ion Channels/*metabolism ; Molecular Sequence Data ; N-Methylaspartate/metabolism ; Neurons/*metabolism ; Oligopeptides/pharmacology ; Patch-Clamp Techniques ; Phosphorylation ; Phosphotyrosine/metabolism ; Rats ; Rats, Wistar ; Receptors, N-Methyl-D-Aspartate/*metabolism ; Spinal Cord/cytology ; Synapses/*metabolism ; Synaptic Transmission ; src-Family Kinases/chemistry/*metabolism
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    Cdc25 mitotic inducer targeted by chk1 DNA damage checkpoint kinase (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-09-05
    Description: Arrest of the cell cycle at the G2 checkpoint, induced by DNA damage, requires inhibitory phosphorylation of the kinase Cdc2 in both fission yeast and human cells. The kinase Wee1 and the phosphatase Cdc25, which regulate Cdc2 phosphorylation, were evaluated as targets of Chk1, a kinase essential for the checkpoint. Fission yeast cdc2-3w Deltacdc25 cells, which express activated Cdc2 and lack Cdc25, were responsive to Wee1 but insensitive to Chk1 and irradiation. Expression of large amounts of Chk1 produced the same phenotype as did loss of the cdc25 gene in cdc2-3w cells. Cdc25 associated with Chk1 in vivo and was phosphorylated when copurified in Chk1 complexes. These findings identify Cdc25, but not Wee1, as a target of the DNA damage checkpoint.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Furnari, B -- Rhind, N -- Russell, P -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1495-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, The 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/9278510" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; CDC2 Protein Kinase/*metabolism ; Cell Cycle Proteins/*metabolism ; Cell Division ; *DNA Damage ; DNA Helicases/metabolism ; Fungal Proteins/*metabolism ; G2 Phase ; Gamma Rays ; Genes, Fungal ; *Mitosis ; Models, Biological ; Mutation ; *Nuclear Proteins ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Kinases/genetics/*metabolism ; Protein-Tyrosine Kinases/genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/cytology/genetics/*metabolism/radiation effects ; Schizosaccharomyces pombe Proteins ; Signal Transduction ; Temperature ; *ras-GRF1
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    The product of the proto-oncogene c-cbl: a negative regulator of the Syk tyrosine kinase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-18
    Description: Engagement of antigen and immunoglobulin receptors on hematopoietic cells is directly coupled to activation of nonreceptor protein tyrosine kinases (PTKs) that then phosphorylate critical intracellular substrates. In mast cells stimulated through the FcvarepsilonRI receptor, activation of several PTKs including Syk leads to degranulation and release of such mediators of the allergic response as histamine and serotonin. Regulation of Syk function occurred through interaction with the Cbl protein, itself a PTK substrate in this system. Overexpression of Cbl led to inhibition of Syk and suppression of serotonin release from mast cells, demonstrating its ability to inhibit a nonreceptor tyrosine kinase. Complex adaptor proteins such as Cbl can directly regulate the functions of the proteins they bind.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ota, Y -- Samelson, L E -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):418-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-5430, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9103201" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Degranulation ; Enzyme Precursors/antagonists & inhibitors/*metabolism ; Genetic Vectors ; Intracellular Signaling Peptides and Proteins ; Mast Cells/*metabolism ; Mutation ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors/*metabolism ; Proto-Oncogene Proteins/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins c-cbl ; Rats ; Receptors, IgE/metabolism ; Receptors, IgG/metabolism ; Recombinant Proteins/metabolism ; Serotonin/metabolism ; Signal Transduction ; Tumor Cells, Cultured ; *Ubiquitin-Protein Ligases ; Vaccinia virus
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    Signaling vascular morphogenesis and maintenance (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanahan, D -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):48-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of California at San Francisco, San Francisco, CA 94143-0534, USA. dougvhanahan@biochem.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9229772" target="_blank"〉PubMed〈/a〉
    Keywords: Angiopoietin-1 ; Angiopoietin-2 ; Animals ; Apoptosis ; Blood Vessels/*embryology/growth & development/metabolism ; Cell Division ; Endothelial Growth Factors/metabolism ; Endothelium, Vascular/*cytology/metabolism ; Lymphokines/metabolism ; Membrane Glycoproteins/metabolism ; Mice ; Mice, Knockout ; Morphogenesis ; *Neovascularization, Physiologic ; Phosphorylation ; Proteins/metabolism ; Proto-Oncogene Proteins/metabolism ; Receptor Protein-Tyrosine Kinases/*metabolism ; Receptor, TIE-2 ; Receptors, Growth Factor/metabolism ; Receptors, Vascular Endothelial Growth Factor ; *Signal Transduction ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factor Receptor-1 ; Vascular Endothelial Growth Factors
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    PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-07
    Description: Protein dephosphorylation by phosphatase PP1 plays a central role in mediating the effects of insulin on glucose and lipid metabolism. A PP1C-targeting protein expressed in 3T3-L1 adipocytes (called PTG, for protein targeting to glycogen) was cloned and characterized. PTG was expressed predominantly in insulin-sensitive tissues. In addition to binding and localizing PP1C to glycogen, PTG formed complexes with phosphorylase kinase, phosphorylase a, and glycogen synthase, the primary enzymes involved in the hormonal regulation of glycogen metabolism. Overexpression of PTG markedly increased basal and insulin-stimulated glycogen synthesis in Chinese hamster ovary cells overexpressing the insulin receptor, which do not express endogenous PTG. These results suggest that PTG is critical for glycogen metabolism, possibly functioning as a molecular scaffold.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Printen, J A -- Brady, M J -- Saltiel, A R -- New York, N.Y. -- Science. 1997 Mar 7;275(5305):1475-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Michigan School of Medicine, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9045612" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; CHO Cells ; Carrier Proteins/chemistry/genetics/*metabolism ; Cloning, Molecular ; Cricetinae ; DNA, Complementary/genetics ; Glycogen/biosynthesis/*metabolism ; Glycogen Synthase/metabolism ; Insulin/pharmacology ; *Intracellular Signaling Peptides and Proteins ; Mice ; Molecular Sequence Data ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylase Kinase/metabolism ; Phosphorylase a/metabolism ; Phosphorylation ; Protein Binding ; Protein Phosphatase 1 ; Recombinant Fusion Proteins/metabolism ; Substrate Specificity ; Transfection
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  • 36
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    A mammalian telomerase-associated protein (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-02-14
    Description: The telomerase ribonucleoprotein catalyzes the addition of new telomeres onto chromosome ends. A gene encoding a mammalian telomerase homolog called TP1 (telomerase-associated protein 1) was identified and cloned. TP1 exhibited extensive amino acid similarity to the Tetrahymena telomerase protein p80 and was shown to interact specifically with mammalian telomerase RNA. Antiserum to TP1 immunoprecipitated telomerase activity from cell extracts, suggesting that TP1 is associated with telomerase in vivo. The identification of TP1 suggests that telomerase-associated proteins are conserved from ciliates to humans.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrington, L -- McPhail, T -- Mar, V -- Zhou, W -- Oulton, R -- Bass, M B -- Arruda, I -- Robinson, M O -- New York, N.Y. -- Science. 1997 Feb 14;275(5302):973-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Arruda, Ontario Cancer Institute-Amgen Institute, Department of Medical Biophysics, University of Toronto, 620 University Avenue, Toronto, Ontario M5G 2C1, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9020079" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Carrier Proteins/*chemistry/genetics/immunology/*metabolism ; Cell Line ; Cloning, Molecular ; DNA, Complementary/genetics ; Humans ; Mice ; Molecular Sequence Data ; Precipitin Tests ; RNA/*metabolism ; RNA, Messenger/genetics/metabolism ; Sequence Homology, Amino Acid ; Telomerase/*chemistry/genetics/metabolism ; Tetrahymena/chemistry/genetics ; Transfection ; Tumor Cells, Cultured
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  • 37
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    Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-05-09
    Description: Timely deactivation of kinase cascades is crucial to the normal control of cell signaling and is partly accomplished by protein phosphatase 2A (PP2A). The catalytic (alpha) subunit of the serine-threonine kinase casein kinase 2 (CK2) bound to PP2A in vitro and in mitogen-starved cells; binding required the integrity of a sequence motif common to CK2alpha and SV40 small t antigen. Overexpression of CK2alpha resulted in deactivation of mitogen-activated protein kinase kinase (MEK) and suppression of cell growth. Moreover, CK2alpha inhibited the transforming activity of oncogenic Ras, but not that of constitutively activated MEK. Thus, CK2alpha may regulate the deactivation of the mitogen-activated protein kinase pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heriche, J K -- Lebrin, F -- Rabilloud, T -- Leroy, D -- Chambaz, E M -- Goldberg, Y -- New York, N.Y. -- Science. 1997 May 9;276(5314):952-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Commissariat a l'Energie Atomique, Departement de Biologie Moleculaire et Structurale, Laboratoire de Biochimie des Regulations Cellulaires Endocrines, Unite 244, F-38054 Grenoble Cedex 9, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9139659" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Antigens, Polyomavirus Transforming ; Binding Sites ; Casein Kinase II ; Cell Division ; Cell Transformation, Neoplastic ; MAP Kinase Kinase 1 ; Mice ; *Mitogen-Activated Protein Kinase Kinases ; Mutation ; Okadaic Acid/pharmacology ; Phosphoprotein Phosphatases/*metabolism ; Phosphorylation ; Platelet-Derived Growth Factor/pharmacology ; Protein Phosphatase 2 ; Protein-Serine-Threonine Kinases/*metabolism/pharmacology ; Protein-Tyrosine Kinases/metabolism/pharmacology ; Recombinant Fusion Proteins/metabolism ; Transfection ; ras Proteins/pharmacology
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  • 38
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    Worm longevity gene cloned (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):897-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9281069" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caenorhabditis elegans/*genetics/growth & development/metabolism ; Caenorhabditis elegans Proteins ; Cloning, Molecular ; Energy Intake ; *Genes, Helminth ; Glucose/metabolism ; Humans ; Insulin/metabolism ; Longevity/*genetics ; Mice ; Mutation ; Phosphatidylinositol 3-Kinases ; Phosphotransferases (Alcohol Group Acceptor)/genetics/metabolism ; Receptor, Insulin/*genetics/metabolism ; Second Messenger Systems ; Signal Transduction
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    Interleukin-3-induced phosphorylation of BAD through the protein kinase Akt (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-24
    Description: BAD is a distant member of the Bcl-2 family that promotes cell death. Phosphorylation of BAD prevents this. BAD phosphorylation induced by interleukin-3 (IL-3) was inhibited by specific inhibitors of phosphoinositide 3-kinase (PI 3-kinase). Akt, a survival-promoting serine-threonine protein kinase, was activated by IL-3 in a PI 3-kinase-dependent manner. Active, but not inactive, forms of Akt were found to phosphorylate BAD in vivo and in vitro at the same residues that are phosphorylated in response to IL-3. Thus, the proapoptotic function of BAD is regulated by the PI 3-kinase-Akt pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉del Peso, L -- Gonzalez-Garcia, M -- Page, C -- Herrera, R -- Nunez, G -- CA-64556/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):687-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Comprehensive Cancer Center, University of Michigan Medical School, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381178" target="_blank"〉PubMed〈/a〉
    Keywords: Androstadienes/pharmacology ; Animals ; Apoptosis ; Carrier Proteins/*metabolism ; Cell Line ; Chromones/pharmacology ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; Interleukin-3/*pharmacology ; Mice ; Morpholines/pharmacology ; Phosphatidylinositol 3-Kinases/antagonists & inhibitors/*metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-akt ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Recombinant Proteins/metabolism ; Signal Transduction ; bcl-Associated Death Protein ; bcl-X Protein
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    Hyperplasia of lymphatic vessels in VEGF-C transgenic mice (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-30
