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  • Science. 200(4347): 1281-3.  (1)
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  • Books
  • Articles  (120)
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  • 1995-1999  (115)
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Year
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  • 101
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    Phosphorylation of Sic1p by G1 Cdk required for its degradation and entry into S phase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-10-23
    Description: G1 cyclin-dependent kinase (Cdk)-triggered degradation of the S-phase Cdk inhibitor Sic1p has been implicated in the transition from G1 to S phase in the cell cycle of budding yeast. A multidimensional electrospray mass spectrometry technique was used to map G1 Cdk phosphorylation sites in Sic1p both in vitro and in vivo. A Sic1p mutant lacking three Cdk phosphorylation sites did not serve as a substrate for Cdc34p-dependent ubiquitination in vitro, was stable in vivo, and blocked DNA replication. Moreover, purified phosphoSic1p was ubiquitinated in cyclin-depleted G1 extract, indicating that a primary function of G1 cyclins is to tag Sic1p for destruction. These data suggest a molecular model of how phosphorylation and proteolysis cooperate to bring about the G1/S transition in budding yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verma, R -- Annan, R S -- Huddleston, M J -- Carr, S A -- Reynard, G -- Deshaies, R J -- R01 GM52466-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Oct 17;278(5337):455-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, Box 156-29, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9334303" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase-Promoting Complex-Cyclosome ; Cyclin G ; Cyclin-Dependent Kinase Inhibitor Proteins ; Cyclin-Dependent Kinases/*metabolism ; Cyclins/*metabolism ; DNA Replication ; Enzyme Inhibitors/metabolism ; Fungal Proteins/*metabolism ; G1 Phase ; Ligases/metabolism ; Molecular Sequence Data ; Mutagenesis ; Phenotype ; Phosphopeptides/metabolism ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; *S Phase ; *Saccharomyces cerevisiae Proteins ; *Ubiquitin-Protein Ligase Complexes ; Ubiquitin-Protein Ligases ; Ubiquitins/metabolism ; Yeasts/*cytology/metabolism
    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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  • 102
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    A DNA damage checkpoint meets the cell cycle engine (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weinert, T -- New York, N.Y. -- Science. 1997 Sep 5;277(5331):1450-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, University of Arizona, Tuscon, AZ 85721, USA. tedvweinert@tikal.biosci.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9304216" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; Animals ; CDC2 Protein Kinase/*metabolism ; Cell Cycle Proteins/metabolism ; *DNA Damage ; Fungal Proteins/metabolism ; *G2 Phase ; Humans ; Mice ; Models, Biological ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Proteins/metabolism ; S Phase ; Schizosaccharomyces/cytology/metabolism ; *Tyrosine 3-Monooxygenase ; cdc25 Phosphatases ; *ras-GRF1
    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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  • 103
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    A cytoplasmic inhibitor of the JNK signal transduction pathway (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    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
    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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  • 104
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    Structure and function of a squalene cyclase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-09-20
    Description: The crystal structure of squalene-hopene cyclase from Alicyclobacillus acidocaldarius was determined at 2.9 angstrom resolution. The mechanism and sequence of this cyclase are closely related to those of 2,3-oxidosqualene cyclases that catalyze the cyclization step in cholesterol biosynthesis. The structure reveals a membrane protein with membrane-binding characteristics similar to those of prostaglandin-H2 synthase, the only other reported protein of this type. The active site of the enzyme is located in a large central cavity that is of suitable size to bind squalene in its required conformation and that is lined by aromatic residues. The structure supports a mechanism in which the acid starting the reaction by protonating a carbon-carbon double bond is an aspartate that is coupled to a histidine. Numerous surface alpha helices are connected by characteristic QW-motifs (Q is glutamine and W is tryptophan) that tighten the protein structure, possibly for absorbing the reaction energy without structural damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wendt, K U -- Poralla, K -- Schulz, G E -- New York, N.Y. -- Science. 1997 Sep 19;277(5333):1811-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Organische Chemie und Biochemie, Albertstrasse 21, D-79104 Freiburg im Breisgau, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9295270" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacillaceae/*enzymology ; Binding Sites ; Cell Membrane/enzymology ; Crystallization ; Crystallography, X-Ray ; Cyclization ; Dimerization ; Humans ; Hydrogen Bonding ; *Intramolecular Transferases ; Isomerases/*chemistry/metabolism ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Recombinant Proteins/chemistry/metabolism ; Sequence Alignment ; Squalene/metabolism ; Thermodynamics
