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  • Molecular Sequence Data  (51)
  • Cell Line  (27)
  • American Association for the Advancement of Science (AAAS)  (68)
  • Springer Nature
  • 2000-2004
  • 1995-1999  (68)
  • 1980-1984
  • 1940-1944
  • 1998  (68)
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  • American Association for the Advancement of Science (AAAS)  (68)
  • Springer Nature
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  • 2000-2004
  • 1995-1999  (68)
  • 1980-1984
  • 1940-1944
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  • 1
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    Mutation of a gene encoding a protein with extracellular matrix motifs in Usher syndrome type IIa (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-20
    Description: Usher syndrome type IIa (OMIM 276901), an autosomal recessive disorder characterized by moderate to severe sensorineural hearing loss and progressive retinitis pigmentosa, maps to the long arm of human chromosome 1q41 between markers AFM268ZD1 and AFM144XF2. Three biologically important mutations in Usher syndrome type IIa patients were identified in a gene (USH2A) isolated from this critical region. The USH2A gene encodes a protein with a predicted size of 171.5 kilodaltons that has laminin epidermal growth factor and fibronectin type III motifs; these motifs are most commonly observed in proteins comprising components of the basal lamina and extracellular matrixes and in cell adhesion molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eudy, J D -- Weston, M D -- Yao, S -- Hoover, D M -- Rehm, H L -- Ma-Edmonds, M -- Yan, D -- Ahmad, I -- Cheng, J J -- Ayuso, C -- Cremers, C -- Davenport, S -- Moller, C -- Talmadge, C B -- Beisel, K W -- Tamayo, M -- Morton, C C -- Swaroop, A -- Kimberling, W J -- Sumegi, J -- 5PO1 DC01813-05/DC/NIDCD NIH HHS/ -- DC03402/DC/NIDCD NIH HHS/ -- EY07003/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 12;280(5370):1753-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, NE 68198, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9624053" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Adhesion Molecules/chemistry ; Chromosome Mapping ; Chromosomes, Human, Pair 1 ; Cochlea/chemistry ; Epidermal Growth Factor/chemistry ; Extracellular Matrix Proteins/chemistry/*genetics/physiology ; Female ; Fibronectins/chemistry ; Frameshift Mutation ; Gene Expression ; Genes, Recessive ; Glycosylation ; Hearing Loss, Sensorineural/*genetics ; Humans ; Laminin/chemistry ; Male ; Molecular Sequence Data ; Pedigree ; Retina/chemistry ; Retinitis Pigmentosa/*genetics ; Syndrome ; Tumor Cells, Cultured
    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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    Chromosome 2 sequence of the human malaria parasite Plasmodium falciparum (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-06
    Description: Chromosome 2 of Plasmodium falciparum was sequenced; this sequence contains 947,103 base pairs and encodes 210 predicted genes. In comparison with the Saccharomyces cerevisiae genome, chromosome 2 has a lower gene density, introns are more frequent, and proteins are markedly enriched in nonglobular domains. A family of surface proteins, rifins, that may play a role in antigenic variation was identified. The complete sequencing of chromosome 2 has shown that sequencing of the A+T-rich P. falciparum genome is technically feasible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gardner, M J -- Tettelin, H -- Carucci, D J -- Cummings, L M -- Aravind, L -- Koonin, E V -- Shallom, S -- Mason, T -- Yu, K -- Fujii, C -- Pederson, J -- Shen, K -- Jing, J -- Aston, C -- Lai, Z -- Schwartz, D C -- Pertea, M -- Salzberg, S -- Zhou, L -- Sutton, G G -- Clayton, R -- White, O -- Smith, H O -- Fraser, C M -- Adams, M D -- Venter, J C -- Hoffman, S L -- R01 AI40125-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 6;282(5391):1126-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genomic Research, Rockville, MD 20850, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9804551" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Protozoan/chemistry/genetics ; Base Composition ; Chromosomes/*genetics ; Evolution, Molecular ; *Genes, Protozoan ; Genome, Protozoan ; Introns ; Membrane Proteins/chemistry/genetics ; Molecular Sequence Data ; Multigene Family ; Physical Chromosome Mapping ; Plasmodium falciparum/*genetics ; Protozoan Proteins/chemistry/*genetics ; RNA, Protozoan/genetics ; RNA, Transfer, Glu/genetics ; Repetitive Sequences, Nucleic Acid ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Alignment ; *Sequence Analysis, DNA
    Print ISSN: 0036-8075
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  • 3
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    A carrot leucine-rich-repeat protein that inhibits ice recrystallization (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-10-02
