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  • Articles  (53)
  • Cloning, Molecular  (53)
  • American Association for the Advancement of Science (AAAS)  (53)
  • American Institute of Physics (AIP)
  • American Society of Hematology
  • EMBO Press
  • Essen : Verl. Glückauf
  • 2005-2009
  • 1995-1999  (53)
  • 1997  (53)
Collection
  • Articles  (53)
Publisher
  • American Association for the Advancement of Science (AAAS)  (53)
  • American Institute of Physics (AIP)
  • American Society of Hematology
  • EMBO Press
  • Essen : Verl. Glückauf
Years
  • 2005-2009
  • 1995-1999  (53)
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    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
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  • 2
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    American Association for the Advancement of Science (AAAS)
    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
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  • 3
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    American Association for the Advancement of Science (AAAS)
    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
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  • 4
    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
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  • 5
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    American Association for the Advancement of Science (AAAS)
    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
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  • 6
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    American Association for the Advancement of Science (AAAS)
    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
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  • 7
    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
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  • 8
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    American Association for the Advancement of Science (AAAS)
    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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  • 9
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    American Association for the Advancement of Science (AAAS)
    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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  • 10
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    American Association for the Advancement of Science (AAAS)
    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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  • 11
    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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  • 12
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    American Association for the Advancement of Science (AAAS)
    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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  • 13
    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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  • 14
    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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  • 15
    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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  • 16
    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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  • 17
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    American Association for the Advancement of Science (AAAS)
    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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  • 18
    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
    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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  • 19
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    American Association for the Advancement of Science (AAAS)
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 21
    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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  • 22
    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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  • 23
    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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  • 24
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    American Association for the Advancement of Science (AAAS)
    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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  • 25
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    American Association for the Advancement of Science (AAAS)
    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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  • 26
    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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  • 27
    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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  • 28
    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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  • 29
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    American Association for the Advancement of Science (AAAS)
    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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  • 30
    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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  • 31
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    American Association for the Advancement of Science (AAAS)
    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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  • 32
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    American Association for the Advancement of Science (AAAS)
    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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  • 33
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    American Association for the Advancement of Science (AAAS)
    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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  • 34
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    American Association for the Advancement of Science (AAAS)
    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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  • 35
    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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  • 36
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    American Association for the Advancement of Science (AAAS)
    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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  • 37
    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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  • 38
    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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  • 39
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    American Association for the Advancement of Science (AAAS)
    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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  • 40
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    American Association for the Advancement of Science (AAAS)
    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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  • 41
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    American Association for the Advancement of Science (AAAS)
    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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  • 42
    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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  • 43
    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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  • 44
    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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  • 45
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    American Association for the Advancement of Science (AAAS)
    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
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 46
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    American Association for the Advancement of Science (AAAS)
    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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  • 47
    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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  • 48
    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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  • 49
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    American Association for the Advancement of Science (AAAS)
    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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  • 50
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    American Association for the Advancement of Science (AAAS)
    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
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  • 51
    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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  • 52
    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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  • 53
    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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