    Description: No growth factors specific for the lymphatic vascular system have yet been described. Vascular endothelial growth factor (VEGF) regulates vascular permeability and angiogenesis, but does not promote lymphangiogenesis. Overexpression of VEGF-C, a ligand of the VEGF receptors VEGFR-3 and VEGFR-2, in the skin of transgenic mice resulted in lymphatic, but not vascular, endothelial proliferation and vessel enlargement. Thus, VEGF-C induces selective hyperplasia of the lymphatic vasculature, which is involved in the draining of interstitial fluid and in immune function, inflammation, and tumor metastasis. VEGF-C may play a role in disorders involving the lymphatic system and may be of potential use in therapeutic lymphangiogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jeltsch, M -- Kaipainen, A -- Joukov, V -- Meng, X -- Lakso, M -- Rauvala, H -- Swartz, M -- Fukumura, D -- Jain, R K -- Alitalo, K -- New York, N.Y. -- Science. 1997 May 30;276(5317):1423-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular/Cancer Biology Laboratory, Haartman Institute, University of Helsinki, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9162011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division ; Cloning, Molecular ; Endothelial Growth Factors/genetics/*physiology ; Endothelium, Lymphatic/physiology/ultrastructure ; Endothelium, Vascular/physiology ; Humans ; Hyperplasia ; Immunohistochemistry ; In Situ Hybridization ; Lymphatic System/*pathology ; Mice ; Mice, Inbred C57BL ; Mice, Inbred DBA ; Mice, Transgenic ; Molecular Sequence Data ; RNA, Messenger/metabolism ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptors, Cell Surface/metabolism ; Receptors, Growth Factor/metabolism ; Receptors, Vascular Endothelial Growth Factor ; Skin/pathology ; Vascular Endothelial Growth Factor C ; Vascular Endothelial Growth Factor Receptor-3
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    Activation of beta-catenin-Tcf signaling in colon cancer by mutations in beta-catenin or APC (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-21
    Description: Inactivation of the adenomatous polyposis coli (APC) tumor suppressor gene initiates colorectal neoplasia. One of the biochemical activities associated with the APC protein is down-regulation of transcriptional activation mediated by beta-catenin and T cell transcription factor 4 (Tcf-4). The protein products of mutant APC genes present in colorectal tumors were found to be defective in this activity. Furthermore, colorectal tumors with intact APC genes were found to contain activating mutations of beta-catenin that altered functionally significant phosphorylation sites. These results indicate that regulation of beta-catenin is critical to APC's tumor suppressive effect and that this regulation can be circumvented by mutations in either APC or beta-catenin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morin, P J -- Sparks, A B -- Korinek, V -- Barker, N -- Clevers, H -- Vogelstein, B -- Kinzler, K W -- CA57345/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 21;275(5307):1787-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Johns Hopkins Oncology Center, 424 North Bond Street, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9065402" target="_blank"〉PubMed〈/a〉
    Keywords: Adenomatous Polyposis Coli Protein ; Colonic Neoplasms/*genetics/metabolism ; Cytoskeletal Proteins/*genetics/*metabolism ; Gene Expression Regulation, Neoplastic ; *Genes, APC ; Genes, Reporter ; Germ-Line Mutation ; Humans ; Mutation ; Phosphorylation ; Signal Transduction ; TCF Transcription Factors ; *Trans-Activators ; Transcription Factor 7-Like 2 Protein ; Transcription Factors/*metabolism ; *Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; beta Catenin
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  • 42
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    Positive selection of T cells induced by viral delivery of neopeptides to the thymus (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-31
    Description: The relation between an antigenic peptide that can stimulate a mature T cell and the natural peptide that promoted selection of this cell in the thymus is still unknown. An experimental system was devised to address this issue in vivo-mice expressing neopeptides in thymic stromal cells after adenovirus-mediated delivery of invariant chain-peptide fusion proteins. In this system, selection of T cells capable of responding to a given antigenic peptide could be promoted by the peptide itself, by closely related analogs lacking agonist and antagonist activity, or by ostensibly unrelated peptides. However, the precise repertoire of T cells selected was dictated by the particular neopeptide expressed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakano, N -- Rooke, R -- Benoist, C -- Mathis, D -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):678-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Genetique et de Biologie Moleculaire et Cellulaire (INSERM, CNRS, Universite Louis Pasteur), 1 rue Laurent Fries, 67404 Illkirch, C.U. de Strasbourg, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005856" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Amino Acid Sequence ; Animals ; Antigen-Presenting Cells/immunology ; Antigens, Differentiation, B-Lymphocyte/genetics ; Cells, Cultured ; Cloning, Molecular ; Cross Reactions ; Cytochrome c Group/immunology ; DNA, Complementary/genetics ; Genetic Vectors ; Histocompatibility Antigens Class II/genetics ; Hybridomas ; Interleukin-2/biosynthesis ; *Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Peptides/chemistry/*immunology ; Receptors, Antigen, T-Cell/*immunology ; Recombinant Fusion Proteins ; T-Lymphocytes/*immunology ; Thymus Gland/cytology/*immunology
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    Dynamic molecular combing: stretching the whole human genome for high-resolution studies (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-05
    Description: DNA in amounts representative of hundreds of eukaryotic genomes was extended on silanized surfaces by dynamic molecular combing. The precise measurement of hybridized DNA probes was achieved directly without requiring normalization. This approach was validated with the high-resolution mapping of cosmid contigs on a yeast artificial chromosome (YAC) within yeast genomic DNA. It was extended to human genomic DNA for precise measurements ranging from 7 to 150 kilobases, of gaps within a contig, and of microdeletions in the tuberous sclerosis 2 gene on patients' DNA. The simplicity, reproducibility, and precision of this approach makes it a powerful tool for a variety of genomic studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Michalet, X -- Ekong, R -- Fougerousse, F -- Rousseaux, S -- Schurra, C -- Hornigold, N -- van Slegtenhorst, M -- Wolfe, J -- Povey, S -- Beckmann, J S -- Bensimon, A -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1518-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de Biophysique de l'ADN, Departement des Biotechnologies, Institut Pasteur, 25 rue du Dr. Roux, 75724 Paris Cedex 15, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278517" target="_blank"〉PubMed〈/a〉
    Keywords: Calpain/genetics ; Chromosome Mapping/*methods ; Chromosomes, Artificial, Yeast ; Cloning, Molecular ; Cosmids ; DNA Probes ; Electrophoresis, Gel, Pulsed-Field ; *Genetic Techniques ; *Genome, Fungal ; *Genome, Human ; Humans ; In Situ Hybridization, Fluorescence ; Isoenzymes/genetics ; *Muscle Proteins ; Muscular Dystrophies/genetics ; Mutation ; Proteins/genetics ; Repressor Proteins/genetics ; Reproducibility of Results ; Sequence Deletion ; Silanes ; Tuberous Sclerosis/genetics ; Tumor Suppressor Proteins
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    Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-28
    Description: The transcription factor NF-AT responds to Ca2+-calcineurin signals by translocating to the nucleus, where it participates in the activation of early immune response genes. Calcineurin dephosphorylates conserved serine residues in the amino terminus of NF-AT, resulting in nuclear import. Purification of the NF-AT kinase revealed that it is composed of a priming kinase activity and glycogen synthase kinase-3 (GSK-3). GSK-3 phosphorylates conserved serines necessary for nuclear export, promotes nuclear exit, and thereby opposes Ca2+-calcineurin signaling. Because GSK-3 responds to signals initiated by Wnt and other ligands, NF-AT family members could be effectors of these pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beals, C R -- Sheridan, C M -- Turck, C W -- Gardner, P -- Crabtree, G R -- New York, N.Y. -- Science. 1997 Mar 28;275(5308):1930-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Developmental Biology, Stanford University, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072970" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Transport ; Brain/enzymology ; COS Cells ; Calcineurin ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Calmodulin-Binding Proteins/metabolism ; Cell Nucleus/*metabolism ; Cloning, Molecular ; Cyclic AMP-Dependent Protein Kinases/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Glycogen Synthase Kinase 3 ; Glycogen Synthase Kinases ; Humans ; Molecular Sequence Data ; NFATC Transcription Factors ; *Nuclear Proteins ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Rats ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transcription Factors/genetics/*metabolism ; Transfection
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  • 45
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    How cells get the right chromosomes (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-31
    Description: When cells divide, the chromosomes must be delivered flawlessly to the daughter cells. Missing or extra chromosomes can result in birth defects and cancer. Chance events are the starting point for chromosome delivery, which makes the process prone to error. Errors are avoided by diverse uses of mechanical tension from mitotic forces. Tension stabilizes the proper chromosome configuration, controls a cell cycle checkpoint, and changes chromosome chemistry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nicklas, R B -- GM-13745/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):632-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, LSRC Building, Duke University, Box 91000, Durham, NC 27708-1000, USA. bnicklas@acpub.duke.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005842" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes/*metabolism ; Humans ; Kinetochores/*metabolism ; *Meiosis ; Microtubules/*metabolism ; *Mitosis ; Nuclear Proteins/metabolism ; Phosphorylation ; Selection, Genetic ; Spindle Apparatus/*metabolism ; Stress, Mechanical
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    Unusual oligomerization required for activity of NtrC, a bacterial enhancer-binding protein (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-14
    Description: Nitrogen regulatory protein C (NtrC) contacts a bacterial RNA polymerase from distant enhancers by means of DNA loops and activates transcription by allowing polymerase to gain access to the template DNA strand. It was shown that NtrC from Salmonella typhimurium must build large oligomers to activate transcription. In contrast to eukaryotic enhancer-binding proteins, most of which must bind directly to DNA, some NtrC dimers were bound solely by protein-protein interactions. NtrC oligomers were visualized with scanning force microscopy. Evidence of their functional importance was provided by showing that some inactive non-DNA-binding and DNA-binding mutant forms of NtrC can cooperate to activate transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wyman, C -- Rombel, I -- North, A K -- Bustamante, C -- Kustu, S -- GM17078/GM/NIGMS NIH HHS/ -- GM32543/GM/NIGMS NIH HHS/ -- GM38361/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 14;275(5306):1658-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant 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/9054362" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; *Bacterial Proteins ; DNA, Bacterial/*metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Dimerization ; Enhancer Elements, Genetic ; PII Nitrogen Regulatory Proteins ; Phosphorylation ; Promoter Regions, Genetic ; RNA Polymerase Sigma 54 ; Salmonella typhimurium/genetics/metabolism ; Sigma Factor/*metabolism ; *Trans-Activators ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic ; *Transcriptional Activation
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    A cyanobacterial phytochrome two-component light sensory system (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-05
    Description: The biliprotein phytochrome regulates plant growth and developmental responses to the ambient light environment through an unknown mechanism. Biochemical analyses demonstrate that phytochrome is an ancient molecule that evolved from a more compact light sensor in cyanobacteria. The cyanobacterial phytochrome Cph1 is a light-regulated histidine kinase that mediates red, far-red reversible phosphorylation of a small response regulator, Rcp1 (response regulator for cyanobacterial phytochrome), encoded by the adjacent gene, thus implicating protein phosphorylation-dephosphorylation in the initial step of light signal transduction by phytochrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yeh, K C -- Wu, S H -- Murphy, J T -- Lagarias, J C -- 1 P41 RR06009/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1505-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278513" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Proteins ; Cloning, Molecular ; Cyanobacteria/chemistry/genetics/*metabolism ; Genes, Bacterial ; *Light ; Molecular Sequence Data ; Operon ; Phosphorylation ; Protein Kinases/chemistry/genetics/*metabolism ; Proteins ; Recombinant Fusion Proteins/chemistry/metabolism ; Sequence Deletion ; Signal Transduction
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    Expression cloning in the test tube (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, R W -- Lustig, K D -- Stukenberg, P T -- McGarry, T J -- Kirschner, M W -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):973-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. king@bcmp.med.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9281074" target="_blank"〉PubMed〈/a〉
    Keywords: Apoptosis ; Cloning, Molecular/*methods ; DNA, Complementary/genetics ; Enzymes/metabolism ; Gene Expression ; Mitosis ; Phosphorylation ; Plasmids ; Protein Processing, Post-Translational ; Proteins/genetics/*metabolism
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  • 49
