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  • Kinetics  (239)
  • Chemistry
  • American Association for the Advancement of Science (AAAS)  (250)
  • 1990-1994  (250)
  • 1955-1959
  • 1950-1954
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  • 1
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    Control of kinetic properties of AMPA receptor channels by nuclear RNA editing (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-09
    Description: AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor channels mediate the fast component of excitatory postsynaptic currents in the central nervous system. Site-selective nuclear RNA editing controls the calcium permeability of these channels, and RNA editing at a second site is shown here to affect the kinetic aspects of these channels in rat brain. In three of the four AMPA receptor subunits (GluR-B, -C, and -D), intronic elements determine a codon switch (AGA, arginine, to GGA, glycine) in the primary transcripts in a position termed the R/G site, which immediately precedes the alternatively spliced modules "flip" and "flop." The extent of editing at this site progresses with brain development in a manner specific for subunit and splice form, and edited channels possess faster recovery rates from desensitization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lomeli, H -- Mosbacher, J -- Melcher, T -- Hoger, T -- Geiger, J R -- Kuner, T -- Monyer, H -- Higuchi, M -- Bach, A -- Seeburg, P H -- New York, N.Y. -- Science. 1994 Dec 9;266(5191):1709-13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Neuroendocrinology, University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7992055" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Amino Acid Sequence ; Animals ; Base Sequence ; Brain/embryology/*metabolism ; Cell Nucleus/metabolism ; Exons ; Glutamic Acid/pharmacology ; Glycine/genetics ; Introns ; Kinetics ; Membrane Potentials ; Molecular Sequence Data ; Oocytes ; PC12 Cells ; Patch-Clamp Techniques ; *RNA Editing ; Rats ; Rats, Wistar ; Receptors, AMPA/*genetics/*metabolism ; Recombinant Proteins/metabolism ; Xenopus
    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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    Two identical noninteracting sites in an ion channel revealed by proton transfer (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-23
    Description: The functional consequences of single proton transfers occurring in the pore of a cyclic nucleotide-gated channel were observed with patch recording techniques. These results led to three conclusions about the chemical nature of ion binding sites in the conduction pathway: The channel contains two identical titratable sites, even though there are more than two (probably four) identical subunits; the sites are formed by glutamate residues that have a pKa (where K(a) is the acid constant) of 7.6; and protonation of one site does not perturb the pKa of the other. These properties point to an unusual arrangement of carboxyl side-chain residues in the pore of a cation channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Root, M J -- MacKinnon, R -- 5 T32 GM083113/GM/NIGMS NIH HHS/ -- GM47400/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 23;265(5180):1852-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7522344" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Calcium Channels/metabolism ; Catfishes ; Electric Conductivity ; Hydrogen-Ion Concentration ; Ion Channel Gating ; Ion Channels/chemistry/genetics/*metabolism ; Kinetics ; Molecular Sequence Data ; Mutation ; *Protons ; Sodium/metabolism ; Xenopus
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Stern-volmer in reverse: 2:1 stoichiometry of the cytochrome c-cytochrome c peroxidase electron-transfer complex (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-16
    Description: A reverse protocol for measurements of molecular binding and reactivity by excited-state quenching has been developed in which the quencher, held at a fixed concentration, is titrated by a photoexcitable probe molecule whose decay is monitored. The binding stoichiometries, affinities, and reactivities of the electron-transfer complexes between cytochrome c (Cc) and cytochrome c peroxidase (CcP) were determined over a wide range of ionic strengths (4.5 to 118 millimolar) by the study of photoinduced electron-transfer quenching of the triplet excited state of zinc-substituted Cc (ZnCc) by Fe3+CcP. The 2:1 stoichiometry seen for the binding of Cc to CcP at low ionic strength persists at the physiologically relevant ionic strengths and likely has functional significance. Analysis of the stoichiometric binding and rate constants confirms that one surface domain of CcP binds Cc with a high affinity but with poor electron-transfer quenching of triplet-state ZnCc, whereas a second binds weakly but with a high rate of electron-transfer quenching.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, J S -- Hoffman, B M -- HL13531/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 16;265(5179):1693-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Northwestern University, Evanston, IL 60208-3113.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8085152" target="_blank"〉PubMed〈/a〉
    Keywords: Cytochrome c Group/chemistry/*metabolism ; Cytochrome-c Peroxidase/chemistry/*metabolism ; Electron Transport ; Ferric Compounds ; Kinetics ; Osmolar Concentration ; Oxidation-Reduction ; Zinc