    Print ISSN: 0036-8075
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  • 105
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    A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-14
    Description: Cleland and Kreevoy recently advanced the idea that a special type of hydrogen bond (H-bond), termed a low-barrier hydrogen bond (LBHB), may account for the "missing" transition state stabilization underlying the catalytic power of many enzymes, and Frey et al. have proposed that the H-bond between aspartic acid 102 and histidine 57 in the catalytic triad of serine proteases is an example of a catalytically important LBHB. Experimental facts are here considered regarding the aspartic acid-histidine and cis-urocanic H-bonds that are inconsistent with fundamental tenets of the LBHB hypothesis. The inconsistencies between theory and experiment in these paradigm systems cast doubt on the existence of LBHBs, as currently defined, within enzyme active sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ash, E L -- Sudmeier, J L -- De Fabo, E C -- Bachovchin, W W -- GM27927/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 7;278(5340):1128-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Tufts University School of Medicine, Boston, MA 02111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9353195" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/chemistry ; Binding Sites ; Boronic Acids/metabolism ; Catalysis ; Histidine/chemistry ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Magnetic Resonance Spectroscopy ; Oligopeptides/metabolism ; Protons ; Serine Endopeptidases/*chemistry/metabolism ; Serine Proteinase Inhibitors/metabolism ; Subtilisins/chemistry ; Temperature ; Urocanic Acid/chemistry
    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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  • 106
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    IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-05
    Description: Activation of the transcription factor nuclear factor kappa B (NF-kappaB) is controlled by sequential phosphorylation, ubiquitination, and degradation of its inhibitory subunit IkappaB. A large multiprotein complex, the IkappaB kinase (IKK) signalsome, was purified from HeLa cells and found to contain a cytokine-inducible IkappaB kinase activity that phosphorylates IkappaB-alpha and IkappaB-beta. Two components of the IKK signalsome, IKK-1 and IKK-2, were identified as closely related protein serine kinases containing leucine zipper and helix-loop-helix protein interaction motifs. Mutant versions of IKK-2 had pronounced effects on RelA nuclear translocation and NF-kappaB-dependent reporter activity, consistent with a critical role for the IKK kinases in the NF-kappaB signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mercurio, F -- Zhu, H -- Murray, B W -- Shevchenko, A -- Bennett, B L -- Li, J -- Young, D B -- Barbosa, M -- Mann, M -- Manning, A -- Rao, A -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):860-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Signal Pharmaceuticals, Inc., 5555 Oberlin Drive, San Diego, CA 92121, USA. fmercuri@signalpharm.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9346484" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Cycle Proteins ; Cloning, Molecular ; Dual Specificity Phosphatase 1 ; Enzyme Activation ; HeLa Cells ; Helix-Loop-Helix Motifs ; Humans ; I-kappa B Kinase ; Immediate-Early Proteins/metabolism ; Leucine Zippers ; Molecular Sequence Data ; NF-kappa B/*metabolism ; *Phosphoprotein Phosphatases ; Phosphorylation ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Sequence Homology, Amino Acid ; Substrate Specificity
    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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  • 107
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    IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-05