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    First nematode-resistance gene found (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moffat, A S -- New York, N.Y. -- Science. 1997 Feb 7;275(5301):757.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036535" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; *Genes, Plant ; Nematoda/*pathogenicity ; Plant Diseases/*genetics/parasitology ; Transformation, Genetic ; Vegetables/*genetics/*parasitology
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  • 50
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    Regulation of distinct stages of skeletal muscle differentiation by mitogen-activated protein kinases (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-21
    Description: The signal transduction pathway or pathways linking extracellular signals to myogenesis are poorly defined. Upon mitogen withdrawal from C2C12 myoblasts, the mitogen-activated protein kinase (MAPK) p42Erk2 is inactivated concomitant with up-regulation of muscle-specific genes. Overexpression of MAPK phosphatase-1 (MKP-1) inhibited p42Erk2 activity and was sufficient to relieve the inhibitory effects of mitogens on muscle-specific gene expression. Later during myogenesis, endogenous expression of MKP-1 decreased. MKP-1 overexpression during differentiation prevented myotube formation despite appropriate expression of myosin heavy chain. This indicates that muscle-specific gene expression is necessary but not sufficient to commit differentiated myocytes to myotubes and suggests a function for the MAPKs during the early and late stages of skeletal muscle differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bennett, A M -- Tonks, N K -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1288-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Demerec Building, 1 Bungtown Road, Post Office Box 100, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360925" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; *Cell Cycle Proteins ; Cell Differentiation ; Cell Division ; Cell Line ; Cloning, Molecular ; Culture Media ; Cyclin D1/genetics ; Dual Specificity Phosphatase 1 ; Gene Expression Regulation, Developmental ; Immediate-Early Proteins/genetics/*metabolism ; JNK Mitogen-Activated Protein Kinases ; Mice ; Mitogen-Activated Protein Kinase 1/antagonists & inhibitors/*metabolism ; *Mitogen-Activated Protein Kinases ; Mitogens/pharmacology ; Muscle Proteins/*genetics ; Muscle, Skeletal/*cytology/*enzymology/metabolism ; *Phosphoprotein Phosphatases ; Phosphorylation ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Tetracycline/pharmacology ; Transcription, Genetic
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    Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-05
    Description: The carboxyl-terminal domain, residues 146 to 231, of the human immunodeficiency virus-1 (HIV-1) capsid protein [CA(146-231)] is required for capsid dimerization and viral assembly. This domain contains a stretch of 20 residues, called the major homology region (MHR), which is conserved across retroviruses and is essential for viral assembly, maturation, and infectivity. The crystal structures of CA(146-231) and CA(151-231) reveal that the globular domain is composed of four helices and an extended amino-terminal strand. CA(146-231) dimerizes through parallel packing of helix 2 across a dyad. The MHR is distinct from the dimer interface and instead forms an intricate hydrogen-bonding network that interconnects strand 1 and helices 1 and 2. Alignment of the CA(146-231) dimer with the crystal structure of the capsid amino-terminal domain provides a model for the intact protein and extends models for assembly of the central conical core of HIV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gamble, T R -- Yoo, S -- Vajdos, F F -- von Schwedler, U K -- Worthylake, D K -- Wang, H -- McCutcheon, J P -- Sundquist, W I -- Hill, C P -- R01 AI40333/AI/NIAID NIH HHS/ -- R01 AI43036/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):849-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Utah, Salt Lake City, UT 84132, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9346481" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Capsid/*chemistry/genetics ; Cell Line ; Cloning, Molecular ; Cloning, Organism ; Crystallography, X-Ray ; Dimerization ; HIV-1/*chemistry/genetics/physiology ; Humans ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptidylprolyl Isomerase/chemistry ; *Protein Conformation ; Virus Replication
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  • 52
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    A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-29
    Description: Newly assembled major histocompatibility complex (MHC) class I molecules, together with the endoplasmic reticulum chaperone calreticulin, interact with the transporter associated with antigen processing (TAP) through a molecule called tapasin. The molecular cloning of tapasin revealed it to be a transmembrane glycoprotein encoded by an MHC-linked gene. It is a member of the immunoglobulin superfamily with a probable cytoplasmic endoplasmic reticulum retention signal. Up to four MHC class I-tapasin complexes were found to bind to each TAP molecule. Expression of tapasin in a negative mutant human cell line (220) restored class I-TAP association and normal class I cell surface expression. Tapasin expression also corrected the defective recognition of virus-infected 220 cells by class I-restricted cytotoxic T cells, establishing a critical functional role for tapasin in MHC class I-restricted antigen processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ortmann, B -- Copeman, J -- Lehner, P J -- Sadasivan, B -- Herberg, J A -- Grandea, A G -- Riddell, S R -- Tampe, R -- Spies, T -- Trowsdale, J -- Cresswell, P -- AI30581/AI/NIAID NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1997 Aug 29;277(5330):1306-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Section of Immunobiology, Yale University School of Medicine, 310 Cedar Street, New Haven, CT 06510, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9271576" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/*metabolism ; Amino Acid Sequence ; Antigen Presentation ; Antiporters/chemistry/genetics/*metabolism ; Calcium-Binding Proteins/metabolism ; Calreticulin ; Cell Line ; Cell Line, Transformed ; Chromosome Mapping ; Chromosomes, Human, Pair 6 ; Cloning, Molecular ; Dimerization ; Endoplasmic Reticulum/metabolism ; Genetic Linkage ; HLA Antigens/*metabolism ; Histocompatibility Antigens Class I/*metabolism ; Humans ; Immunoglobulin G/chemistry ; Immunoglobulins/chemistry/genetics/*metabolism ; Major Histocompatibility Complex/genetics ; Membrane Transport Proteins ; Molecular Sequence Data ; Ribonucleoproteins/metabolism ; Sequence Homology, Amino Acid ; T-Lymphocytes, Cytotoxic ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Maintenance of human T cell anergy: blocking of IL-2 gene transcription by activated Rap1 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-06
    Description: In the absence of costimulation, T cells activated through their antigen receptor become unresponsive (anergic) and do not transcribe the gene encoding interleukin-2 (IL-2) when restimulated with antigen. Anergic alloantigen-specific human T cells contained phosphorylated Cbl that coimmunoprecipitated with Fyn. The adapter protein CrkL was associated with both phosphorylated Cbl and the guanidine nucleotide-releasing factor C3G, which catalyzes guanosine triphosphate (GTP) exchange on Rap1. Active Rap1 (GTP-bound form) was present in anergic cells. Forced expression of low amounts of Rap1-GTP in Jurkat T cells recapitulated the anergic defect and blocked T cell antigen receptor (TCR)- and CD28-mediated IL-2 gene transcription. Therefore, Rap1 functions as a negative regulator of TCR-mediated IL-2 gene transcription and may be responsible for the specific defect in IL-2 production in T cell anergy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boussiotis, V A -- Freeman, G J -- Berezovskaya, A -- Barber, D L -- Nadler, L M -- AI 35225/AI/NIAID NIH HHS/ -- AI39671/AI/NIAID NIH HHS/ -- HL 54785/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 3;278(5335):124-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Adult Oncology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA. vassiliki_boussiotis@macmailgw.dfci.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9311917" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Antigens, CD28/immunology ; *Clonal Anergy ; GTP-Binding Proteins/*metabolism ; Gene Expression Regulation ; Guanine Nucleotide Exchange Factors ; Guanosine Triphosphate/metabolism ; Humans ; Interleukin-2/*genetics ; Jurkat Cells ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Proteins/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-cbl ; Proto-Oncogene Proteins c-fyn ; Receptors, Antigen, T-Cell/immunology ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; T-Lymphocytes/*immunology/metabolism ; *Transcription, Genetic ; Transfection ; *Ubiquitin-Protein Ligases ; rap GTP-Binding Proteins ; ras Guanine Nucleotide Exchange Factors ; ras Proteins/metabolism ; src Homology Domains
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    Defective TNF-alpha-induced apoptosis in STAT1-null cells due to low constitutive levels of caspases (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: Signal transducers and activators of transcription (STATs) enhance transcription of specific genes in response to cytokines and growth factors. STAT1 is also required for efficient constitutive expression of the caspases Ice, Cpp32, and Ich-1 in human fibroblasts. As a consequence, STAT1-null cells are resistant to apoptosis by tumor necrosis factor alpha (TNF-alpha). Reintroduction of STAT1alpha restored both TNF-alpha-induced apoptosis and the expression of Ice, Cpp32, and Ich-1. Variant STAT1 proteins carrying point mutations that inactivate domains required for STAT dimer formation nevertheless restored protease expression and sensitivity to apoptosis, indicating that the functions of STAT1 required for these activities are different from those that mediate induced gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kumar, A -- Commane, M -- Flickinger, T W -- Horvath, C M -- Stark, G R -- P01 CA62220/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1630-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Lerner Research Institute, The Cleveland Clinic Foundation, Cleveland, OH 44195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9374464" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Caspase 1 ; Caspase 2 ; Caspase 3 ; *Caspases ; Cell Line ; Cysteine Endopeptidases/genetics/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Dactinomycin/pharmacology ; Dimerization ; Gene Expression Regulation, Enzymologic ; Humans ; Interferon-gamma/pharmacology ; Phosphorylation ; Point Mutation ; Proteins/genetics/*metabolism ; STAT1 Transcription Factor ; Signal Transduction ; Trans-Activators/chemistry/genetics/*metabolism ; Transfection ; Tumor Necrosis Factor-alpha/*pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Control of filament formation in Candida albicans by the transcriptional repressor TUP1 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-04
    Description: The pathogenic yeast Candida albicans regulates its cellular morphology in response to environmental conditions. Ellipsoidal, single cells (blastospores) predominate in rich media, whereas filaments composed of elongated cells that are attached end-to-end form in response to starvation, serum, and other conditions. The TUP1 gene, which encodes a general transcriptional repressor in Saccharomyces cerevisiae, was isolated from C. albicans and disrupted. The resulting tup1 mutant strain of C. albicans grew exclusively as filaments under all conditions tested. TUP1 was epistatic to the transcriptional activator CPH1, previously found to promote filamentous growth. The results suggest a model where TUP1 represses genes responsible for initiating filamentous growth and this repression is lifted under inducing environmental conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Braun, B R -- Johnson, A D -- GM37049/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):105-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, University of California, San Francisco, 513 Parnassus Avenue, San Francisco, CA 94143-0414, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204892" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Candida albicans/*cytology/*genetics/growth & development/metabolism ; Cloning, Molecular ; Culture Media ; DNA-Binding Proteins/metabolism ; Epistasis, Genetic ; Fungal Proteins/chemistry/*genetics/*metabolism ; Gene Deletion ; Genes, Fungal ; Glycerol/metabolism ; Models, Genetic ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; Phenotype ; Repressor Proteins/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Temperature ; Transcription Factors/metabolism ; Transcription, Genetic
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    Flexibility in DNA recombination: structure of the lambda integrase catalytic core (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-04
    Description: Lambda integrase is archetypic of site-specific recombinases that catalyze intermolecular DNA rearrangements without energetic input. DNA cleavage, strand exchange, and religation steps are linked by a covalent phosphotyrosine intermediate in which Tyr342 is attached to the 3'-phosphate of the DNA cut site. The 1.9 angstrom crystal structure of the integrase catalytic domain reveals a protein fold that is conserved in organisms ranging from archaebacteria to yeast and that suggests a model for interaction with target DNA. The attacking Tyr342 nucleophile is located on a flexible loop about 20 angstroms from a basic groove that contains all the other catalytically essential residues. This bipartite active site can account for several apparently paradoxical features of integrase family recombinases, including the capacity for both cis and trans cleavage of DNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1839824/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1839824/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kwon, H J -- Tirumalai, R -- Landy, A -- Ellenberger, T -- AI13544/AI/NIAID NIH HHS/ -- GM33928/GM/NIGMS NIH HHS/ -- R01 GM033928/GM/NIGMS NIH HHS/ -- R01 GM062723/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Apr 4;276(5309):126-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9082984" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Attachment Sites, Microbiological ; Bacteriophage lambda/*enzymology ; Binding Sites ; Cloning, Molecular ; Conserved Sequence ; Crystallography, X-Ray ; DNA/*metabolism ; DNA Nucleotidyltransferases/chemistry/metabolism ; Hydrogen Bonding ; Integrases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Recombinases ; *Recombination, Genetic ; Tyrosine/chemistry/metabolism ; Virus Integration