    Description: Many organisms adapted to live at subzero temperatures express antifreeze proteins that improve their tolerance to freezing. Although structurally diverse, all antifreeze proteins interact with ice surfaces, depress the freezing temperature of aqueous solutions, and inhibit ice crystal growth. A protein purified from carrot shares these functional features with antifreeze proteins of fish. Expression of the carrot complementary DNA in tobacco resulted in the accumulation of antifreeze activity in the apoplast of plants grown at greenhouse temperatures. The sequence of carrot antifreeze protein is similar to that of polygalacturonase inhibitor proteins and contains leucine-rich repeats.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worrall, D -- Elias, L -- Ashford, D -- Smallwood, M -- Sidebottom, C -- Lillford, P -- Telford, J -- Holt, C -- Bowles, D -- New York, N.Y. -- Science. 1998 Oct 2;282(5386):115-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Plant Laboratory, Biology Department, University of York, Post Office Box 373, York, YO1 5YW, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9756474" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antifreeze Proteins ; Cloning, Molecular ; Crystallization ; DNA, Complementary ; Daucus carota/*chemistry/physiology ; Glycoproteins/*chemistry/genetics/isolation & purification/*physiology ; Glycosylation ; *Ice ; Isoelectric Point ; Leucine/chemistry ; Membrane Proteins/*chemistry/isolation & purification/*physiology/secretion ; Molecular Sequence Data ; Molecular Weight ; Plant Proteins/*chemistry/genetics/isolation & purification/*physiology ; Plant Roots/chemistry ; Plants, Genetically Modified ; Plants, Toxic ; Tobacco
    Print ISSN: 0036-8075
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  • 4
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    Inhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-11
    Description: Although isoniazid (isonicotinic acid hydrazide, INH) is widely used for the treatment of tuberculosis, its molecular target has remained elusive. In response to INH treatment, saturated hexacosanoic acid (C26:0) accumulated on a 12-kilodalton acyl carrier protein (AcpM) that normally carried mycolic acid precursors as long as C50. A protein species purified from INH-treated Mycobacterium tuberculosis was shown to consist of a covalent complex of INH, AcpM, and a beta-ketoacyl acyl carrier protein synthase, KasA. Amino acid-altering mutations in the KasA protein were identified in INH-resistant patient isolates that lacked other mutations associated with resistance to this drug.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mdluli, K -- Slayden, R A -- Zhu, Y -- Ramaswamy, S -- Pan, X -- Mead, D -- Crane, D D -- Musser, J M -- Barry, C E 3rd -- AI37004/AI/NIAID NIH HHS/ -- Z01 AI000783-11/Intramural NIH HHS/ -- New York, N.Y. -- Science. 1998 Jun 5;280(5369):1607-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tuberculosis Research Unit, Laboratory of Intracellular Parasites, Rocky Mountain Laboratories, National Institute for Allergy and Infectious Diseases (NIAID), National Institutes of Health, Hamilton, MT 59840, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9616124" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/*antagonists & ; inhibitors/chemistry/genetics ; Acyl Carrier Protein/chemistry/genetics/metabolism ; Amino Acid Sequence ; Antitubercular Agents/*pharmacology ; Drug Resistance, Microbial ; Enzyme Inhibitors/pharmacology ; Fatty Acids/metabolism ; Genes, Bacterial ; Humans ; Isoniazid/*pharmacology ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Mycobacterium tuberculosis/drug effects/*enzymology/genetics ; Mycolic Acids/metabolism ; Tuberculosis/microbiology ; Up-Regulation
    Print ISSN: 0036-8075
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  • 5
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    Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-02-07
    Description: The bacterium Helicobacter pylori is the causative agent for peptic ulcer disease. Bacterial adherence to the human gastric epithelial lining is mediated by the fucosylated Lewis b (Leb) histo-blood group antigen. The Leb-binding adhesin, BabA, was purified by receptor activity-directed affinity tagging. The bacterial Leb-binding phenotype was associated with the presence of the cag pathogenicity island among clinical isolates of H. pylori. A vaccine strategy based on the BabA adhesin might serve as a means to target the virulent type I strains of H. pylori.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ilver, D -- Arnqvist, A -- Ogren, J -- Frick, I M -- Kersulyte, D -- Incecik, E T -- Berg, D E -- Covacci, A -- Engstrand, L -- Boren, T -- New York, N.Y. -- Science. 1998 Jan 16;279(5349):373-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Umea University, SE-901 87 Umea, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9430586" target="_blank"〉PubMed〈/a〉
    Keywords: Adhesins, Bacterial/chemistry/genetics/*isolation & purification/metabolism ; Amino Acid Sequence ; *Antigens, Bacterial ; Bacterial Adhesion ; Bacterial Proteins/genetics/physiology ; Base Composition ; Base Sequence ; Biotinylation ; Cell Membrane/chemistry ; Cloning, Molecular ; Codon, Initiator ; Fucose ; Gastric Mucosa/microbiology ; Genes, Bacterial ; Glycoconjugates/metabolism ; Helicobacter pylori/isolation & purification/*metabolism/pathogenicity ; Humans ; Lewis Blood-Group System/*metabolism ; Ligands ; Molecular Sequence Data ; Virulence
