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  • Kinetics  (17)
  • Structure-Activity Relationship
  • American Association for the Advancement of Science (AAAS)  (21)
  • Annual Reviews
  • 1990-1994  (21)
  • 1980-1984
  • 1975-1979
  • 1965-1969
  • 1935-1939
  • 1990  (21)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (21)
  • Annual Reviews
Years
  • 1990-1994  (21)
  • 1980-1984
  • 1975-1979
  • 1965-1969
  • 1935-1939
Year
  • 1
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    Design, activity, and 2.8 A crystal structure of a C2 symmetric inhibitor complexed to HIV-1 protease (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-03
    Description: A two-fold (C2) symmetric inhibitor of the protease of human immunodeficiency virus type-1 (HIV-1) has been designed on the basis of the three-dimensional symmetry of the enzyme active site. The symmetric molecule inhibited both protease activity and acute HIV-1 infection in vitro, was at least 10,000-fold more potent against HIV-1 protease than against related enzymes, and appeared to be stable to degradative enzymes. The 2.8 angstrom crystal structure of the inhibitor-enzyme complex demonstrated that the inhibitor binds to the enzyme in a highly symmetric fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erickson, J -- Neidhart, D J -- VanDrie, J -- Kempf, D J -- Wang, X C -- Norbeck, D W -- Plattner, J J -- Rittenhouse, J W -- Turon, M -- Wideburg, N -- AI 27220/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1990 Aug 3;249(4968):527-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Computer-Assisted Molecular Design, Abbott Laboratories, Abbott Park, IL 60064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2200122" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Drug Design ; Endopeptidases/*metabolism ; Gene Products, pol/*metabolism ; HIV Protease ; HIV-1/*enzymology ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Protease Inhibitors/*pharmacology ; Protein Conformation ; Sugar Alcohols/*pharmacology ; Valine/*analogs & derivatives/pharmacology
    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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    Prevention of HIV-1 infection and preservation of CD4 function by the binding of CPFs to gp120 (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-20
    Description: Infection by human immunodeficiency virus type-1 (HIV-1) is initiated when its envelope protein, gp120, binds to its receptor, the cell surface glycoprotein CD4. Small molecules, termed N-carbomethoxycarbonyl-prolyl-phenylalanyl benzyl esters (CPFs), blocked this binding. CPFs interacted with gp120 and did not interfere with the binding of CD4 to class II major histocompatibility complex molecules. One CPF isomer, CPF(DD), preserved CD4-dependent T cell function while inhibiting HIV-1 infection of H9 tumor cells and human T cells. Although the production of viral proteins in infected T cells is unaltered by CPF(DD), this compound prevents the spread of infection in an in vitro model system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finberg, R W -- Diamond, D C -- Mitchell, D B -- Rosenstein, Y -- Soman, G -- Norman, T C -- Schreiber, S L -- Burakoff, S J -- New York, N.Y. -- Science. 1990 Jul 20;249(4966):287-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Department of Medicine, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2115689" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*immunology ; Antiviral Agents/*pharmacology ; Benzyl Compounds/pharmacology ; Cell Line ; Genes, MHC Class II ; HIV Envelope Protein gp120/*immunology ; HIV-1/drug effects/immunology/*physiology ; Humans ; Kinetics ; T-Lymphocytes/immunology
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  • 3
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    Electrophoresis of flexible macromolecules: evidence for a new mode of transport in gels (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-08
    Description: Movement of macromolecules through low concentration agarose gels was investigated with linear poly(styrenesulfonate), linear DNA, star-shaped poly(styrenesulfonate), and circular DNA. Mobilities of weakly entangled flexible macromolecules were independent of molecular radius; within a homologous chemical sequence, electrophoretic separation at low field strengths depended solely on the degree of polymerization. These observations cannot be explained either by sieving or by reptation mechanisms; transport was apparently controlled by spatial variations of chain configurational entropy. Only when the chain was highly entangled did chain topology affect mobility. Evidence for entropically regulated transport clarifies how gel electrophoresis separates flexible macromolecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smisek, D L -- Hoagland, D A -- New York, N.Y. -- Science. 1990 Jun 8;248(4960):1221-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Polymer Science and Engineering, University of Massachusetts, Amherst 01003.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2349481" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/*isolation & purification ; DNA, Circular/*isolation & purification ; Electrophoresis, Agar Gel/methods ; Molecular Conformation ; Polystyrenes/*isolation & purification ; Resins, Synthetic ; Structure-Activity Relationship
