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  • 1995-1999  (318)
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  • 1
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    Earthquake ground motion and structural response in alluvial valleys (1999)
    In:  J. Geotech. Eng., Warszawa, Elsevier, vol. 125, no. 7, pp. 413-423, pp. L21303, (ISBN: 0-12-018847-3)
    Details
    Publication Date: 1999
    Keywords: Modelling ; Synthetic seismograms ; Strong motions ; Site amplification
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    BIBLIOGRAPHY SEISMOLOGY
  • 2
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    The 1996 Ml = 7.0 Lijiang earthquake, Yunnan, China: An anticipated event (1999)
    In:  Journal of Geodynamics, Kunming, China, 3-4, vol. 27, no. 4-5, pp. 529-546, pp. B05301, (ISSN: 1340-4202)
    Details
    Publication Date: 1999
    Keywords: Earthquake ; Crustal deformation (cf. Earthquake precursor: deformation or strain) ; Earthquake hazard ; forecasting ; JGD
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    BIBLIOGRAPHY SEISMOLOGY
  • 3
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    The Gelation of CO(2): A Sustainable Route to the Creation of Microcellular Materials (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-24
    Description: Compounds with strong thermodynamic affinity for carbon dioxide (CO(2)) have been designed and synthesized that dissolve in CO(2), then associate to form gels. Upon removal of the CO(2), these gels produced free-standing foams with cells with an average diameter smaller than 1 micrometer and a bulk density reduction of 97 percent relative to the parent material.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shi -- Huang -- Kilic -- Xu -- Enick -- Beckman -- Carr -- Melendez -- Hamilton -- New York, N.Y. -- Science. 1999 Nov 19;286(5444):1540-1543.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical and Petroleum Engineering, University of Pittsburgh, Pittsburgh, PA 15261, USA. Department of Chemistry, Yale University, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10567255" 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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    Evolution of shape complementarity and catalytic efficiency from a primordial antibody template (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-12-22
    Description: The crystal structure of an efficient Diels-Alder antibody catalyst at 1.9 angstrom resolution reveals almost perfect shape complementarity with its transition state analog. Comparison with highly related progesterone and Diels-Alderase antibodies that arose from the same primordial germ line template shows the relatively subtle mutational steps that were able to evolve both structural complementarity and catalytic efficiency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, J -- Deng, Q -- Chen, J -- Houk, K N -- Bartek, J -- Hilvert, D -- Wilson, I A -- CA27489/CA/NCI NIH HHS/ -- GM38273/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 17;286(5448):2345-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, The 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/10600746" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Catalytic/*chemistry/genetics/*metabolism ; Binding Sites, Antibody ; Catalysis ; Chemistry, Physical ; Crystallography, X-Ray ; *Evolution, Molecular ; Haptens/chemistry/metabolism ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/chemistry/metabolism ; Ligands ; Models, Molecular ; Mutation ; Physicochemical Phenomena ; Progesterone/immunology ; Protein Conformation ; Solubility ; Temperature ; Templates, 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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  • 5
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    Differential stimulation of PKC phosphorylation of potassium channels by ZIP1 and ZIP2 (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-09-08
    Description: Targeting of protein modification enzymes is a key biochemical step to achieve specific and effective posttranslational modifications. Two alternatively spliced ZIP1 and ZIP2 proteins are described, which bind to both Kvbeta2 subunits of potassium channel and protein kinase C (PKC) zeta, thereby acting as a physical link in the assembly of PKCzeta-ZIP-potassium channel complexes. ZIP1 and ZIP2 differentially stimulate phosphorylation of Kvbeta2 by PKCzeta. They also interact to form heteromultimers, which allows for a hybrid stimulatory activity to PKCzeta. Finally, ZIP1 and ZIP2 coexist in the same cell type and are elevated differentially by neurotrophic factors. These results provide a mechanism for specificity and regulation of PKCzeta-targeted phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gong, J -- Xu, J -- Bezanilla, M -- van Huizen, R -- Derin, R -- Li, M -- NS33324/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1999 Sep 3;285(5433):1565-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, The Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10477520" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Binding Sites ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cerebellum/metabolism ; DNA, Complementary ; Isoenzymes/metabolism ; Molecular Sequence Data ; Myelin Basic Protein/metabolism ; Nerve Growth Factors/pharmacology ; Neurons/*metabolism ; Phosphorylation ; Potassium Channels/*metabolism ; Protein Kinase C/*metabolism ; Pyramidal Cells/metabolism ; RNA, Messenger/genetics/metabolism ; Rats ; Rats, Sprague-Dawley ; Recombinant Fusion Proteins/chemistry/metabolism ; Substrate Specificity ; 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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  • 6