    Print ISSN: 0036-8075
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  • 6
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    Genetic evaluation of suspected cases of transient HIV-1 infection of infants (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-06-06
    Description: Detection of human immunodeficiency virus-type 1 (HIV-1) on only one or a few occasions in infants born to infected mothers has been interpreted to indicate that infection may be transient rather than persistent. Forty-two cases of suspected transient HIV-1 viremia among 1562 perinatally exposed seroreverting infants and one mother were reanalyzed. HIV-1 env sequences were not found in specimens from 20; in specimens from 6, somatic genetic analysis revealed that specimens were mistakenly attributed to an infant; and in specimens from 17, phylogenetic analysis failed to demonstrate the expected linkage between the infant's and the mother's virus. These findings argue that transient HIV-1 infection, if it exists, will only rarely be satisfactorily documented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frenkel, L M -- Mullins, J I -- Learn, G H -- Manns-Arcuino, L -- Herring, B L -- Kalish, M L -- Steketee, R W -- Thea, D M -- Nichols, J E -- Liu, S L -- Harmache, A -- He, X -- Muthui, D -- Madan, A -- Hood, L -- Haase, A T -- Zupancic, M -- Staskus, K -- Wolinsky, S -- Krogstad, P -- Zhao, J -- Chen, I -- Koup, R -- Ho, D -- Korber, B -- Apple, R J -- Coombs, R W -- Pahwa, S -- Roberts, N J Jr -- AI27757/AI/NIAID NIH HHS/ -- AI32910/AI/NIAID NIH HHS/ -- UO1-27658/PHS HHS/ -- etc. -- New York, N.Y. -- Science. 1998 May 15;280(5366):1073-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, University of Rochester, Rochester, NY 14642, USA. lfrenkel@u.washington.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9582120" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Viral/analysis/genetics ; Diagnostic Errors ; Equipment Contamination ; Female ; Genes, env ; HIV Infections/immunology/transmission/*virology ; HIV-1/*genetics/*isolation & purification ; Humans ; Infant ; Infant, Newborn ; Infectious Disease Transmission, Vertical ; Molecular Sequence Data ; Phylogeny ; Polymerase Chain Reaction ; RNA, Viral/analysis ; *Specimen Handling ; T-Lymphocytes, Cytotoxic/immunology ; Viremia/virology
    Print ISSN: 0036-8075
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  • 7
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    Molecular basis of T cell inactivation by CTLA-4 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-18
    Description: CTLA-4, a negative regulator of T cell function, was found to associate with the T cell receptor (TCR) complex zeta chain in primary T cells. The association of TCRzeta with CTLA-4, reconstituted in 293 transfectants, was enhanced by p56(lck)-induced tyrosine phosphorylation. Coexpression of the CTLA-4-associated tyrosine phosphatase, SHP-2, resulted in dephosphorylation of TCRzeta bound to CTLA-4 and abolished the p56(lck)-inducible TCRzeta-CTLA-4 interaction. Thus, CTLA-4 inhibits TCR signal transduction by binding to TCRzeta and inhibiting tyrosine phosphorylation after T cell activation. These findings have broad implications for the negative regulation of T cell function and T cell tolerance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, K M -- Chuang, E -- Griffin, M -- Khattri, R -- Hong, D K -- Zhang, W -- Straus, D -- Samelson, L E -- Thompson, C B -- Bluestone, J A -- P01 AI35294-6/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1998 Dec 18;282(5397):2263-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ben May Institute for Cancer Research, and Committee on Immunology, University of Chicago, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9856951" target="_blank"〉PubMed〈/a〉
    Keywords: Abatacept ; Animals ; Antigens, CD ; Antigens, Differentiation/*metabolism ; CTLA-4 Antigen ; Cell Line ; Cells, Cultured ; Humans ; *Immunoconjugates ; Intracellular Signaling Peptides and Proteins ; *Lymphocyte Activation ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/genetics/metabolism ; Membrane Proteins/*metabolism ; Mice ; Mice, Inbred BALB C ; Models, Immunological ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/genetics/metabolism ; Receptors, Antigen, T-Cell/*metabolism ; Recombinant Fusion Proteins/metabolism ; SH2 Domain-Containing Protein Tyrosine Phosphatases ; *Signal Transduction ; T-Lymphocytes/*immunology ; Transfection ; src Homology Domains
    Print ISSN: 0036-8075
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  • 8
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    An essential role for ectodomain shedding in mammalian development (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-11-13