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  • 4
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    Evidence of changes in protease sensitivity and subunit exchange rate on DNA binding by C/EBP (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-08-17
    Description: The transcription factor C/EBP uses a bipartite structural motif to bind DNA. Two protein chains dimerize through a set of amphipathic alpha helices termed the leucine zipper. Highly basic polypeptide regions emerge from the zipper to form a linked set of DNA contact surfaces. In the recently proposed a "scissors grip" model, the paired set of basic regions begin DNA contact at a central point and track in opposite directions along the major groove, forming a molecular clamp around DNA. This model predicts that C/EBP must undertake significant changes in protein conformation as it binds and releases DNA. The basic region of ligand-free C/EBP is highly sensitive to protease digestion. Pronounced resistance to proteolysis occurred when C/EBP associated with its specific DNA substrate. Sequencing of discrete proteolytic fragments showed that prominent sites for proteolysis occur at two junction points predicted by the "scissors grip" model. One junction corresponds to the cleft where the basic regions emerge from the leucine zipper. The other corresponds to a localized nonhelical segment that has been hypothesized to contain an N-cap and facilitate the sharp angulation necessary for the basic region to track continuously in the major groove of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuman, J D -- Vinson, C R -- McKnight, S L -- New York, N.Y. -- Science. 1990 Aug 17;249(4970):771-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Department of Embryology, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2202050" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; CCAAT-Enhancer-Binding Proteins ; Chromatography, High Pressure Liquid ; DNA/*metabolism ; DNA-Binding Proteins/metabolism ; Kinetics ; Leucine ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Peptide Fragments/metabolism ; Peptide Hydrolases/*metabolism ; Protein Conformation ; Transcription Factors/*metabolism ; Trypsin/metabolism
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  • 5
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    Direct interaction of a ligand for the erbB2 oncogene product with the EGF receptor and p185erbB2 (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-28
    Description: The erbB2 oncogene encodes a 185-kilodalton transmembrane protein whose sequence is similar to the epidermal growth factor receptor (EGFR). A 30-kilodalton factor (gp30) secreted from MDA-MB-231 human breast cancer cells was shown to be a ligand for p185erbB2. An antibody to EGFR abolished the tyrosine phosphorylation induced by EGF and transforming growth factor-alpha (TGF-alpha) but only partially blocked that produced by gp30 in SK-BR-3 breast cancer cells. In two cell lines that overexpress erbB2 but do not expresss EGFR (MDA-MB-453 breast cancer cells and a Chinese hamster ovary cell line that had been transfected with erbB2), phosphorylation of p185erbB2 was induced only by gp30. The gp30 specifically inhibited the growth of cells that overexpressed p185erbB2. An antibody to EGFR had no effect on the inhibition of SK-BR-3 cell colony formation obtained with gp30. Thus, it appeared that gp30 interacted directly with the EGFR and erbB2. Direct binding of gp30 to p185erbB2 was confirmed by binding competition experiments, where gp30 was found to displace the p185erbB2 binding of a specific antibody to p185erbB2. The evidence described here suggests that gp30 is a ligand for p185erbB2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lupu, R -- Colomer, R -- Zugmaier, G -- Sarup, J -- Shepard, M -- Slamon, D -- Lippman, M E -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1552-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vincent T. Lombardi Cancer Research Center, Georgetown University Medical Center, Washington, DC 20007.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218496" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Binding, Competitive ; Breast Neoplasms ; Cell Line ; Chromatography, Affinity ; Female ; Humans ; Kinetics ; Ligands ; Molecular Weight ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Proto-Oncogene Proteins/genetics/immunology/*metabolism ; Proto-Oncogenes ; Receptor, Epidermal Growth Factor/isolation & purification/*metabolism ; Transfection