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    Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-04-16
    Description: The in vivo biological function of a steroid receptor coactivator was assessed in mice in which the SRC-1 gene was inactivated by gene targeting. Although in both sexes the homozygous mutants were viable and fertile, target organs such as uterus, prostate, testis, and mammary gland exhibited decreased growth and development in response to steroid hormones. Expression of RNA encoding TIF2, a member of the SRC-1 family, was increased in the SRC-1 null mutant, perhaps compensating partially for the loss of SRC-1 function in target tissues. The results indicate that SRC-1 mediates steroid hormone responses in vivo and that loss of its coactivator function results in partial resistance to hormone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xu, J -- Qiu, Y -- DeMayo, F J -- Tsai, S Y -- Tsai, M J -- O'Malley, B W -- New York, N.Y. -- Science. 1998 Mar 20;279(5358):1922-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, 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/9506940" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Drug Resistance ; Estradiol/blood/pharmacology ; Female ; Gene Targeting ; Genitalia, Male/drug effects/*growth & development ; Gonadal Steroid Hormones/*pharmacology ; Histone Acetyltransferases ; Male ; Mammary Glands, Animal/drug effects/*growth & development ; Mice ; Nuclear Receptor Coactivator 1 ; Nuclear Receptor Coactivator 2 ; Organ Size/drug effects ; Pregnancy ; Progesterone/blood/pharmacology ; Prostate/drug effects/growth & development ; Stem Cells ; Testis/drug effects/growth & development ; Testosterone/blood/pharmacology ; Transcription Factors/genetics/*physiology ; Uterus/drug effects/*growth & development
    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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    Activation of PPARgamma coactivator-1 through transcription factor docking (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-11-13
    Description: Transcriptional coactivators have been viewed as constitutively active components, using transcription factors mainly to localize their functions. Here, it is shown that PPARgamma coactivator-1 (PGC-1) promotes transcription through the assembly of a complex that includes the histone acetyltransferases steroid receptor coactivator-1 (SRC-1) and CREB binding protein (CBP)/p300. PGC-1 has a low inherent transcriptional activity when it is not bound to a transcription factor. The docking of PGC-1 to peroxisome proliferator-activated receptor gamma (PPARgamma) stimulates an apparent conformational change in PGC-1 that permits binding of SRC-1 and CBP/p300, resulting in a large increase in transcriptional activity. Thus, transcription factor docking switches on the activity of a coactivator protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Puigserver, P -- Adelmant, G -- Wu, Z -- Fan, M -- Xu, J -- O'Malley, B -- Spiegelman, B M -- DK54477/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1999 Nov 12;286(5443):1368-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute and Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10558993" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; COS Cells ; DNA-Binding Proteins/metabolism ; E1A-Associated p300 Protein ; Gene Expression Regulation ; Histone Acetyltransferases ; Mice ; Nuclear Proteins/chemistry/*metabolism ; Nuclear Receptor Coactivator 1 ; Nuclear Respiratory Factors ; Protein Binding ; Protein Conformation ; Receptors, Cytoplasmic and Nuclear/*metabolism ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/chemistry/*metabolism ; Transcription Factors/chemistry/*metabolism ; *Transcription, Genetic ; 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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    Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-01-07
    Description: Pin1 is an essential and conserved mitotic peptidyl-prolyl isomerase (PPIase) that is distinct from members of two other families of conventional PPIases, cyclophilins and FKBPs (FK-506 binding proteins). In response to their phosphorylation during mitosis, Pin1 binds and regulates members of a highly conserved set of proteins that overlaps with antigens recognized by the mitosis-specific monoclonal antibody MPM-2. Pin1 is here shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-proline or phosphothreonine-proline bonds present in mitotic phosphoproteins. Both Pin1 and MPM-2 selected similar phosphorylated serine-proline-containing peptides, providing the basis for the specific interaction between Pin1 and MPM-2 antigens. Pin1 preferentially isomerized proline residues preceded by phosphorylated serine or threonine with up to 1300-fold selectivity compared with unphosphorylated peptides. Pin1 may thus regulate mitotic progression by catalyzing sequence-specific and phosphorylation-dependent proline isomerization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yaffe, M