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Mitotic and G2 checkpoint control: regulation of 14-3-3 protein binding by phosphorylation of Cdc25C on serine-216 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-05
    Description: Human Cdc25C is a dual-specificity protein phosphatase that controls entry into mitosis by dephosphorylating the protein kinase Cdc2. Throughout interphase, but not in mitosis, Cdc25C was phosphorylated on serine-216 and bound to members of the highly conserved and ubiquitously expressed family of 14-3-3 proteins. A mutation preventing phosphorylation of serine-216 abrogated 14-3-3 binding. Conditional overexpression of this mutant perturbed mitotic timing and allowed cells to escape the G2 checkpoint arrest induced by either unreplicated DNA or radiation-induced damage. Chk1, a fission yeast kinase involved in the DNA damage checkpoint response, phosphorylated Cdc25C in vitro on serine-216. These results indicate that serine-216 phosphorylation and 14-3-3 binding negatively regulate Cdc25C and identify Cdc25C as a potential target of checkpoint control in human cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peng, C Y -- Graves, P R -- Thoma, R S -- Wu, Z -- Shaw, A S -- Piwnica-Worms, H -- AI34094/AI/NIAID NIH HHS/ -- GM18428/GM/NIGMS NIH HHS/ -- GM47017/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1501-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology and Physiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9278512" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; Amino Acid Sequence ; Cell Cycle Proteins/*metabolism ; DNA Damage ; DNA Replication ; *G2 Phase ; Gamma Rays ; HeLa Cells ; Humans ; Jurkat Cells ; *Mitosis ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Phosphoserine/metabolism ; Protein Kinases/metabolism ; Proteins/*metabolism ; Recombinant Fusion Proteins/metabolism ; S Phase ; *Tyrosine 3-Monooxygenase ; *cdc25 Phosphatases
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A TEL-JAK2 fusion protein with constitutive kinase activity in human leukemia (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-21
    Description: The Janus family of tyrosine kinases (JAK) plays an essential role in development and in coupling cytokine receptors to downstream intracellular signaling events. A t(9;12)(p24;p13) chromosomal translocation in a T cell childhood acute lymphoblastic leukemia patient was characterized and shown to fuse the 3' portion of JAK2 to the 5' region of TEL, a gene encoding a member of the ETS transcription factor family. The TEL-JAK2 fusion protein includes the catalytic domain of JAK2 and the TEL-specific oligomerization domain. TEL-induced oligomerization of TEL-JAK2 resulted in the constitutive activation of its tyrosine kinase activity and conferred cytokine-independent proliferation to the interleukin-3-dependent Ba/F3 hematopoietic cell line.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lacronique, V -- Boureux, A -- Valle, V D -- Poirel, H -- Quang, C T -- Mauchauffe, M -- Berthou, C -- Lessard, M -- Berger, R -- Ghysdael, J -- Bernard, O A -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1309-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉U 301 de l'Institut National de la Sante et de la Recherche Medicale and SD 401 No. 301 CNRS, Institut de Genetique Moleculaire, 27 rue Juliette Dodu, 75010 Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360930" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Biopolymers ; Cell Division ; Cell Line ; Child, Preschool ; DNA-Binding Proteins/chemistry/genetics/metabolism ; Enzyme Activation ; Humans ; Interleukin-3/physiology ; Janus Kinase 2 ; Leukemia-Lymphoma, Adult T-Cell/genetics/*metabolism ; Male ; Mice ; *Milk Proteins ; Molecular Sequence Data ; Oncogene Proteins, Fusion/chemistry/genetics/*metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; *Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-ets ; *Repressor Proteins ; STAT5 Transcription Factor ; Signal Transduction ; Trans-Activators/metabolism ; Transcription Factors/chemistry/genetics/metabolism ; Transfection ; Translocation, Genetic
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    DCP-1, a Drosophila cell death protease essential for development (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-24
    Description: Apoptosis, a form of cellular suicide, involves the activation of CED-3-related cysteine proteases (caspases). The regulation of caspases by apoptotic signals and the precise mechanism by which they kill the cell remain unknown. In Drosophila, different death-inducing stimuli induce the expression of the apoptotic activator reaper. Cell killing by reaper and two genetically linked apoptotic activators, hid and grim, requires caspase activity. A Drosophila caspase, named Drosophila caspase-1 (DCP-1), was identified and found to be structurally and biochemically similar to Caenorhabditis elegans CED-3. Loss of zygotic DCP-1 function in Drosophila caused larval lethality and melanotic tumors, showing that this gene is essential for normal development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Song, Z -- McCall, K -- Steller, H -- New York, N.Y. -- Science. 1997 Jan 24;275(5299):536-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8999799" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; Caenorhabditis elegans Proteins ; *Caspases ; Cloning, Molecular ; Cysteine Endopeptidases/chemistry/genetics/*metabolism ; DNA Fragmentation ; DNA Transposable Elements ; Drosophila/embryology/*enzymology/genetics ; Drosophila Proteins ; Embryo, Nonmammalian/enzymology ; Gene Deletion ; Genes, Insect ; HeLa Cells ; Helminth Proteins/chemistry/metabolism ; Humans ; Molecular Sequence Data ; Mutation ; RNA, Messenger/genetics/metabolism ; Sequence Homology, Amino Acid
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    Functional coherence of the human Y chromosome (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-10-24
    Description: A systematic search of the nonrecombining region of the human Y chromosome (NRY) identified 12 novel genes or families, 10 with full-length complementary DNA sequences. All 12 genes, and six of eight NRY genes or families previously isolated by less systematic means, fell into two classes. Genes in the first group were expressed in many organs; these housekeeping genes have X homologs that escape X inactivation. The second group, consisting of Y-chromosomal gene families expressed specifically in testes, may account for infertility among men with Y deletions. The coherence of the NRY's gene content contrasts with the apparently haphazard content of most eukaryotic chromosomes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lahn, B T -- Page, D C -- New York, N.Y. -- Science. 1997 Oct 24;278(5338):675-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Whitehead Institute, and Department of Biology, Massachusetts Institute of Technology, 9 Cambridge Center, Cambridge, MA 02142, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9381176" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Biological Evolution ; Chromosome Mapping ; Cloning, Molecular ; DNA, Complementary ; Dosage Compensation, Genetic ; Gene Dosage ; Gene Expression ; *Genes ; Humans ; Infertility, Male/genetics ; Male ; Molecular Sequence Data ; Multigene Family ; Proteins ; Recombination, Genetic ; Repetitive Sequences, Nucleic Acid ; Seminal Plasma Proteins ; Sequence Analysis, DNA ; Spermatogenesis/genetics ; Testis/metabolism ; X Chromosome/genetics ; Y Chromosome/*genetics
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    Tyrosine phosphorylation of transmembrane ligands for Eph receptors (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-14
    Description: Axonal pathfinding in the nervous system is mediated in part by cell-to-cell signaling events involving members of the Eph receptor tyrosine kinase (RTK) family and their membrane-bound ligands. Genetic evidence suggests that transmembrane ligands may transduce signals in the developing embryo. The cytoplasmic domain of the transmembrane ligand Lerk2 became phosphorylated on tyrosine residues after contact with the Nuk/Cek5 receptor ectodomain, which suggests that Lerk2 has receptorlike intrinsic signaling potential. Moreover, Lerk2 is an in vivo substrate for the platelet-derived growth factor receptor, which suggests crosstalk between Lerk2 signaling and signaling cascades activated by tyrosine kinases. It is proposed that transmembrane ligands of Eph receptors act not only as conventional RTK ligands but also as receptorlike signaling molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bruckner, K -- Pasquale, E B -- Klein, R -- EY10576/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 14;275(5306):1640-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany. USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9054357" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Axons/physiology ; Brain-Derived Neurotrophic Factor/metabolism ; Cell Membrane/*metabolism ; Embryo, Mammalian/metabolism ; Ephrin-B1 ; Ligands ; Mice ; Phosphorylation ; Phosphotyrosine/*metabolism ; Platelet-Derived Growth Factor/pharmacology ; Proteins/*metabolism/pharmacology ; Receptor Protein-Tyrosine Kinases/*metabolism ; Receptor, Ciliary Neurotrophic Factor ; Receptor, EphB2 ; Receptors, Nerve Growth Factor/metabolism ; Receptors, Platelet-Derived Growth Factor/metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transfection
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    Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-04
    Description: The immunosuppressant rapamycin interferes with G1-phase progression in lymphoid and other cell types by inhibiting the function of the mammalian target of rapamycin (mTOR). mTOR was determined to be a terminal kinase in a signaling pathway that couples mitogenic stimulation to the phosphorylation of the eukaryotic initiation factor (eIF)-4E-binding protein, PHAS-I. The rapamycin-sensitive protein kinase activity of mTOR was required for phosphorylation of PHAS-I in insulin-stimulated human embryonic kidney cells. mTOR phosphorylated PHAS-I on serine and threonine residues in vitro, and these modifications inhibited the binding of PHAS-I to eIF-4E. These studies define a role for mTOR in translational control and offer further insights into the mechanism whereby rapamycin inhibits G1-phase progression in mammalian cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brunn, G J -- Hudson, C C -- Sekulic, A -- Williams, J M -- Hosoi, H -- Houghton, P J -- Lawrence, J C Jr -- Abraham, R T -- AR41189/AR/NIAMS NIH HHS/ -- DK28312/DK/NIDDK NIH HHS/ -- DK50628/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):99-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204908" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Androstadienes/pharmacology ; Animals ; Carrier Proteins/pharmacology ; Cell Line ; DNA-Binding Proteins/pharmacology ; Eukaryotic Initiation Factor-4E ; G1 Phase ; Heat-Shock Proteins/pharmacology ; Humans ; Insulin/pharmacology ; Peptide Initiation Factors/metabolism ; Phosphoproteins/genetics/*metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/antagonists & inhibitors/*metabolism ; Polyenes/*pharmacology ; *Protein Kinases ; Rats ; Recombinant Proteins/metabolism ; Repressor Proteins/genetics/*metabolism ; Signal Transduction ; Sirolimus ; TOR Serine-Threonine Kinases ; Tacrolimus Binding Proteins ; Transfection ; Tumor Cells, Cultured
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    Transgenic lambs from cloning lab (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1997 Aug 1;277(5326):631.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9254425" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Animals, Genetically Modified ; Cloning, Molecular ; Embryo Transfer ; Fetus/cytology ; Fibroblasts/cytology ; *Genetic Engineering ; Genetic Markers ; Humans ; Membrane Fusion ; Nuclear Transfer Techniques ; Ovum/physiology ; Sheep/embryology/*genetics ; *Transgenes
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-25
    Description: Protein kinase B (PKB) is a proto-oncogene that is activated in signaling pathways initiated by phosphoinositide 3-kinase. Chromatographic separation of brain cytosol revealed a kinase activity that phosphorylated and activated PKB only in the presence of phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4,5)P3]. Phosphorylation occurred exclusively on threonine-308, a residue implicated in activation of PKB in vivo. PtdIns(3,4,5)P3 was determined to have a dual role: Its binding to the pleckstrin homology domain of PKB was required to allow phosphorylation by the upstream kinase and it directly activated the upstream kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stokoe, D -- Stephens, L R -- Copeland, T -- Gaffney, P R -- Reese, C B -- Painter, G F -- Holmes, A B -- McCormick, F -- Hawkins, P T -- New York, N.Y. -- Science. 1997 Jul 25;277(5325):567-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Onyx Pharmaceuticals, 3031 Research Drive, Richmond, CA 94806, USA. stokoe@cc.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9228007" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Blood Proteins/chemistry ; Brain/enzymology ; COS Cells ; Cytosol/enzymology ; Enzyme Activation ; Humans ; Male ; Molecular Sequence Data ; Phosphatidylinositol Phosphates/*metabolism ; *Phosphoproteins ; Phosphorylation ; Phosphothreonine/metabolism ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Proto-Oncogene Proteins/chemistry/*metabolism ; Proto-Oncogene Proteins c-akt ; Rats ; Rats, Sprague-Dawley ; Signal Transduction ; Stereoisomerism