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  • 6
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    Recovery of mitogenic activity of a growth factor mutant with a nuclear translocation sequence (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-28
    Description: Heparin-binding growth factor-1 (HBGF-1) is an angiogenic polypeptide mitogen for mesoderm- and neuroectoderm-derived cells in vitro and remains biologically active after truncation of the amino-terminal domain (HBGF-1 alpha) of the HBGF-1 beta precursor. Polymerase chain reaction mutagenesis and prokaryotic expression systems were used to prepare a mutant of HBGF-1 alpha lacking a putative nuclear translocation sequence (amino acid residues 21 to 27; HBGF-1U). Although HBGF-1U retains its ability to bind to heparin, HBGF-1U fails to induce DNA synthesis and cell proliferation at concentrations sufficient to induce intracellular receptor-mediated tyrosine phosphorylation and c-fos expression. Attachment of the nuclear translocation sequence from yeast histone 2B at the amino terminus of HBGF-1U yields a chimeric polypeptide (HBGF-1U2) with mitogenic activity in vitro and indicates that nuclear translocation is important for this biological response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Imamura, T -- Engleka, K -- Zhan, X -- Tokita, Y -- Forough, R -- Roeder, D -- Jackson, A -- Maier, J A -- Hla, T -- Maciag, T -- HL 32348/HL/NHLBI NIH HHS/ -- HL 35627/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1567-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, Jerome H. Holland Laboratory for the Biomedical Sciences, American Red Cross, Rockville, MD 20855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1699274" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding, Competitive ; Cattle ; Cell Division/drug effects ; Cell Line ; Cell Nucleus/metabolism ; Cells, Cultured ; DNA Replication/drug effects ; Endothelium, Vascular/drug effects/metabolism ; Fibroblast Growth Factor 1/*genetics/metabolism/pharmacology ; Kinetics ; Mice ; Mitogens/pharmacology ; Molecular Sequence Data ; *Mutation ; Oligonucleotide Probes ; Receptors, Mitogen/metabolism ; Receptors, Vascular Endothelial Growth Factor ; Recombinant Proteins/metabolism/pharmacology ; Transcription, Genetic/drug effects
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  • 7
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    Intracellular calcium release mediated by sphingosine derivatives generated in cells (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-29
    Description: Soluble and hydrophobic lipid breakdown products have a variety of important signaling roles in cells. Here sphingoid bases derived in cells from sphingolipid breakdown are shown to have a potent and direct effect in mediating calcium release from intracellular stores. Sphingosine must be enzymically converted within the cell to a product believed to be sphingosine-1-phosphate, which thereafter effects calcium release from a pool including the inositol 1,4,5-trisphosphate-sensitive calcium pool. The sensitivity, molecular specificity, and reversibility of the effect on calcium movements closely parallel sphingoid base-mediated inhibition of protein kinase C. Generation of sphingoid bases in cells may activate a dual signaling pathway involving regulation of calcium and protein kinase C, comparable perhaps to the phosphatidylinositol and calcium signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghosh, T K -- Bian, J -- Gill, D L -- NS19304/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1990 Jun 29;248(4963):1653-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Maryland School of Medicine, Baltimore 21201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2163543" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/pharmacology ; Animals ; Calcimycin/pharmacology ; Calcium/*metabolism ; Cell Line ; Kinetics ; Phosphoric Monoester Hydrolases/metabolism ; Phosphorylcholine/analogs & derivatives/pharmacology ; Protein Kinase C/metabolism ; Second Messenger Systems/drug effects ; Sphingosine/*analogs & derivatives/*pharmacology ; Thermodynamics
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  • 8
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    The enzymic nature of antibody catalysis: development of multistep kinetic processing (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-11-23