B -- Schutkowski, M -- Shen, M -- Zhou, X Z -- Stukenberg, P T -- Rahfeld, J U -- Xu, J -- Kuang, J -- Kirschner, M W -- Fischer, G -- Cantley, L C -- Lu, K P -- GM56203/GM/NIGMS NIH HHS/ -- GM56230/GM/NIGMS NIH HHS/ -- R01 GM056203/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Dec 12;278(5345):1957-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine Beth Israel Deaconess Medical Center, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9395400" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/metabolism ; Antibodies, Monoclonal ; Binding Sites ; Carrier Proteins/metabolism ; Cell Cycle Proteins/chemistry/*metabolism ; DNA-Binding Proteins/metabolism ; Epitopes ; HeLa Cells ; Heat-Shock Proteins/metabolism ; Humans ; Isomerism ; *Mitosis ; Models, Molecular ; Oligopeptides/chemistry/*metabolism ; Peptide Library ; Peptidylprolyl Isomerase/chemistry/*metabolism ; Phosphoproteins/chemistry/immunology/*metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Phosphothreonine/metabolism ; Proline/*metabolism ; Protein Conformation ; Recombinant Fusion Proteins/chemistry/metabolism ; Substrate Specificity ; Tacrolimus Binding Proteins
    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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    Recognition of unique carboxyl-terminal motifs by distinct PDZ domains (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-03
    Description: The oriented peptide library technique was used to investigate the peptide-binding specificities of nine PDZ domains. Each PDZ domain selected peptides with hydrophobic residues at the carboxyl terminus. Individual PDZ domains selected unique optimal motifs defined primarily by the carboxyl terminal three to seven residues of the peptides. One family of PDZ domains, including those of the Discs Large protein, selected peptides with the consensus motif Glu-(Ser/Thr)-Xxx-(Val/Ile) (where Xxx represents any amino acid) at the carboxyl terminus. In contrast, another family of PDZ domains, including those of LIN-2, p55, and Tiam-1, selected peptides with hydrophobic or aromatic side chains at the carboxyl terminal three residues. On the basis of crystal structures of the PSD-95-3 PDZ domain, the specificities observed with the peptide library can be rationalized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Songyang, Z -- Fanning, A S -- Fu, C -- Xu, J -- Marfatia, S M -- Chishti, A H -- Crompton, A -- Chan, A C -- Anderson, J M -- Cantley, L C -- CA66263/CA/NCI NIH HHS/ -- DK34989/DK/NIDDK NIH HHS/ -- R01 GM056203/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Jan 3;275(5296):73-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Beth Israel Hospital, and Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8974395" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Crystallography, X-Ray ; Guanine Nucleotide Exchange Factors ; Guanylate Kinase ; Helminth Proteins/chemistry/metabolism ; Humans ; Kinesin/chemistry/metabolism ; Membrane Proteins/chemistry/metabolism ; Models, Molecular ; Myosins/chemistry/metabolism ; Nerve Tissue Proteins/chemistry/metabolism ; Nucleoside-Phosphate Kinase/chemistry/metabolism ; Peptide Library ; Peptides/chemistry/*metabolism ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Tyrosine Phosphatases/chemistry/metabolism ; Proteins/chemistry/*metabolism ; Sequence Homology, Amino Acid
    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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    Major susceptibility locus for prostate cancer on chromosome 1 suggested by a genome-wide search (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-22
    Description: Despite its high prevalence, very little is known regarding genetic predisposition to prostate cancer. A genome-wide scan performed in 66 high-risk prostate cancer families has provided evidence of linkage to the long arm of chromosome 1 (1q24-25). Analysis of an additional set of 25 North American and Swedish families with markers in this region resulted in significant evidence of linkage in the combined set of 91 families. The data provide strong evidence of a major prostate cancer susceptibility locus on chromosome 1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, J R -- Freije, D -- Carpten, J D -- Gronberg, H -- Xu, J -- Isaacs, S D -- Brownstein, M J -- Bova, G S -- Guo, H -- Bujnovszky, P -- Nusskern, D R -- Damber, J E -- Bergh, A -- Emanuelsson, M -- Kallioniemi, O P -- Walker-Daniels, J -- Bailey-Wilson, J E -- Beaty, T H -- Meyers, D A -- Walsh, P C -- Collins, F S -- Trent, J M -- Isaacs, W B -- CA58236/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Nov 22;274(5291):1371-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Human Genome Research, National Institutes of Health, Bethesda, MD, USA. jtrent@nchgr.nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8910276" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Aged, 80 and over ; *Chromosome Mapping ; *Chromosomes, Human, Pair 1 ; Dinucleotide Repeats ; *Genes ; Genetic Linkage ; Genetic Markers ; Genetic Predisposition to Disease ; Humans ; Likelihood Functions ; Male ; Middle Aged ; North America ; Oncogenes ; Pedigree ; Prostatic Neoplasms/*genetics ; Risk Factors ; Statistics, Nonparametric ; Sweden
    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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