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    Merck gives researchers knockout deal (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):527.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9148409" target="_blank"〉PubMed〈/a〉
    Keywords: *Academies and Institutes/economics ; Animals ; Biotechnology ; Cloning, Molecular ; Costs and Cost Analysis ; Databases, Factual ; *Genetic Engineering ; Mice ; Mice, Knockout/*genetics ; Sequence Tagged Sites ; Stem Cells
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    Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: Niemann-Pick type C (NP-C) disease, a fatal neurovisceral disorder, is characterized by lysosomal accumulation of low density lipoprotein (LDL)-derived cholesterol. By positional cloning methods, a gene (NPC1) with insertion, deletion, and missense mutations has been identified in NP-C patients. Transfection of NP-C fibroblasts with wild-type NPC1 cDNA resulted in correction of their excessive lysosomal storage of LDL cholesterol, thereby defining the critical role of NPC1 in regulation of intracellular cholesterol trafficking. The 1278-amino acid NPC1 protein has sequence similarity to the morphogen receptor PATCHED and the putative sterol-sensing regions of SREBP cleavage-activating protein (SCAP) and 3-hydroxy-3-methyl-glutaryl coenzyme A (HMG-CoA) reductase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carstea, E D -- Morris, J A -- Coleman, K G -- Loftus, S K -- Zhang, D -- Cummings, C -- Gu, J -- Rosenfeld, M A -- Pavan, W J -- Krizman, D B -- Nagle, J -- Polymeropoulos, M H -- Sturley, S L -- Ioannou, Y A -- Higgins, M E -- Comly, M -- Cooney, A -- Brown, A -- Kaneski, C R -- Blanchette-Mackie, E J -- Dwyer, N K -- Neufeld, E B -- Chang, T Y -- Liscum, L -- Strauss, J F 3rd -- Ohno, K -- Zeigler, M -- Carmi, R -- Sokol, J -- Markie, D -- O'Neill, R R -- van Diggelen, O P -- Elleder, M -- Patterson, M C -- Brady, R O -- Vanier, M T -- Pentchev, P G -- Tagle, D A -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):228-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Neurological Disorders and Stroke, 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/9211849" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Carrier Proteins ; Cholesterol/*metabolism ; Cholesterol, LDL/metabolism ; Chromosome Mapping ; Chromosomes, Human, Pair 18 ; Cloning, Molecular ; *Drosophila Proteins ; Homeostasis ; Humans ; Hydroxymethylglutaryl CoA Reductases/chemistry ; Insect Proteins/chemistry ; Intracellular Signaling Peptides and Proteins ; Lysosomes/metabolism ; *Membrane Glycoproteins ; Membrane Proteins/chemistry ; Molecular Sequence Data ; Mutation ; Niemann-Pick Diseases/*genetics/metabolism ; Polymorphism, Single-Stranded Conformational ; Proteins/chemistry/*genetics/physiology ; Receptors, Cell Surface/chemistry ; Sequence Homology, Amino Acid ; Transfection
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    Receptor-mediated activation of a MAP kinase in pathogen defense of plants (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-27
    Description: Parsley cells recognize the fungal plant pathogen Phytophthora sojae through a plasma membrane receptor. A pathogen-derived oligopeptide elicitor binds to this receptor and thereby stimulates a multicomponent defense response through sequential activation of ion channels and an oxidative burst. An elicitor-responsive mitogen-activated protein (MAP) kinase was identified that acts downstream of the ion channels but independently or upstream of the oxidative burst. Upon receptor-mediated activation, the MAP kinase is translocated to the nucleus where it might interact with transcription factors that induce expression of defense genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ligterink, W -- Kroj, T -- zur Nieden, U -- Hirt, H -- Scheel, D -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):2054-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Microbiology and Genetics, Vienna Biocenter, Dr.-Bohr-Gasse 9, A-1030 Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9197271" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amphotericin B/pharmacology ; Anthracenes/pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases/chemistry/genetics/*metabolism ; Cell Nucleus/enzymology ; Cells, Cultured ; Enzyme Activation ; Fungal Proteins/*pharmacology ; Ion Channels/drug effects/metabolism ; Membrane Glycoproteins/*pharmacology ; Molecular Sequence Data ; Onium Compounds/pharmacology ; Peptide Fragments/pharmacology ; Phosphorylation ; Phytophthora/metabolism ; Plants/*enzymology/genetics/microbiology ; Respiratory Burst/drug effects
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    Will Dolly send in the clones? (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pennisi, E -- Williams, N -- New York, N.Y. -- Science. 1997 Mar 7;275(5305):1415-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072804" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation/genetics ; Cell Fusion ; Cell Nucleus/genetics ; Clone Cells ; Cloning, Molecular ; Embryo Transfer/veterinary ; *Embryonic and Fetal Development ; Female ; Gene Expression Regulation, Developmental ; *Genetic Engineering ; Humans ; Interphase ; Mammary Glands, Animal/cytology ; *Nuclear Transfer Techniques ; Ovum/cytology ; Reproduction, Asexual ; Sheep/embryology/*genetics
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    Regulation of NF-kappaB by cyclin-dependent kinases associated with the p300 coactivator (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-24
    Description: The nuclear factor kappaB (NF-kappaB) transcription factor is responsive to specific cytokines and stress and is often activated in association with cell damage and growth arrest in eukaryotes. NF-kappaB is a heterodimeric protein, typically composed of 50- and 65-kilodalton subunits of the Rel family, of which RelA(p65) stimulates transcription of diverse genes. Specific cyclin-dependent kinases (CDKs) were found to regulate transcriptional activation by NF-kappaB through interactions with the coactivator p300. The transcriptional activation domain of RelA(p65) interacted with an amino-terminal region of p300 distinct from a carboxyl-terminal region of p300 required for binding to the cyclin E-Cdk2 complex. The CDK inhibitor p21 or a dominant negative Cdk2, which inhibited p300-associated cyclin E-Cdk2 activity, stimulated kappaB-dependent gene expression, which was also enhanced by expression of p300 in the presence of p21. The interaction of NF-kappaB and CDKs through the p300 and CBP coactivators provides a mechanism for the coordination of transcriptional activation with cell cycle progression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perkins, N D -- Felzien, L K -- Betts, J C -- Leung, K -- Beach, D H -- Nabel, G J -- R01 AI29179/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 24;275(5299):523-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Michigan Medical Center, 4520 MSRB I, 1150 West Medical Center Drive, Ann Arbor, MI 48109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8999795" target="_blank"〉PubMed〈/a〉
    Keywords: *CDC2-CDC28 Kinases ; Cell Cycle ; Cell Line ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclin-Dependent Kinases/genetics/*metabolism ; Cyclins/genetics/metabolism ; Genes, Reporter ; Humans ; Jurkat Cells ; NF-kappa B/genetics/*metabolism ; Nuclear Proteins/genetics/*metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Signal Transduction ; Tetradecanoylphorbol Acetate/pharmacology ; *Trans-Activators ; Transcription Factor RelA ; Transcription Factors/genetics/*metabolism ; *Transcriptional Activation ; Transfection
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    daf-16: An HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-21
    Description: The wild-type Caenorhabditis elegans nematode ages rapidly, undergoing development, senescence, and death in less than 3 weeks. In contrast, mutants with reduced activity of the gene daf-2, a homolog of the insulin and insulin-like growth factor receptors, age more slowly than normal and live more than twice as long. These mutants are active and fully fertile and have normal metabolic rates. The life-span extension caused by daf-2 mutations requires the activity of the gene daf-16. daf-16 appears to play a unique role in life-span regulation and encodes a member of the hepatocyte nuclear factor 3 (HNF-3)/forkhead family of transcriptional regulators. In humans, insulin down-regulates the expression of certain genes by antagonizing the activity of HNF-3, raising the possibility that aspects of this regulatory system have been conserved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, K -- Dorman, J B -- Rodan, A -- Kenyon, C -- AG11816/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1319-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-0554, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360933" target="_blank"〉PubMed〈/a〉
    Keywords: Aging/genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Caenorhabditis elegans/*genetics/physiology ; *Caenorhabditis elegans Proteins ; Cloning, Molecular ; DNA, Complementary ; Forkhead Transcription Factors ; Genes, Helminth ; Humans ; Insulin/physiology ; Longevity/genetics ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/genetics ; Phenotype ; Receptor, Insulin/genetics/physiology ; Sequence Alignment ; Somatomedins/physiology ; Transcription Factors/chemistry/*genetics/*physiology
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    Specific inhibition of Stat3 signal transduction by PIAS3 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: The signal transducer and activator of transcription-3 (Stat3) protein is activated by the interleukin 6 (IL-6) family of cytokines, epidermal growth factor, and leptin. A protein named PIAS3 (protein inhibitor of activated STAT) that binds to Stat3 was isolated and characterized. The association of PIAS3 with Stat3 in vivo was only observed in cells stimulated with ligands that cause the activation of Stat3. PIAS3 blocked the DNA-binding activity of Stat3 and inhibited Stat3-mediated gene activation. Although Stat1 is also phosphorylated in response to IL-6, PIAS3 did not interact with Stat1 or affect its DNA-binding or transcriptional activity. The results indicate that PIAS3 is a specific inhibitor of Stat3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chung, C D -- Liao, J -- Liu, B -- Rao, X -- Jay, P -- Berta, P -- Shuai, K -- AI39612/AI/NIAID NIH HHS/ -- T32CA09056/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 5;278(5344):1803-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9388184" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism/pharmacology ; Cell Line ; DNA/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Gene Expression Regulation ; Humans ; Interferon Regulatory Factor-1 ; Interferon-alpha/pharmacology ; Interleukin-6/pharmacology ; *Intracellular Signaling Peptides and Proteins ; Mice ; Molecular Sequence Data ; NF-kappa B/metabolism ; Phosphoproteins/genetics ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Inhibitors of Activated STAT ; Recombinant Fusion Proteins/pharmacology ; STAT1 Transcription Factor ; STAT3 Transcription Factor ; *Signal Transduction ; Trans-Activators/*metabolism ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured ; Tumor Necrosis Factor-alpha/pharmacology
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    Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI 3-kinase gamma (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-17
    Description: The tyrosine kinase class of receptors induces mitogen-activated protein kinase (MAPK) activation through the sequential interaction of the signaling proteins Grb2, Sos, Ras, Raf, and MEK. Receptors coupled to heterotrimeric guanine triphosphate-binding protein (G protein) stimulate MAPK through Gbetagamma subunits, but the subsequent intervening molecules are still poorly defined. Overexpression of phosphoinositide 3-kinase gamma (PI3Kgamma) in COS-7 cells activated MAPK in a Gbetagamma-dependent fashion, and expression of a catalytically inactive mutant of PI3Kgamma abolished the stimulation of MAPK by Gbetagamma or in response to stimulation of muscarinic (m2) G protein-coupled receptors. Signaling from PI3Kgamma to MAPK appears to require a tyrosine kinase, Shc, Grb2, Sos, Ras, and Raf. These findings indicate that PI3Kgamma mediates Gbetagamma-dependent regulation of the MAPK signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lopez-Ilasaca, M -- Crespo, P -- Pellici, P G -- Gutkind, J S -- Wetzker, R -- New York, N.Y. -- Science. 1997 Jan 17;275(5298):394-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Research Unit Molecular Cell Biology, Medical Faculty, University of Jena, 07747 Jena, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8994038" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Androstadienes/pharmacology ; Animals ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Carbachol/pharmacology ; Cell Membrane/enzymology ; Enzyme Activation ; GRB2 Adaptor Protein ; GTP-Binding Proteins/*metabolism ; Guanine Nucleotide Exchange Factors ; Mitogen-Activated Protein Kinase 1 ; Phosphatidylinositol 3-Kinases ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/*metabolism ; Proteins/metabolism ; Receptor Protein-Tyrosine Kinases/metabolism ; Receptor, Muscarinic M2 ; Receptors, Muscarinic/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transfection ; Tyrosine/metabolism ; ras Guanine Nucleotide Exchange Factors ; ras Proteins/metabolism
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    Identification of maize histone deacetylase HD2 as an acidic nucleolar phosphoprotein (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-07-04