    Description: Detailed kinetic investigations of a catalytic antibody that promotes the hydrolyses of an anilide and phenyl ester show that this catalyst uses a multistep kinetic sequence resembling that found in serine proteases to hydrolyze its substrates, although antibody was elicited to a single transition-state analog. Like the serine proteases the antibody catalyzes the hydrolysis reactions through a putative covalent intermediate, but unlike the enzymes it may use hydroxide ion to cleave the intermediates. Nevertheless, the antibody is a potent catalyst with turnover at higher pH values rivaling that of chymotrypsin. This analysis also reveals that turnover by the antibody is ultimately limited by product desorption, suggesting that improvements in catalytic efficiency may be achieved by judicious changes in the structure of the substrate, so that it is not superimposable on that of the eliciting hapten.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benkovic, S J -- Adams, J A -- Borders, C L Jr -- Janda, K D -- Lerner, R A -- GM4385801/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Nov 23;250(4984):1135-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pennsylvania State University, Department of Chemistry, University Park 16802.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2251500" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Aniline Compounds/metabolism ; Antibodies/*metabolism ; Catalysis ; Enzymes/*metabolism ; Hydrogen-Ion Concentration ; Hydrolysis ; Kinetics ; Nitrophenols/metabolism ; Spectrometry, Fluorescence ; Thermodynamics
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  • 9
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    The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-02-23
    Description: Bacterial MerR proteins are dimeric DNA-binding proteins that mediate the Hg(II)-dependent induction of mercury resistance operons. Site-directed mutagenesis of the Bacillus sp. RC607 MerR protein reveals that three of four Cys residues per monomer are required for Hg(II) binding at the single high-affinity binding site. Inactive mutant homodimers can exchange subunits to form heterodimers active for Hg(II) binding. Studies of a heterodimer retaining only three of eight cysteine residues per dimer reveal that Cys79 in one subunit and Cys114 and Cys123 in the second subunit are necessary and sufficient for high-affinity Hg(II) binding in an asymmetric, subunit bridging coordination complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Helmann, J D -- Ballard, B T -- Walsh, C T -- GM20011/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1990 Feb 23;247(4945):946-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2305262" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacillus/*analysis/genetics ; Bacterial Proteins/genetics/*metabolism ; Base Sequence ; Binding Sites ; Cations ; DNA-Binding Proteins/genetics/*metabolism ; Macromolecular Substances ; Mercury/*metabolism ; Molecular Sequence Data ; Mutation ; Structure-Activity Relationship
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  • 10
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    Extension of the life-span of human endothelial cells by an interleukin-1 alpha antisense oligomer (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-09-28
    Description: The proliferative potential of human diploid endothelial cells is finite, and cellular senescence in vitro is accompanied by the failure of the endothelial cell to respond to exogenous growth factors. Senescent human endothelial cells were shown to contain high amounts of the transcript for the cytokine interleukin-1 alpha (IL-1 alpha), a potent inhibitor of endothelial cell proliferation in vitro. In contrast, transformed human endothelial cells did not contain detectable IL-1 alpha messenger RNA. Treatment of human endothelial cell populations with an antisense oligodeoxynucleotide to the human IL-1 alpha transcript prevented cell senescence and extended the proliferative life-span of the cells in vitro. Removal of the IL-1 alpha antisense oligomer resulted in the generation of the senescent phenotype and loss of proliferative potential. These data suggest that human endothelial cell senescence in vitro is a dynamic process regulated by the potential intracellular activity of IL-1 alpha.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maier, J A -- Voulalas, P -- Roeder, D -- Maciag, T -- AG07450/AG/NIA NIH HHS/ -- HL32348/HL/NHLBI NIH HHS/ -- HL35627/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1990 Sep 28;249(4976):1570-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biology, Jerome H. Holland, Laboratory for the Biomedical Sciences, American Red Cross, Rockville, MD 20855.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2218499" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Division ; Cell Survival ; Cells, Cultured ; Endothelium, Vascular/*cytology/physiology ; Humans ; Interleukin-1/*genetics ; Kinetics ; Molecular Sequence Data ; Oligonucleotide Probes ; RNA, Antisense/*genetics
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