    Description: Activation of the transcription factor nuclear factor kappa B (NF-kappaB) by inflammatory cytokines requires the successive action of NF-kappaB-inducing kinase (NIK) and IkappaB kinase-alpha (IKK-alpha). A widely expressed protein kinase was identified that is 52 percent identical to IKK-alpha. IkappaB kinase-beta (IKK-beta) activated NF-kappaB when overexpressed and phosphorylated serine residues 32 and 36 of IkappaB-alpha and serines 19 and 23 of IkappaB-beta. The activity of IKK-beta was stimulated by tumor necrosis factor and interleukin-1 treatment. IKK-alpha and IKK-beta formed heterodimers that interacted with NIK. Overexpression of a catalytically inactive form of IKK-beta blocked cytokine-induced NF-kappaB activation. Thus, an active IkappaB kinase complex may require three distinct protein kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Woronicz, J D -- Gao, X -- Cao, Z -- Rothe, M -- Goeddel, D V -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):866-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Tularik, Two Corporate Drive, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9346485" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cell Line ; Cytokines/metabolism ; Enzyme Activation ; Genes, Reporter ; HeLa Cells ; Humans ; I-kappa B Kinase ; Molecular Sequence Data ; NF-kappa B/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Sequence Homology, Amino Acid ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 108
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    Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-09
    Description: A new class of protein tyrosine kinase inhibitors was identified that is based on an oxindole core (indolinones). Two compounds from this class inhibited the kinase activity of fibroblast growth factor receptor 1 (FGFR1) and showed differential specificity toward other receptor tyrosine kinases. Crystal structures of the tyrosine kinase domain of FGFR1 in complex with the two compounds were determined. The oxindole occupies the site in which the adenine of adenosine triphosphate binds, whereas the moieties that extend from the oxindole contact residues in the hinge region between the two kinase lobes. The more specific inhibitor of FGFR1 induces a conformational change in the nucleotide-binding loop. This structural information will facilitate the design of new inhibitors for use in the treatment of cancer and other diseases in which cell signaling by tyrosine kinases plays a crucial role in disease pathogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mohammadi, M -- McMahon, G -- Sun, L -- Tang, C -- Hirth, P -- Yeh, B K -- Hubbard, S R -- Schlessinger, J -- New York, N.Y. -- Science. 1997 May 9;276(5314):955-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, New York University Medical Center, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9139660" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; Enzyme Inhibitors/chemistry/*metabolism/pharmacology ; Hydrogen Bonding ; Mice ; Models, Molecular ; Phosphorylation ; Phosphotyrosine/metabolism ; Piperazines/chemistry/*metabolism/pharmacology ; Protein-Tyrosine Kinases/antagonists & inhibitors/*chemistry/metabolism ; Pyrroles/chemistry/*metabolism/pharmacology ; *Receptor Protein-Tyrosine Kinases ; Receptor, Epidermal Growth Factor/antagonists & inhibitors/metabolism ; Receptor, Fibroblast Growth Factor, Type 1 ; Receptor, Insulin/antagonists & inhibitors/metabolism ; Receptors, Fibroblast Growth Factor/antagonists & ; inhibitors/*chemistry/metabolism ; Receptors, Platelet-Derived Growth Factor/antagonists & inhibitors/metabolism
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  • 109
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    Paths to activation of transcription (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-03-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Geiduschek, E P -- New York, N.Y. -- Science. 1997 Mar 14;275(5306):1614-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Center for Molecular Genetics, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0634, USA. epg@jeeves.ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9072826" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; *Bacterial Proteins ; Coliphages/genetics ; DNA, Bacterial/metabolism ; DNA-Binding Proteins/metabolism ; DNA-Directed RNA Polymerases/chemistry/*metabolism ; Enhancer Elements, Genetic ; PII Nitrogen Regulatory Proteins ; Phosphorylation ; Promoter Regions, Genetic ; RNA Polymerase Sigma 54 ; Salmonella typhimurium/genetics ; Sigma Factor/metabolism ; *Trans-Activators ; Transcription Factors/*metabolism ; *Transcription, Genetic ; *Transcriptional Activation
    Print ISSN: 0036-8075
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  • 110
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    Repression of c-myc transcription by Blimp-1, an inducer of terminal B cell differentiation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-25