    Description: The steady state of histone acetylation is established and maintained by multiple histone acetyltransferases and deacetylases, and this steady state affects chromatin structure and function. The identification of a maize complementary DNA encoding the chromatin-bound deacetylase HD2 is reported. This protein was not homologous to the yeast RPD3 transcriptional regulator. It was expressed throughout embryo germination in correlation with the proliferative activity of cells. Antibodies against recombinant HD2-p39 immunoprecipitated the native enzyme complex, which was composed of phosphorylated p39 subunits. Immunofluorescence microscopy and sequence homologies suggested nucleolar localization. HD2 is an acidic nucleolar phosphoprotein that might regulate ribosomal chromatin structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lusser, A -- Brosch, G -- Loidl, A -- Haas, H -- Loidl, P -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):88-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Innsbruck Medical School, Fritz-Pregl-Str. 3, A-6020 Innsbruck, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9204905" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Sequence ; Base Sequence ; Cell Nucleolus/*enzymology ; Chromatin/metabolism ; Cloning, Molecular ; DNA, Complementary ; Germination ; Histone Deacetylases/*chemistry/genetics/isolation & purification/*metabolism ; Histones/metabolism ; Hydrogen-Ion Concentration ; Molecular Sequence Data ; Phosphoproteins/*chemistry/metabolism ; Phosphorylation ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Seeds/enzymology ; Zea mays/embryology/*enzymology
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    SBF cell cycle regulator as a target of the yeast PKC-MAP kinase pathway (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-03-21
    Description: Protein kinase C (PKC) signaling is highly conserved among eukaryotes and has been implicated in the regulation of cellular processes such as cell proliferation and growth. In the budding yeast, PKC1 functions to activate the SLT2(MPK1) mitogen-activated protein (MAP) kinase cascade, which is required for the maintenance of cell integrity during asymmetric cell growth. Genetic studies, coimmunoprecipitation experiments, and analysis of protein phosphorylation in vivo and in vitro indicate that the SBF transcription factor (composed of Swi4p and Swi6p), an important regulator of gene expression at the G1 to S phase cell cycle transition, is a target of the Slt2p(Mpk1p) MAP kinase. These studies provide evidence for a direct role of the PKC1 pathway in the regulation of the yeast cell cycle and cell growth and indicate that conserved signaling pathways can act to control key regulators of cell division.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Madden, K -- Sheu, Y J -- Baetz, K -- Andrews, B -- Snyder, M -- GM36494/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Mar 21;275(5307):1781-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Yale University, Post Office Box 208103, New Haven, CT 06520-8103, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9065400" target="_blank"〉PubMed〈/a〉
    Keywords: Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; *Cell Cycle ; Cyclins/genetics ; Fungal Proteins/genetics/*metabolism ; G1 Phase ; Gene Expression Regulation, Fungal ; *Mitogen-Activated Protein Kinases ; Phosphorylation ; Protein Kinase C/genetics/*metabolism ; S Phase ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Transcription Factors/genetics/*metabolism ; Transformation, Genetic ; Yeasts/cytology/genetics/growth & development/*metabolism
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    An NGF-TrkA-mediated retrograde signal to transcription factor CREB in sympathetic neurons (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-22
    Description: Nerve growth factor (NGF) is a neurotrophic factor secreted by cells that are the targets of innervation of sympathetic and some sensory neurons. However, the mechanism by which the NGF signal is propagated from the axon terminal to the cell body, which can be more than 1 meter away, to influence biochemical events critical for growth and survival of neurons has remained unclear. An NGF-mediated signal transmitted from the terminals and distal axons of cultured rat sympathetic neurons to their nuclei regulated phosphorylation of the transcription factor CREB (cyclic adenosine monophosphate response element-binding protein). Internalization of NGF and its receptor tyrosine kinase TrkA, and their transport to the cell body, were required for transmission of this signal. The tyrosine kinase activity of TrkA was required to maintain it in an autophosphorylated state upon its arrival in the cell body and for propagation of the signal to CREB within neuronal nuclei. Thus, an NGF-TrkA complex is a messenger that delivers the NGF signal from axon terminals to cell bodies of sympathetic neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Riccio, A -- Pierchala, B A -- Ciarallo, C L -- Ginty, D D -- New York, N.Y. -- Science. 1997 Aug 22;277(5329):1097-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9262478" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; *Axonal Transport ; Axons/*metabolism ; Carbazoles/pharmacology ; Cell Membrane/metabolism ; Cells, Cultured ; Cyclic AMP Response Element-Binding Protein/*metabolism ; Indole Alkaloids ; Microspheres ; Nerve Growth Factors/*metabolism/pharmacology ; Neurons/*metabolism ; Phosphorylation ; Proto-Oncogene Proteins/antagonists & inhibitors/*metabolism ; Rats ; Receptor Protein-Tyrosine Kinases/antagonists & inhibitors/*metabolism ; Receptor, trkA ; Receptors, Nerve Growth Factor/antagonists & inhibitors/*metabolism ; Signal Transduction ; Superior Cervical Ganglion/cytology
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    A G protein-coupled receptor phosphatase required for rhodopsin function (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-01
    Description: Heterotrimeric guanine nucleotide-binding protein (G protein)-coupled receptors are phosphorylated by kinases that mediate agonist-dependent receptor deactivation. Although many receptor kinases have been isolated, the corresponding phosphatases, necessary for restoring the ground state of the receptor, have not been identified. Drosophila RDGC (retinal degeneration C) is a phosphatase required for rhodopsin dephosphorylation in vivo. Loss of RDGC caused severe defects in the termination of the light response as well as extensive light-dependent retinal degeneration. These phenotypes resulted from the hyperphosphorylation of rhodopsin because expression of a truncated rhodopsin lacking the phosphorylation sites restored normal photoreceptor function. These results suggest the existence of a family of receptor phosphatases involved in the regulation of G protein-coupled signaling cascades.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vinos, J -- Jalink, K -- Hardy, R W -- Britt, S G -- Zuker, C S -- New York, N.Y. -- Science. 1997 Aug 1;277(5326):687-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biology, University of California at San Diego, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9235891" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Genetically Modified ; Arrestin/metabolism ; *Calcium-Binding Proteins ; Darkness ; Drosophila ; *Drosophila Proteins ; Electroretinography ; GTP-Binding Proteins/*metabolism ; Light ; Mutation ; Phosphoprotein Phosphatases/genetics/*metabolism ; Phosphorylation ; Photoreceptor Cells, Invertebrate/*metabolism ; Retina/metabolism ; Retinal Degeneration ; Rhodopsin/*metabolism ; Signal Transduction
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    Clinton urges outlawing human cloning (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, E -- New York, N.Y. -- Science. 1997 Jun 13;276(5319):1640.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9206825" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; *Bioethics ; Cloning, Molecular ; Embryo Research ; Federal Government ; Genetic Engineering/*legislation & jurisprudence ; *Government Regulation ; Humans ; Research ; Research Support as Topic ; United States
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    Induction of apoptosis by ASK1, a mammalian MAPKKK that activates SAPK/JNK and p38 signaling pathways (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-01-03
    Description: Mitogen-activated protein (MAP) kinase cascades are activated in response to various extracellular stimuli, including growth factors and environmental stresses. A MAP kinase kinase kinase (MAPKKK), termed ASK1, was identified that activated two different subgroups of MAP kinase kinases (MAPKK), SEK1 (or MKK4) and MKK3/MAPKK6 (or MKK6), which in turn activated stress-activated protein kinase (SAPK, also known as JNK; c-Jun amino-terminal kinase) and p38 subgroups of MAP kinases, respectively. Overexpression of ASK1 induced apoptotic cell death, and ASK1 was activated in cells treated with tumor necrosis factor-alpha (TNF-alpha). Moreover, TNF-alpha-induced apoptosis was inhibited by a catalytically inactive form of ASK1. ASK1 may be a key element in the mechanism of stress- and cytokine-induced apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ichijo, H -- Nishida, E -- Irie, K -- ten Dijke, P -- Saitoh, M -- Moriguchi, T -- Takagi, M -- Matsumoto, K -- Miyazono, K -- Gotoh, Y -- New York, N.Y. -- Science. 1997 Jan 3;275(5296):90-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, The Cancer Institute, Tokyo, Japanese Foundation for Cancer Research, 1-37-1 Kami-Ikebukuro, Toshima-ku, Tokyo 170, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8974401" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Apoptosis ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Division ; Cell Line ; Cell Survival ; Enzyme Activation ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase 6 ; MAP Kinase Kinase Kinases ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Polymerase Chain Reaction ; Protein-Serine-Threonine Kinases/chemistry/*metabolism ; Protein-Tyrosine Kinases/metabolism ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/genetics/growth & development/metabolism ; *Signal Transduction ; Transfection ; Tumor Necrosis Factor-alpha/pharmacology ; p38 Mitogen-Activated Protein Kinases
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    Akt signaling: linking membrane events to life and death decisions (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hemmings, B A -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):628-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher Institute, Post Office Box 2543, CH-4002, Basel, Switzerland. hemmings@fmi.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9019819" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cell Membrane/*metabolism ; Enzyme Activation ; Growth Substances/pharmacology ; Neurons/*cytology/metabolism ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; *Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-akt ; Second Messenger Systems ; *Signal Transduction
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    Activation of the G protein Gq/11 through tyrosine phosphorylation of the alpha subunit (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: Various receptors coupled to the heterotrimeric guanine nucleotide-binding protein Gq/11 stimulate formation of inositol-1,4,5-trisphosphate (IP3). Activation of these receptors also induces protein tyrosine phosphorylation. Formation of IP3 in response to stimulated receptors that couple to Gq/11 was blocked by protein tyrosine kinase inhibitors. These inhibitors appeared to act before activation of Gq/11. Moreover, stimulation of receptors coupled to Gq/11 induced phosphorylation on a tyrosine residue (Tyr356) of the Galphaq/11 subunit, and this tyrosine phosphorylation event was essential for Gq/11 activation. Tyrosine phosphorylation of Galphaq/11 induced changes in its interaction with receptors. Therefore, tyrosine phosphorylation of Galphaq/11 appears to regulate the activation of Gq/11 protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Umemori, H -- Inoue, T -- Kume, S -- Sekiyama, N -- Nagao, M -- Itoh, H -- Nakanishi, S -- Mikoshiba, K -- Yamamoto, T -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1878-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Oncology, Institute of Medical Science, University of Tokyo, Tokyo 108, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Calcium/metabolism ; Carbachol/pharmacology ; Cell Line ; Cricetinae ; Enzyme Inhibitors/pharmacology ; GTP-Binding Proteins/*metabolism ; Genistein ; Inositol 1,4,5-Trisphosphate/metabolism ; Isoflavones/pharmacology ; Phosphorylation ; Phosphotyrosine/*metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors/metabolism ; Receptors, Cholinergic/*metabolism ; Receptors, Metabotropic Glutamate/*metabolism ; Signal Transduction
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    ARF1, a transcription factor that binds to auxin response elements (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-06-20
    Description: The plant hormone auxin regulates plant physiology by modulating the interaction of transcription factors with auxin response elements (AuxREs) of the affected genes. A transcription factor, Auxin Response Factor 1 (ARF1), that binds to the sequence TGTCTC in AuxREs was cloned from Arabidopsis by using a yeast one-hybrid system. ARF1 has an amino-terminal DNA-binding domain related to the carboxyl terminus of the maize transactivator Viviparous-1. Sequence requirements for ARF1 binding in vitro are identical to those that confer auxin responsiveness in vivo. The carboxyl terminus of ARF1 contains two motifs found in the Aux/IAA class of proteins and appears to mediate protein-protein interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ulmasov, T -- Hagen, G -- Guilfoyle, T J -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1865-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188533" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics ; Arabidopsis Proteins ; Base Sequence ; Binding Sites ; Cloning, Molecular ; DNA, Plant/genetics/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Genes, Plant ; Indoleacetic Acids/*pharmacology ; Molecular Sequence Data ; Mutation ; Plant Proteins ; *Promoter Regions, Genetic ; *Repetitive Sequences, Nucleic Acid ; Transcription Factors/chemistry/genetics/*metabolism