    Description: The ectodomains of numerous proteins are released from cells by proteolysis to yield soluble intercellular regulators. The responsible protease, tumor necrosis factor-alpha converting enzyme (TACE), has been identified only in the case when tumor necrosis factor-alpha (TNFalpha) is released. Analyses of cells lacking this metalloproteinase-disintegrin revealed an expanded role for TACE in the processing of other cell surface proteins, including a TNF receptor, the L-selectin adhesion molecule, and transforming growth factor-alpha (TGFalpha). The phenotype of mice lacking TACE suggests an essential role for soluble TGFalpha in normal development and emphasizes the importance of protein ectodomain shedding in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peschon, J J -- Slack, J L -- Reddy, P -- Stocking, K L -- Sunnarborg, S W -- Lee, D C -- Russell, W E -- Castner, B J -- Johnson, R S -- Fitzner, J N -- Boyce, R W -- Nelson, N -- Kozlosky, C J -- Wolfson, M F -- Rauch, C T -- Cerretti, D P -- Paxton, R J -- March, C J -- Black, R A -- CA43793/CA/NCI NIH HHS/ -- DK53804/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1998 Nov 13;282(5392):1281-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101, USA. peschon@immunex.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9812885" target="_blank"〉PubMed〈/a〉
    Keywords: ADAM Proteins ; Amino Acid Sequence ; Animals ; Catalytic Domain ; Cell Membrane/*metabolism ; Cells, Cultured ; Crosses, Genetic ; *Embryonic and Fetal Development ; L-Selectin/metabolism ; Ligands ; Membrane Proteins/*metabolism ; Metalloendopeptidases/chemistry/genetics/*metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Mutation ; Phenotype ; Protein Processing, Post-Translational ; Receptors, Tumor Necrosis Factor/metabolism ; Transforming Growth Factor alpha/metabolism ; Tumor Necrosis Factor-alpha/*metabolism
    Print ISSN: 0036-8075
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  • 9
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    Activation of the ATM kinase by ionizing radiation and phosphorylation of p53 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-11
    Description: The p53 tumor suppressor protein is activated and phosphorylated on serine-15 in response to various DNA damaging agents. The gene product mutated in ataxia telangiectasia, ATM, acts upstream of p53 in a signal transduction pathway initiated by ionizing radiation. Immunoprecipitated ATM had intrinsic protein kinase activity and phosphorylated p53 on serine-15 in a manganese-dependent manner. Ionizing radiation, but not ultraviolet radiation, rapidly enhanced this p53-directed kinase activity of endogenous ATM. These observations, along with the fact that phosphorylation of p53 on serine-15 in response to ionizing radiation is reduced in ataxia telangiectasia cells, suggest that ATM is a protein kinase that phosphorylates p53 in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Canman, C E -- Lim, D S -- Cimprich, K A -- Taya, Y -- Tamai, K -- Sakaguchi, K -- Appella, E -- Kastan, M B -- Siliciano, J D -- CA71387/CA/NCI NIH HHS/ -- ES05777/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1677-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Johns Hopkins School of Medicine, Oncology Center, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9733515" target="_blank"〉PubMed〈/a〉
    Keywords: Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins ; Cell Line ; DNA Damage ; DNA-Activated Protein Kinase ; *DNA-Binding Proteins ; Enzyme Activation ; Humans ; Lymphocytes/metabolism/radiation effects ; Mutation ; Nuclear Proteins ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Proteins/genetics/*metabolism ; *Radiation, Ionizing ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Signal Transduction ; Transfection ; Tumor Suppressor Protein p53/*metabolism ; Tumor Suppressor Proteins ; Ultraviolet Rays
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  • 10
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    Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-25
    Description: Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCzeta and PKCdelta in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)-dependent manner in vivo in human embryonic kidney (293) cells. All members of the PKC family tested formed complexes with PDK1. PDK1-dependent phosphorylation of PKCdelta in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCdelta in response to serum stimulation of cells was PI 3-kinase-dependent and was enhanced by PDK1 coexpression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Le Good, J A -- Ziegler, W H -- Parekh, D B -- Alessi, D R -- Cohen, P -- Parker, P J -- New York, N.Y. -- Science. 1998 Sep 25;281(5385):2042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9748166" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Binding Sites ; Cell Line ; Chromones/pharmacology ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; Isoenzymes/*metabolism ; Morpholines/pharmacology ; Phosphatidylcholines/pharmacology ; Phosphatidylinositol 3-Kinases/*metabolism ; Phosphatidylinositol Phosphates ; Phosphatidylserines/pharmacology ; Phosphorylation ; Protein Kinase C/*metabolism ; Protein Kinase C beta ; Protein-Serine-Threonine Kinases/*metabolism ; Recombinant Proteins/metabolism ; Tetradecanoylphorbol Acetate/pharmacology
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