    Description: Transcription of c-myc in plasma cells, which are terminally differentiated B cells, is repressed by plasmacytoma repressor factor. This factor was identified as Blimp-1, known for its ability to induce B cell differentiation. Blimp-1 repressed c-myc promoter activity in a binding site-dependent manner. Treatment of BCL1 lymphoma cells with interleukin-2 (IL-2) plus IL-5 induced Blimp-1 and caused a subsequent decline in c-Myc protein. Ectopic expression of Blimp-1 in Abelson-transformed precursor B cells repressed endogenous c-Myc and caused apoptosis; Blimp-1-induced death was partially overcome by ectopic expression of c-Myc. Thus, repression of c-myc is a component of the Blimp-1 program of terminal B cell differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, Y -- Wong, K -- Calame, K -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):596-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9110979" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; B-Lymphocytes/*cytology/metabolism ; Binding Sites ; Cell Differentiation ; Cell Line ; Gene Expression Regulation ; *Genes, myc ; Interleukin-2/pharmacology ; Interleukin-5/pharmacology ; Mice ; Mutagenesis, Site-Directed ; Plasmacytoma ; Promoter Regions, Genetic ; *Repressor Proteins ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; Zinc Fingers
    Print ISSN: 0036-8075
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  • 111
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    How TRAIL kills cancer cells, but not normal cells (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-08-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gura, T -- New York, N.Y. -- Science. 1997 Aug 8;277(5327):768.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9273698" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Apoptosis Regulatory Proteins ; Binding Sites ; Databases, Factual ; GPI-Linked Proteins ; Humans ; Membrane Glycoproteins/*metabolism/therapeutic use ; Neoplasms/*metabolism/pathology ; Rats ; Receptors, TNF-Related Apoptosis-Inducing Ligand ; Receptors, Tumor Necrosis Factor/chemistry/*metabolism ; TNF-Related Apoptosis-Inducing Ligand ; Tumor Cells, Cultured ; Tumor Necrosis Factor Decoy Receptors ; Tumor Necrosis Factor-alpha/*metabolism/therapeutic use
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 112
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    STAT3 as an adapter to couple phosphatidylinositol 3-kinase to the IFNAR1 chain of the type I interferon receptor (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-30
    Description: STAT (signal transducers and activators of transcription) proteins undergo cytokine-dependent phosphorylation on serine and tyrosine. STAT3, a transcription factor for acute phase response genes, was found to act as an adapter molecule in signal transduction from the type I interferon receptor. STAT3 bound to a conserved sequence in the cytoplasmic tail of the IFNAR1 chain of the receptor and underwent interferon-dependent tyrosine phosphorylation. The p85 regulatory subunit of phosphatidylinositol 3-kinase, which activates a series of serine kinases, bound to phosphorylated STAT3 and subsequently underwent tyrosine phosphorylation. Thus, STAT3 acts as an adapter to couple another signaling pathway to the interferon receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfeffer, L M -- Mullersman, J E -- Pfeffer, S R -- Murti, A -- Shi, W -- Yang, C H -- New York, N.Y. -- Science. 1997 May 30;276(5317):1418-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Tennessee Health Science Center, Memphis, TN 38163, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9162009" target="_blank"〉PubMed〈/a〉
    Keywords: Acute-Phase Proteins/*genetics ; Amino Acid Sequence ; Androstadienes/pharmacology ; Animals ; Binding Sites ; COS Cells ; Cell Line ; Cloning, Molecular ; Conserved Sequence ; DNA-Binding Proteins/genetics/*metabolism ; Enzyme Inhibitors/pharmacology ; Membrane Proteins ; Molecular Sequence Data ; Phosphatidylinositol 3-Kinases ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/antagonists & ; inhibitors/genetics/*metabolism ; Point Mutation ; Protein Binding ; Receptor, Interferon alpha-beta ; Receptors, Interferon/*metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; STAT3 Transcription Factor ; Signal Transduction ; Trans-Activators/genetics/*metabolism ; Tyrosine/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 113
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    Joining the two domains of a group I ribozyme to form the catalytic core (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-07
    Description: Self-splicing group I introns, like other large catalytic RNAs, contain structural domains. Although the crystal structure of one of these domains has been determined by x-ray analysis, its connection to the other major domain that contains the guanosine-binding site has not been known. Site-directed mutagenesis and kinetic analysis of RNA splicing were used to identify a base triple in the conserved core of both a cyanobacterial (Anabaena) and a eukaryotic (Tetrahymena) group I intron. This long-range interaction connects a sequence adjacent to the guanosine-binding site with the domain implicated in coordinating the 5' splice site helix, and it thereby contributes to formation of the active site. The resulting five-strand junction, in which a short helix forms base triples with three separate strands in the Tetrahymena intron, reveals exceptionally dense packing of RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanner, M A -- Cech, T R -- GM28039/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Feb 7;275(5301):847-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado, Boulder, Colorado 80309-0215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9012355" target="_blank"〉PubMed〈/a〉
