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  • 1995-1999  (197)
  • 1945-1949  (23)
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  • 1
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    Major improvements in progress for southern California earthquake monitoring (1998)
    In:  Eos, Trans., Am. Geophys. Un., Edmonton, Conseil de l'Europe, vol. 79, no. 18, pp. 217, 221, pp. B05402, (ISSN: 1340-4202)
    Details
    Publication Date: 1998
    Keywords: Seismic networks ; Instruments ; SCEC ; Real time earthquake monitoring ; Seismicity
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    BIBLIOGRAPHY SEISMOLOGY
  • 2
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    Global Positioning System applications for geodynamics and earthquake studies (1997)
    In:  Ann. Rev. Earth Planet. Sci., Luxembourg, Conseil de l'Europe, vol. 25, no. 14, pp. 301-336, pp. 1006, (ISSN: 1340-4202)
    Details
    Publication Date: 1997
    Keywords: Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Review article ; Earthquake precursor: deformation or strain ; GeodesyY ; Geodesy ; ANREV
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    BIBLIOGRAPHY SEISMOLOGY
  • 3
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    Electrical conductivity in the precambrian lithosphere of western canada (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-01-29
    Description: The subcrustal lithosphere underlying the southern Archean Churchill Province (ACP) in western Canada is at least one order of magnitude more electrically conductive than the lithosphere beneath adjacent Paleoproterozoic crust. The measured electrical properties of the lithosphere underlying most of the Paleoproterozoic crust can be explained by the conductivity of olivine. Mantle xenolith and geological mapping evidence indicate that the lithosphere beneath the southern ACP was substantially modified as a result of being trapped between two nearly synchronous Paleoproterozoic subduction zones. Tectonically induced metasomatism thus may have enhanced the subcrustal lithosphere conductivity of the southern ACP.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boerner -- Kurtz -- Craven -- Ross -- Jones -- Davis -- New York, N.Y. -- Science. 1999 Jan 29;283(5402):668-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉D. E. Boerner and J. A. Craven, Geological Survey of Canada, 615 Booth Street, Ottawa, Ontario K1A OE9, Canada. R. D. Kurtz and W. J. Davis, Geological Survey of Canada, 601 Booth Street, Ottawa, Ontario K1A OE8, Canada. G. M. Ross, Geologica.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9924022" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Postnatal sex reversal of the ovaries in mice lacking estrogen receptors alpha and beta (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-22
    Description: Mice lacking estrogen receptors alpha and beta were generated to clarify the roles of each receptor in the physiology of estrogen target tissues. Both sexes of alphabeta estrogen receptor knockout (alphabetaERKO) mutants exhibit normal reproductive tract development but are infertile. Ovaries of adult alphabetaERKO females exhibit follicle transdifferentiation to structures resembling seminiferous tubules of the testis, including Sertoli-like cells and expression of Mullerian inhibiting substance, sulfated glycoprotein-2, and Sox9. Therefore, loss of both receptors leads to an ovarian phenotype that is distinct from that of the individual ERKO mutants, which indicates that both receptors are required for the maintenance of germ and somatic cells in the postnatal ovary.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couse, J F -- Hewitt, S C -- Bunch, D O -- Sar, M -- Walker, V R -- Davis, B J -- Korach, K S -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2328-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Receptor Biology Section, Laboratory of Reproductive and Developmental Toxicology, Laboratory of Experimental Pathology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10600740" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Mullerian Hormone ; Cell Differentiation ; Clusterin ; *Disorders of Sex Development ; Estradiol/physiology ; Estrogen Receptor alpha ; Estrogen Receptor beta ; Female ; Gene Targeting ; Glycoproteins/analysis ; Growth Inhibitors/analysis ; High Mobility Group Proteins/analysis ; Luteinizing Hormone/blood ; Male ; Mice ; Mice, Knockout ; *Molecular Chaperones ; Ovary/*anatomy & histology/cytology/growth & development/*physiology ; Receptors, Estrogen/genetics/*physiology ; SOX9 Transcription Factor ; Seminiferous Tubules/anatomy & histology/cytology ; Sertoli Cells/cytology ; Signal Transduction ; Testicular Hormones/analysis ; Testis/anatomy & histology/cytology/growth & development/physiology ; Transcription Factors/analysis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Nuclear accumulation of NFAT4 opposed by the JNK signal transduction pathway (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-12-31