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    A new player in cell death (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-12-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoey, T -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1578-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik, South San Francisco, CA 94080, USA. hoey@tularik.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9411781" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Caspase 1 ; Cell Line ; Cysteine Endopeptidases/metabolism ; DNA-Binding Proteins/chemistry/genetics/metabolism/*physiology ; Gene Expression Regulation ; Gene Expression Regulation, Enzymologic ; Humans ; Interferon Regulatory Factor-1 ; Interferon-gamma/pharmacology ; Models, Genetic ; Mutation ; Phosphoproteins/metabolism ; Phosphorylation ; STAT1 Transcription Factor ; *Signal Transduction ; Trans-Activators/chemistry/genetics/*physiology ; Transcription Factors/metabolism ; Tumor Necrosis Factor-alpha/pharmacology
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    Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-10-23
    Description: G1 cyclin-dependent kinase (Cdk)-triggered degradation of the S-phase Cdk inhibitor Sic1p has been implicated in the transition from G1 to S phase in the cell cycle of budding yeast. A multidimensional electrospray mass spectrometry technique was used to map G1 Cdk phosphorylation sites in Sic1p both in vitro and in vivo. A Sic1p mutant lacking three Cdk phosphorylation sites did not serve as a substrate for Cdc34p-dependent ubiquitination in vitro, was stable in vivo, and blocked DNA replication. Moreover, purified phosphoSic1p was ubiquitinated in cyclin-depleted G1 extract, indicating that a primary function of G1 cyclins is to tag Sic1p for destruction. These data suggest a molecular model of how phosphorylation and proteolysis cooperate to bring about the G1/S transition in budding yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verma, R -- Annan, R S -- Huddleston, M J -- Carr, S A -- Reynard, G -- Deshaies, R J -- R01 GM52466-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):455-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, Box 156-29, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9334303" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase-Promoting Complex-Cyclosome ; Cyclin G ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cyclin-Dependent Kinases/*metabolism ; Cyclins/*metabolism ; DNA Replication ; Enzyme Inhibitors/metabolism ; Fungal Proteins/*metabolism ; G1 Phase ; Ligases/metabolism ; Molecular Sequence Data ; Mutagenesis ; Phenotype ; Phosphopeptides/metabolism ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; *S Phase ; *Saccharomyces cerevisiae Proteins ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; Ubiquitins/metabolism ; Yeasts/*cytology/metabolism
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    Bacterial interference caused by autoinducing peptide variants (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-06-27
    Description: The synthesis of virulence factors and other extracellular proteins by Staphylococcus aureus is globally controlled by the agr locus, which encodes a two-component signaling pathway whose activating ligand is an agr-encoded autoinducing peptide. The cognate peptides produced by some strains inhibit the expression of agr in other strains, and the amino acid sequences of peptide and receptor are markedly different between such strains, suggesting a hypervariability-generating mechanism. Cross-inhibition of gene expression represents a type of bacterial interference that could be correlated with the ability of one strain to exclude others from infection or colonization sites, or both.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ji, G -- Beavis, R -- Novick, R P -- R01-AI30138/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):2027-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Skirball Institute of Biomolecular Medicine, New York University Medical Center, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9197262" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Antibiosis ; Bacterial Proteins/chemistry/*genetics/metabolism ; Cloning, Molecular ; Dimerization ; *Gene Expression Regulation, Bacterial ; Mass Spectrometry ; Molecular Sequence Data ; Peptides/chemistry/*genetics/metabolism ; Promoter Regions, Genetic ; Signal Transduction ; Staphylococcus aureus/*genetics/metabolism/pathogenicity ; *Trans-Activators ; Transcription Factors/chemistry/*genetics/metabolism ; Virulence
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    AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-08-15
    Description: Members of the recently recognized SRC-1 family of transcriptional coactivators interact with steroid hormone receptors to enhance ligand-dependent transcription. AIB1, a member of the SRC-1 family, was cloned during a search on the long arm of chromosome 20 for genes whose expression and copy number were elevated in human breast cancers. AIB1 amplification and overexpression were observed in four of five estrogen receptor-positive breast and ovarian cancer cell lines. Subsequent evaluation of 105 unselected specimens of primary breast cancer found AIB1 amplification in approximately 10 percent and high expression in 64 percent of the primary tumors analyzed. AIB1 protein interacted with estrogen receptors in a ligand-dependent fashion, and transfection of AIB1 resulted in enhancement of estrogen-dependent transcription. These observations identify AIB1 as a nuclear receptor coactivator whose altered expression may contribute to development of steroid-dependent cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anzick, S L -- Kononen, J -- Walker, R L -- Azorsa, D O -- Tanner, M M -- Guan, X Y -- Sauter, G -- Kallioniemi, O P -- Trent, J M -- Meltzer, P S -- New York, N.Y. -- Science. 1997 Aug 15;277(5328):965-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cancer Genetics, National Human Genome Research Institute, National Institutes of Health, Bethesda, MD, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9252329" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Breast/metabolism ; Breast Neoplasms/*genetics/metabolism ; Chromosomes, Human, Pair 20 ; Cloning, Molecular ; Estradiol/metabolism/pharmacology ; Female ; *Gene Amplification ; Gene Dosage ; Gene Expression Regulation, Neoplastic ; Histone Acetyltransferases ; Humans ; In Situ Hybridization, Fluorescence ; Ligands ; Molecular Sequence Data ; Neoplasms, Hormone-Dependent/*genetics/metabolism ; Nuclear Receptor Coactivator 1 ; Nuclear Receptor Coactivator 2 ; Ovarian Neoplasms/*genetics/metabolism ; Receptors, Estrogen/genetics/*metabolism ; Transcription Factors/genetics ; Transcriptional Activation ; Transfection ; Tumor Cells, Cultured
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    A DNA damage checkpoint meets the cell cycle engine (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-09-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weinert, T -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1450-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, University of Arizona, Tuscon, AZ 85721, USA. tedvweinert@tikal.biosci.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9304216" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; Animals ; CDC2 Protein Kinase/*metabolism ; Cell Cycle Proteins/metabolism ; *DNA Damage ; Fungal Proteins/metabolism ; *G2 Phase ; Humans ; Mice ; Models, Biological ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Proteins/metabolism ; S Phase ; Schizosaccharomyces/cytology/metabolism ; *Tyrosine 3-Monooxygenase ; cdc25 Phosphatases ; *ras-GRF1
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    A cytoplasmic inhibitor of the JNK signal transduction pathway (1997)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1997-08-01
    Description: The c-Jun amino-terminal kinase (JNK) is a member of the stress-activated group of mitogen-activated protein (MAP) kinases that are implicated in the control of cell growth. A murine cytoplasmic protein that binds specifically to JNK [the JNK interacting protein-1 (JIP-1)] was characterized and cloned. JIP-1 caused cytoplasmic retention of JNK and inhibition of JNK-regulated gene expression. In addition, JIP-1 suppressed the effects of the JNK signaling pathway on cellular proliferation, including transformation by the Bcr-Abl oncogene. This analysis identifies JIP-1 as a specific inhibitor of the JNK signal transduction pathway and establishes protein targeting as a mechanism that regulates signaling by stress-activated MAP kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dickens, M -- Rogers, J S -- Cavanagh, J -- Raitano, A -- Xia, Z -- Halpern, J R -- Greenberg, M E -- Sawyers, C L -- Davis, R J -- CA43855/CA/NCI NIH HHS/ -- CA65861/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Aug 1;277(5326):693-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9235893" target="_blank"〉PubMed〈/a〉
    Keywords: Activating Transcription Factor 2 ; Animals ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Carrier Proteins/chemistry/*metabolism ; Cell Nucleus/metabolism ; Cell Transformation, Neoplastic ; Cells, Cultured ; Cloning, Molecular ; Cyclic AMP Response Element-Binding Protein/metabolism ; Cytoplasm/metabolism ; Fusion Proteins, bcr-abl/metabolism ; Gene Expression Regulation ; JNK Mitogen-Activated Protein Kinases ; Mitogen-Activated Protein Kinase 9 ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Phosphorylation ; Protein Kinases/metabolism ; Proto-Oncogene Proteins c-jun/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transcription Factors/metabolism ; Transcriptional Activation ; Transfection
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    IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-05
    Description: Activation of the transcription factor nuclear factor kappa B (NF-kappaB) is controlled by sequential phosphorylation, ubiquitination, and degradation of its inhibitory subunit IkappaB. A large multiprotein complex, the IkappaB kinase (IKK) signalsome, was purified from HeLa cells and found to contain a cytokine-inducible IkappaB kinase activity that phosphorylates IkappaB-alpha and IkappaB-beta. Two components of the IKK signalsome, IKK-1 and IKK-2, were identified as closely related protein serine kinases containing leucine zipper and helix-loop-helix protein interaction motifs. Mutant versions of IKK-2 had pronounced effects on RelA nuclear translocation and NF-kappaB-dependent reporter activity, consistent with a critical role for the IKK kinases in the NF-kappaB signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mercurio, F -- Zhu, H -- Murray, B W -- Shevchenko, A -- Bennett, B L -- Li, J -- Young, D B -- Barbosa, M -- Mann, M -- Manning, A -- Rao, A -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):860-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Signal Pharmaceuticals, Inc., 5555 Oberlin Drive, San Diego, CA 92121, USA. fmercuri@signalpharm.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9346484" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Cycle Proteins ; Cloning, Molecular ; Dual Specificity Phosphatase 1 ; Enzyme Activation ; HeLa Cells ; Helix-Loop-Helix Motifs ; Humans ; I-kappa B Kinase ; Immediate-Early Proteins/metabolism ; Leucine Zippers ; Molecular Sequence Data ; NF-kappa B/*metabolism ; *Phosphoprotein Phosphatases ; Phosphorylation ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Sequence Homology, Amino Acid ; Substrate Specificity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 89
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    How jet-lag hormone does double duty in the brain (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1997 Jul 25;277(5325):480.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9254421" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Circadian Rhythm/*physiology ; Cloning, Molecular ; Humans ; Melatonin/*physiology ; Mice ; Mice, Knockout ; Neurons/physiology ; Receptors, Cell Surface/genetics/*physiology ; Receptors, Cytoplasmic and Nuclear/genetics/*physiology ; Receptors, Melatonin ; Reproduction ; Sleep/physiology ; Suprachiasmatic Nucleus/*physiology ; Wakefulness/physiology
    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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  • 90
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    As time PASses: the first mammalian clock gene (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kay, S A -- New York, N.Y. -- Science. 1997 May 16;276(5315):1093.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NSF Center for Biological Timing, Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA. stevek@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9173542" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Clocks/*genetics ; Circadian Rhythm/*genetics ; Cloning, Molecular ; Helix-Loop-Helix Motifs ; Mice ; Mutation
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  • 91
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    IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-05
    Description: Activation of the transcription factor nuclear factor kappa B (NF-kappaB) by inflammatory cytokines requires the successive action of NF-kappaB-inducing kinase (NIK) and IkappaB kinase-alpha (IKK-alpha). A widely expressed protein kinase was identified that is 52 percent identical to IKK-alpha. IkappaB kinase-beta (IKK-beta) activated NF-kappaB when overexpressed and phosphorylated serine residues 32 and 36 of IkappaB-alpha and serines 19 and 23 of IkappaB-beta. The activity of IKK-beta was stimulated by tumor necrosis factor and interleukin-1 treatment. IKK-alpha and IKK-beta formed heterodimers that interacted with NIK. Overexpression of a catalytically inactive form of IKK-beta blocked cytokine-induced NF-kappaB activation. Thus, an active IkappaB kinase complex may require three distinct protein kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Woronicz, J D -- Gao, X -- Cao, Z -- Rothe, M -- Goeddel, D V -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):866-9.〈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/9346485" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Line ; Cytokines/metabolism ; Enzyme Activation ; Genes, Reporter ; HeLa Cells ; Humans ; I-kappa B Kinase ; Molecular Sequence Data ; NF-kappa B/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Sequence Homology, Amino Acid ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    Role of the major antigen of Mycobacterium tuberculosis in cell wall biogenesis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-30