    Keywords: Anabaena/genetics ; Animals ; Base Composition ; Binding Sites ; Guanosine/metabolism ; *Introns ; Mutagenesis, Site-Directed ; *Nucleic Acid Conformation ; RNA Splicing ; RNA, Bacterial/genetics ; RNA, Catalytic/*chemistry/genetics/metabolism ; RNA, Protozoan/genetics ; Tetrahymena/genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 114
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    Learning mechanisms: the case for CaM-KII (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-06-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lisman, J -- Malenka, R C -- Nicoll, R A -- Malinow, R -- New York, N.Y. -- Science. 1997 Jun 27;276(5321):2001-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Brandeis University, Waltham, MA 02254, USA. lisman@binah.cc.brandeis.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9221509" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Hippocampus/metabolism ; *Long-Term Potentiation ; Memory ; Mice ; Mice, Transgenic ; Phosphorylation ; Receptors, AMPA/*metabolism ; Signal Transduction ; Synapses/*metabolism ; *Synaptic Transmission ; Vision, Ocular
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 115
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    Reverse transcriptase motifs in the catalytic subunit of telomerase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-25
    Description: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Telomerase RNA components have been identified from many organisms, but no protein component has been demonstrated to catalyze telomeric DNA extension. Telomerase was purified from Euplotes aediculatus, a ciliated protozoan, and one of its proteins was partially sequenced by nanoelectrospray tandem mass spectrometry. Cloning and sequence analysis of the corresponding gene revealed that this 123-kilodalton protein (p123) contains reverse transcriptase motifs. A yeast (Saccharomyces cerevisiae) homolog was found and subsequently identified as EST2 (ever shorter telomeres), deletion of which had independently been shown to produce telomere defects. Introduction of single amino acid substitutions within the reverse transcriptase motifs of Est2 protein led to telomere shortening and senescence in yeast, indicating that these motifs are important for catalysis of telomere elongation in vivo. In vitro telomeric DNA extension occurred with extracts from wild-type yeast but not from est2 mutants or mutants deficient in telomerase RNA. Thus, the reverse transcriptase protein fold, previously known to be involved in retroviral replication and retrotransposition, is essential for normal chromosome telomere replication in diverse eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lingner, J -- Hughes, T R -- Shevchenko, A -- Mann, M -- Lundblad, V -- Cech, T R -- AG11728/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1997 Apr 25;276(5312):561-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309-0215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9110970" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Catalysis ; Chromosomes/metabolism ; DNA, Fungal/metabolism ; DNA-Binding Proteins ; Euplotes/*enzymology ; Evolution, Molecular ; Fungal Proteins/chemistry/metabolism ; Genes, Fungal ; Genes, Protozoan ; Molecular Sequence Data ; Protein Conformation ; *Rna ; RNA, Fungal/metabolism ; RNA, Protozoan/metabolism ; RNA-Directed DNA Polymerase/*chemistry/metabolism ; Saccharomyces cerevisiae/enzymology ; Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Telomerase/*chemistry/genetics/isolation & purification/metabolism ; Telomere/metabolism ; Templates, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 116
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    The biology of oxygen radicals (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-09-08
    Description: The reactive superoxide radical, O2-, formerly of concern only to radiation chemists and radiobiologists, is now understood to be a normal product of the biological reduction of molecular oxygen. An unusual family of enzymes, the superoxide dismutases, protect against the deleterious actions of this radical by catalyzing its dismutation to hydrogen peroxide plus oxygen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fridovich, I -- New York, N.Y. -- Science. 1978 Sep 8;201(4359):875-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/210504" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Catalase/metabolism ; Free Radicals ; Inflammation/metabolism ; Kinetics ; Metals ; Oxidation-Reduction ; Oxygen/*metabolism ; Paraquat/pharmacology ; Peroxidases/metabolism ; Superoxide Dismutase/*metabolism ; Superoxides/*metabolism/toxicity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 117