    Description: The nuclear factor of activated T cells (NFAT) group of transcription factors is retained in the cytoplasm of quiescent cells. NFAT activation is mediated in part by induced nuclear import. This process requires calcium-dependent dephosphorylation of NFAT caused by the phosphatase calcineurin. The c-Jun amino-terminal kinase (JNK) phosphorylates NFAT4 on two sites. Mutational removal of the JNK phosphorylation sites caused constitutive nuclear localization of NFAT4. In contrast, JNK activation in calcineurin-stimulated cells caused nuclear exclusion of NFAT4. These findings show that the nuclear accumulation of NFAT4 promoted by calcineurin is opposed by the JNK signal transduction pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chow, C W -- Rincon, M -- Cavanagh, J -- Dickens, M -- Davis, R J -- CA58396/CA/NCI NIH HHS/ -- CA65831/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 28;278(5343):1638-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9374467" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; COS Cells ; Calcineurin/metabolism ; Calcineurin Inhibitors ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Cell Line ; Cell Nucleus/*metabolism ; Cyclosporine/pharmacology ; Cytoplasm/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Humans ; JNK Mitogen-Activated Protein Kinases ; Jurkat Cells ; Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Mutation ; NFATC Transcription Factors ; *Nuclear Proteins ; Phosphorylation ; Protein Kinases/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; T-Lymphocytes/metabolism ; Transcription Factors/genetics/*metabolism ; Transcription, Genetic
    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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  • 6
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    Defective T cell differentiation in the absence of Jnk1 (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-12-16
    Description: The c-Jun NH2-terminal kinase (JNK) signaling pathway has been implicated in the immune response that is mediated by the activation and differentiation of CD4 helper T (TH) cells into TH1 and TH2 effector cells. JNK activity observed in wild-type activated TH cells was severely reduced in TH cells from Jnk1-/- mice. The Jnk1-/- T cells hyperproliferated, exhibited decreased activation-induced cell death, and preferentially differentiated to TH2 cells. The enhanced production of TH2 cytokines by Jnk1-/- cells was associated with increased nuclear accumulation of the transcription factor NFATc. Thus, the JNK1 signaling pathway plays a key role in T cell receptor-initiated TH cell proliferation, apoptosis, and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dong, C -- Yang, D D -- Wysk, M -- Whitmarsh, A J -- Davis, R J -- Flavell, R A -- CA65861/CA/NCI NIH HHS/ -- CA72009/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1998 Dec 11;282(5396):2092-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9851932" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/*metabolism ; Cell Differentiation ; Cell Division ; DNA-Binding Proteins/metabolism ; Female ; Gene Targeting ; Hemocyanin/immunology ; Interferon-gamma/biosynthesis ; Interleukins/biosynthesis ; JNK Mitogen-Activated Protein Kinases ; *Lymphocyte Activation ; Male ; Mice ; Mice, Knockout ; *Mitogen-Activated Protein Kinases ; NFATC Transcription Factors ; *Nuclear Proteins ; Signal Transduction ; T-Lymphocytes, Helper-Inducer/cytology/*immunology/metabolism ; Th1 Cells/cytology/immunology ; Th2 Cells/cytology/immunology ; Transcription Factors/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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  • 7
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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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  • 8
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    A mammalian scaffold complex that selectively mediates MAP kinase activation (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-09-11
    Description: The c-Jun NH2-terminal kinase (JNK) group of mitogen-activated protein (MAP) kinases is activated by the exposure of cells to multiple forms of stress. A putative scaffold protein was identified that interacts with multiple components of the JNK signaling pathway, including the mixed-lineage group of MAP kinase kinase kinases (MLK), the MAP kinase kinase MKK7, and the MAP kinase JNK. This scaffold protein selectively enhanced JNK activation by the MLK signaling pathway. These data establish that a mammalian scaffold protein can mediate activation of a MAP kinase signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitmarsh, A J -- Cavanagh, J -- Tournier, C -- Yasuda, J -- Davis, R J -- New York, N.Y. -- Science. 1998 Sep 11;281(5383):1671-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School and Howard Hughes Medical Institute, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9733513" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COS Cells ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Carrier Proteins/*metabolism ; Cell Line ; Cercopithecus aethiops ; Enzyme Activation ; Interleukin-1/metabolism ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase 7 ; *MAP Kinase Kinase Kinases ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Molecular Sequence Data ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction
    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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  • 9
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    Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-11-24
    Description: Apoptosis plays an important role during neuronal development, and defects in apoptosis may underlie various neurodegenerative disorders. To characterize molecular mechanisms that regulate neuronal apoptosis, the contributions to cell death of mitogen-activated protein (MAP) kinase family members, including ERK (extracellular signal-regulated kinase), JNK (c-JUN NH2-terminal protein kinase), and p38, were examined after withdrawal of nerve growth factor (NGF) from rat PC-12 pheochromocytoma cells. NGF withdrawal led to sustained activation of the JNK and p38 enzymes and inhibition of ERKs. The effects of dominant-interfering or constitutively activated forms of various components of the JNK-p38 and ERK signaling pathways demonstrated that activation of JNK and p38 and concurrent inhibition of ERK are critical for induction of apoptosis in these cells. Therefore, the dynamic balance between growth factor-activated ERK and stress-activated JNK-p38 pathways may be important in determining whether a cell survives or undergoes apoptosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xia, Z -- Dickens, M -- Raingeaud, J -- Davis, R J -- Greenberg, M E -- CA43855/CA/NCI NIH HHS/ -- CA65861/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1995 Nov 24;270(5240):1326-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7481820" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaloids/pharmacology ; Animals ; *Apoptosis ; Calcium-Calmodulin-Dependent Protein Kinases/*antagonists & ; inhibitors/genetics/*metabolism ; Cell Differentiation ; Enzyme Activation ; Genes, jun ; *JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase 1 ; MAP Kinase Kinase 3 ; MAP Kinase Kinase 4 ; MAP Kinase Kinase Kinases ; Mitogen-Activated Protein Kinase 1 ; Mitogen-Activated Protein Kinase 3 ; *Mitogen-Activated Protein Kinase Kinases ; *Mitogen-Activated Protein Kinases ; Nerve Growth Factors/pharmacology ; Neurons/*cytology/enzymology ; PC12 Cells ; Protein Kinases/*metabolism ; Protein-Serine-Threonine Kinases/genetics/metabolism ; Protein-Tyrosine Kinases/*antagonists & inhibitors/genetics/metabolism ; Rats ; *Signal Transduction ; Staurosporine ; Sympathetic Nervous System/cytology ; p38 Mitogen-Activated Protein Kinases
    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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  • 10
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    Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-06-21
    Description: ZPR1 is a zinc finger protein that binds to the cytoplasmic tyrosine kinase domain of the epidermal growth factor receptor (EGFR). Deletion analysis demonstrated that this binding interaction is mediated by the zinc fingers of ZPR1 and subdomains X and XI of the EGFR tyrosine kinase. Treatment of mammalian cells with EGF caused decreased binding of ZPR1 to the EGFR and the accumulation of ZPR1 in the nucleus. The effect of EGF to regulate ZPR1 binding is dependent on tyrosine phosphorylation of the EGFR. ZPR1 therefore represents a prototype for a class of molecule that binds to the EGFR and is released from the receptor after activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galcheva-Gargova, Z -- Konstantinov, K N -- Wu, I H -- Klier, F G -- Barrett, T -- Davis, R J -- R01-CA58396/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1797-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650580" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/*metabolism/secretion ; Cell Line ; Cell Nucleus/metabolism ; Cloning, Molecular ; Cytoplasm/metabolism ; Epidermal Growth Factor/pharmacology ; Humans ; Immunoblotting ; Male ; Mice ; Molecular Sequence Data ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Structure, Secondary ; RNA, Messenger/genetics/metabolism ; Receptor, Epidermal Growth Factor/chemistry/*metabolism ; Testis/metabolism ; Type C Phospholipases/metabolism ; Vanadates/pharmacology ; *Zinc Fingers ; src Homology Domains
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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