    Description: The dominant exported proteins and protective antigens of Mycobacterium tuberculosis are a triad of related gene products called the antigen 85 (Ag85) complex. Each has also been implicated in disease pathogenesis through its fibronectin-binding capacities. A carboxylesterase domain was found within the amino acid sequences of Ag85A, B, and C, and each protein acted as a mycolyltransferase involved in the final stages of mycobacterial cell wall assembly, as shown by direct enzyme assay and site-directed mutagenesis. Furthermore, the use of an antagonist (6-azido-6-deoxy-alpha, alpha'-trehalose) of this activity demonstrates that these proteins are essential and potential targets for new antimycobacterial drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Belisle, J T -- Vissa, V D -- Sievert, T -- Takayama, K -- Brennan, P J -- Besra, G S -- AI-18357/AI/NIAID NIH HHS/ -- AI-35220/AI/NIAID NIH HHS/ -- AI-38087/AI/NIAID NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 May 30;276(5317):1420-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Colorado State University, Fort Collins, CO 80523, USA. jbelisle@vines.colostate.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9162010" target="_blank"〉PubMed〈/a〉
    Keywords: *Acyltransferases ; Amino Acid Sequence ; Antigens, Bacterial/*physiology ; Azides/metabolism ; Bacterial Proteins/physiology ; Cell Wall/*metabolism ; Chromatography, Thin Layer ; Cloning, Molecular ; Cord Factors/antagonists & inhibitors/metabolism ; Escherichia coli/drug effects ; Esterification ; Molecular Sequence Data ; Mycobacterium tuberculosis/drug effects/enzymology/immunology/*physiology ; Mycolic Acids/metabolism ; Serine/metabolism ; Trehalose/analogs & derivatives/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-09
    Description: A new class of protein tyrosine kinase inhibitors was identified that is based on an oxindole core (indolinones). Two compounds from this class inhibited the kinase activity of fibroblast growth factor receptor 1 (FGFR1) and showed differential specificity toward other receptor tyrosine kinases. Crystal structures of the tyrosine kinase domain of FGFR1 in complex with the two compounds were determined. The oxindole occupies the site in which the adenine of adenosine triphosphate binds, whereas the moieties that extend from the oxindole contact residues in the hinge region between the two kinase lobes. The more specific inhibitor of FGFR1 induces a conformational change in the nucleotide-binding loop. This structural information will facilitate the design of new inhibitors for use in the treatment of cancer and other diseases in which cell signaling by tyrosine kinases plays a crucial role in disease pathogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mohammadi, M -- McMahon, G -- Sun, L -- Tang, C -- Hirth, P -- Yeh, B K -- Hubbard, S R -- Schlessinger, J -- New York, N.Y. -- Science. 1997 May 9;276(5314):955-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, New York University Medical Center, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9139660" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; Enzyme Inhibitors/chemistry/*metabolism/pharmacology ; Hydrogen Bonding ; Mice ; Models, Molecular ; Phosphorylation ; Phosphotyrosine/metabolism ; Piperazines/chemistry/*metabolism/pharmacology ; Protein-Tyrosine Kinases/antagonists & inhibitors/*chemistry/metabolism ; Pyrroles/chemistry/*metabolism/pharmacology ; *Receptor Protein-Tyrosine Kinases ; Receptor, Epidermal Growth Factor/antagonists & inhibitors/metabolism ; Receptor, Fibroblast Growth Factor, Type 1 ; Receptor, Insulin/antagonists & inhibitors/metabolism ; Receptors, Fibroblast Growth Factor/antagonists & ; inhibitors/*chemistry/metabolism ; Receptors, Platelet-Derived Growth Factor/antagonists & inhibitors/metabolism
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  • 94
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    Analysis of a chemical plant defense mechanism in grasses (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-01
    Description: In the Gramineae, the cyclic hydroxamic acids 2,4-dihydroxy-1, 4-benzoxazin-3-one (DIBOA) and 2,4-dihydroxy-7-methoxy-1, 4-benzoxazin-3-one (DIMBOA) form part of the defense against insects and microbial pathogens. Five genes, Bx1 through Bx5, are required for DIBOA biosynthesis in maize. The functions of these five genes, clustered on chromosome 4, were demonstrated in vitro. Bx1 encodes a tryptophan synthase alpha homolog that catalyzes the formation of indole for the production of secondary metabolites rather than tryptophan, thereby defining the branch point from primary to secondary metabolism. Bx2 through Bx5 encode cytochrome P450-dependent monooxygenases that catalyze four consecutive hydroxylations and one ring expansion to form the highly oxidized DIBOA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frey, M -- Chomet, P -- Glawischnig, E -- Stettner, C -- Grun, S -- Winklmair, A -- Eisenreich, W -- Bacher, A -- Meeley, R B -- Briggs, S P -- Simcox, K -- Gierl, A -- New York, N.Y. -- Science. 1997 Aug 1;277(5326):696-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Genetik, Technische Universitat Munchen, Lichtenbergstrasse 4, 85747 Garching, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9235894" target="_blank"〉PubMed〈/a〉
    Keywords: Benzoxazines ; Cloning, Molecular ; Crosses, Genetic ; Cytochrome P-450 Enzyme System/genetics/metabolism ; DNA Transposable Elements ; *Genes, Plant ; Hydroxylation ; Indoles/metabolism ; Molecular Sequence Data ; Oxazines/*metabolism ; Plant Shoots/metabolism ; Substrate Specificity ; Tryptophan Synthase/genetics/metabolism ; Zea mays/*genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 95
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    Ethical and policy issues of human cloning (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shapiro, H T -- New York, N.Y. -- Science. 1997 Jul 11;277(5323):195-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Bioethics Advisory Commission, Princeton, NJ 08544, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9235635" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; *Bioethics ; Cloning, Molecular ; Embryo Research ; Federal Government ; Financing, Government ; *Genetic Engineering ; Genetic Research ; Government Regulation ; Humans ; *Public Policy ; Reproduction, Asexual ; Research Support as Topic ; Risk Assessment ; United States
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    Cloning sparks calls for new laws (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, N -- New York, N.Y. -- Science. 1997 Mar 7;275(5305):1415.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072803" target="_blank"〉PubMed〈/a〉
    Keywords: Advisory Committees ; *Bioethics ; Clone Cells ; Cloning, Molecular ; Embryo Research ; *Embryo, Mammalian ; Europe ; Genetic Engineering/*legislation & jurisprudence ; *Government Regulation ; Humans ; *Internationality ; *Nuclear Transfer Techniques ; Research/*legislation & jurisprudence ; United States
    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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  • 97
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    Paths to activation of transcription (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geiduschek, E P -- New York, N.Y. -- Science. 1997 Mar 14;275(5306):1614-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Center for Molecular Genetics, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0634, USA. epg@jeeves.ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072826" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; *Bacterial Proteins ; Coliphages/genetics ; DNA, Bacterial/metabolism ; DNA-Binding Proteins/metabolism ; DNA-Directed RNA Polymerases/chemistry/*metabolism ; Enhancer Elements, Genetic ; PII Nitrogen Regulatory Proteins ; Phosphorylation ; Promoter Regions, Genetic ; RNA Polymerase Sigma 54 ; Salmonella typhimurium/genetics ; Sigma Factor/metabolism ; *Trans-Activators ; Transcription Factors/*metabolism ; *Transcription, Genetic ; *Transcriptional Activation
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  • 98
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    Transformation of chicken cells by the gene encoding the catalytic subunit of PI 3-kinase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-20
    Description: The avian sarcoma virus 16 (ASV 16) is a retrovirus that induces hemangiosarcomas in chickens. Analysis of the ASV 16 genome revealed that it encodes an oncogene that is derived from the cellular gene for the catalytic subunit of phosphoinositide 3-kinase (PI 3-kinase). The gene is referred to as v-p3k, and like its cellular counterpart c-p3k, it is a potent transforming gene in cultured chicken embryo fibroblasts (CEFs). The products of the viral and cellular p3k genes have PI 3-kinase activity. CEFs transformed with either gene showed elevated levels of phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate and activation of Akt kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, H W -- Aoki, M -- Fruman, D -- Auger, K R -- Bellacosa, A -- Tsichlis, P N -- Cantley, L C -- Roberts, T M -- Vogt, P K -- CA 42564/CA/NCI NIH HHS/ -- GM 41890/GM/NIGMS NIH HHS/ -- R01 GM041890/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jun 20;276(5320):1848-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Experimental Medicine, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9188528" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Avian Sarcoma Viruses/*genetics/physiology ; *Cell Transformation, Neoplastic ; *Cell Transformation, Viral ; Cells, Cultured ; Chick Embryo ; Chickens ; Cloning, Molecular ; Enzyme Activation ; Genes, Viral ; Hemangiosarcoma/genetics/virology ; Molecular Sequence Data ; *Oncogenes ; Phosphatidylinositol 3-Kinases ; Phosphatidylinositol Phosphates/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/*genetics/metabolism ; Platelet-Derived Growth Factor/pharmacology ; Protein-Serine-Threonine Kinases/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Signal Transduction ; Transfection
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  • 99
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    25-Hydroxyvitamin D3 1alpha-hydroxylase and vitamin D synthesis (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-20
    Description: Renal 25-hydroxyvitamin D3 1alpha-hydroxylase [1alpha(OH)ase] catalyzes metabolic activation of 25-hydroxyvitamin D3 into 1alpha, 25-dihydroxyvitamin D3 [1alpha,25(OH)2D3], an active form of vitamin D, and is inhibited by 1alpha,25(OH)2D3. 1alpha(OH)ase, which was cloned from the kidney of mice lacking the vitamin D receptor (VDR-/- mice), is a member of the P450 family of enzymes (P450VD1alpha). Expression of 1alpha(OH)ase was suppressed by 1alpha, 25(OH)2D3 in VDR+/+ and VDR+/- mice but not in VDR-/- mice. These results indicate that the negative feedback regulation of active vitamin D synthesis is mediated by 1alpha(OH)ase through liganded VDR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takeyama, K -- Kitanaka, S -- Sato, T -- Kobori, M -- Yanagisawa, J -- Kato, S -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1827-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9295274" target="_blank"〉PubMed〈/a〉
    Keywords: 25-Hydroxyvitamin D3 1-alpha-Hydroxylase/*genetics/*metabolism ; Amino Acid Sequence ; Animals ; COS Cells ; Calcifediol/metabolism ; Calcitriol/*biosynthesis/metabolism/pharmacology ; Cloning, Molecular ; Feedback ; *Gene Expression Regulation, Enzymologic ; Kidney/enzymology/metabolism ; Ligands ; Mice ; Mice, Knockout ; Molecular Sequence Data ; RNA, Messenger/genetics/metabolism ; Receptors, Calcitriol/metabolism ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    STAT3 as an adapter to couple phosphatidylinositol 3-kinase to the IFNAR1 chain of the type I interferon receptor (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-30
    Description: STAT (signal transducers and activators of transcription) proteins undergo cytokine-dependent phosphorylation on serine and tyrosine. STAT3, a transcription factor for acute phase response genes, was found to act as an adapter molecule in signal transduction from the type I interferon receptor. STAT3 bound to a conserved sequence in the cytoplasmic tail of the IFNAR1 chain of the receptor and underwent interferon-dependent tyrosine phosphorylation. The p85 regulatory subunit of phosphatidylinositol 3-kinase, which activates a series of serine kinases, bound to phosphorylated STAT3 and subsequently underwent tyrosine phosphorylation. Thus, STAT3 acts as an adapter to couple another signaling pathway to the interferon receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfeffer, L M -- Mullersman, J E -- Pfeffer, S R -- Murti, A -- Shi, W -- Yang, C H -- New York, N.Y. -- Science. 1997 May 30;276(5317):1418-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Tennessee Health Science Center, Memphis, TN 38163, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9162009" target="_blank"〉PubMed〈/a〉
    Keywords: Acute-Phase Proteins/*genetics ; Amino Acid Sequence ; Androstadienes/pharmacology ; Animals ; Binding Sites ; COS Cells ; Cell Line ; Cloning, Molecular ; Conserved Sequence ; DNA-Binding Proteins/genetics/*metabolism ; Enzyme Inhibitors/pharmacology ; Membrane Proteins ; Molecular Sequence Data ; Phosphatidylinositol 3-Kinases ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/antagonists & ; inhibitors/genetics/*metabolism ; Point Mutation ; Protein Binding ; Receptor, Interferon alpha-beta ; Receptors, Interferon/*metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; STAT3 Transcription Factor ; Signal Transduction ; Trans-Activators/genetics/*metabolism ; Tyrosine/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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