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    Thrombin-induced platelet aggregation is mediated by a platelet plasma membrane-bound lectin (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-06-16
    Description: Throbin-activated human platelets cause agglutination of trypsinized, formalinized bovine erythrocytes. This lectin activity of stimulated platelets was blocked by galactosamine, glucosamine, mannosamine, lysine, and arginine, but not by N-acetylated sugars, other neutral sugars, or other amino acids. Inhibitors of the thrombin-induced lectin activity also blocked thrombin-induced platelet aggregation. It appears that a membrane surface component that has lectin activity mediates platelet aggregation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gartner, T K -- Williams, D C -- Minion, F C -- Phillips, D R -- New York, N.Y. -- Science. 1978 Jun 16;200(4347):1281-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/663608" target="_blank"〉PubMed〈/a〉
    Keywords: *Agglutinins ; Amino Acids/pharmacology ; Amino Sugars/pharmacology ; Animals ; Binding Sites ; Cytochalasin B/pharmacology ; *Hemagglutinins ; Humans ; Membrane Proteins/blood ; Platelet Aggregation/*drug effects ; Prostaglandins E/pharmacology ; Species Specificity ; Thrombin/*pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 118
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    Rapid changes in brain benzodiazepine receptors after experimental seizures (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-24
    Description: Seizures induced in the rat by electroshock or by injections of pentylenetetrazol increase the specific binding of diazepam to putative receptor sites in cerebral cortical membranes. The enhancement of diazepam binding results from a rapid increase in the number of available binding sites rather than a change in receptor affinity. The postictal increase in cortical benzodiazepine receptors suggests that the cerebral cortex might be more sensitive to the anticonvulsant effects of the benzodiazepines after seizures. This observation may be related to the mechanism of action of these drugs in the treatment of recurrent seizures such as status epilepticus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paul, S M -- Skolnick, P -- New York, N.Y. -- Science. 1978 Nov 24;202(4370):892-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/715447" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anoxia/metabolism ; Binding Sites ; Brain/*metabolism ; Cerebral Cortex/metabolism ; Diazepam/*metabolism ; Electroshock ; Kinetics ; Male ; Pentylenetetrazole ; Rats ; Receptors, Drug/*metabolism ; Seizures/*metabolism ; Synaptosomes/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 119
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    Prolactin binding sites in the rat brain (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-09-15
    Description: The principles of the competitive-binding assay were used in conjunction with light microscopic radioautography to demonstrate specific prolactin binding sites localized on ependyma of the rat choroid plexus, a previously unknown prolactin target tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walsh, R J -- Posner, B I -- Kopriwa, B M -- Brawer, J R -- New York, N.Y. -- Science. 1978 Sep 15;201(4360):1041-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/684427" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoradiography ; Binding Sites ; Binding, Competitive ; Brain/cytology/*metabolism ; Female ; Iodine Radioisotopes ; Male ; Prolactin/*metabolism ; Rats
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 120
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    Antibodies to purified insulin receptor have insulin-like activity (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-06-16
    Description: Antibodies to insulin receptors purified from rat liver membranes do not complete with [125I]insulin for binding to the insulin receptor but do precipitate solubilized receptors labeled with [125I]insulin. These antibodies have the insulin-like activities of enhancing glucose oxidation and inhibiting epinephrine-induced lipolysis in rat adipocytes. Thus, antibody binds to the receptor at a different site from that to which insulin binds, yet the interaction can initiate an effective biological response. These results indicate that the previously studied insulin-binding sites are the physiological macromolecular receptors for insulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobs, S -- Chang, K J -- Cuatrecasas, P -- New York, N.Y. -- Science. 1978 Jun 16;200(4347):1283-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/663609" target="_blank"〉PubMed〈/a〉
    Keywords: Acanthosis Nigricans/physiopathology ; Adipose Tissue/metabolism ; Animals ; *Antibodies ; Antigen-Antibody Reactions ; Binding Sites ; Binding, Competitive ; Biological Transport ; Epinephrine/pharmacology ; Glucose/metabolism ; Insulin/metabolism ; Lipid Mobilization ; Liver/immunology ; Rats ; Receptor, Insulin/*physiology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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