    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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  • 4
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    Rapid induction of Alzheimer A beta amyloid formation by zinc (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-02
    Description: A beta 1-40, a major component of Alzheimer's disease cerebral amyloid, is present in the cerebrospinal fluid and remains relatively soluble at high concentrations (less than or equal to 3.7 mM). Thus, physiological factors which induce A beta amyloid formation could provide clues to the pathogenesis of the disease. It has been shown that human A beta specifically and saturably binds zinc. Here, concentrations of zinc above 300 nM rapidly destabilized human A beta 1-40 solutions, inducing tinctorial amyloid formation. However, rat A beta 1-40 binds zinc less avidly and is immune to these effects, perhaps explaining the scarcity with which these animals form cerebral A beta amyloid. These data suggest a role for cerebral zinc metabolism in the neuropathogenesis of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bush, A I -- Pettingell, W H -- Multhaup, G -- d Paradis, M -- Vonsattel, J P -- Gusella, J F -- Beyreuther, K -- Masters, C L -- Tanzi, R E -- R01 AG11899-01/AG/NIA NIH HHS/ -- R01 NS30428-03/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1464-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics and Aging, Massachusetts General Hospital, Boston.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073293" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/etiology/*metabolism ; Amyloid beta-Peptides/chemistry/*metabolism ; Animals ; Brain/metabolism ; Edetic Acid/pharmacology ; Humans ; Kinetics ; Mice ; Peptide Fragments/chemistry/*metabolism ; Rats ; Solubility ; Zinc/*metabolism/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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  • 5
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    A specific inhibitor of the epidermal growth factor receptor tyrosine kinase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-19
    Description: A small molecule called PD 153035 inhibited the epidermal growth factor (EGF) receptor tyrosine kinase with a 5-pM inhibition constant. The inhibitor was specific for the EGF receptor tyrosine kinase and inhibited other purified tyrosine kinases only at micromolar or higher concentrations. PD 153035 rapidly suppressed autophosphorylation of the EGF receptor at low nanomolar concentrations in fibroblasts or in human epidermoid carcinoma cells and selectively blocked EGF-mediated cellular processes including mitogenesis, early gene expression, and oncogenic transformation. PD 153035 demonstrates an increase in potency over that of other tyrosine kinase inhibitors of four to five orders of magnitude for inhibition of isolated EGF receptor tyrosine kinase and three to four orders of magnitude for inhibition of cellular phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fry, D W -- Kraker, A J -- McMichael, A -- Ambroso, L A -- Nelson, J M -- Leopold, W R -- Connors, R W -- Bridges, A J -- New York, N.Y. -- Science. 1994 Aug 19;265(5175):1093-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Parke-Davis Pharmaceutical Research, Division of Warner-Lambert Company, Ann Arbor, MI 48105.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8066447" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Cell Transformation, Neoplastic/drug effects ; Epidermal Growth Factor/pharmacology ; Fibroblast Growth Factor 2/pharmacology ; Gene Expression/drug effects ; Humans ; Kinetics ; Mice ; Mitosis/drug effects ; Phosphorylation/drug effects ; Platelet-Derived Growth Factor/pharmacology ; Protein-Tyrosine Kinases/antagonists & inhibitors ; Quinazolines/*antagonists & inhibitors ; Receptor, Epidermal Growth Factor/*antagonists & inhibitors ; Tumor Cells, Cultured ; Tyrosine/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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  • 6
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    T cell receptor-MHC class I peptide interactions: affinity, kinetics, and specificity (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-12
    Description: The critical discriminatory event in the activation of T lymphocytes bearing alpha beta T cell receptors (TCRs) is their interaction with a molecular complex consisting of a peptide bound to a major histocompatibility complex (MHC)-encoded class I or class II molecule on the surface of an antigen-presenting cell. The kinetics of binding were measured of a purified TCR to molecular complexes of a purified soluble analog of the murine MHC class I molecule H-2Ld (sH-2Ld) and a synthetic octamer peptide p2CL in a direct, real-time assay based on surface plasmon resonance. The kinetic dissociation rate of the MHC-peptide complex from the TCR was rapid (2.6 x 10(-2) second-1, corresponding to a half-time for dissociation of approximately 27 seconds), and the kinetic association rate was 2.1 x 10(5) M-1 second-1. The equilibrium constant for dissociation was approximately 10(-7) M. These values indicate that TCRs must interact with a multivalent array of MHC-peptide complexes to trigger T cell signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corr, M -- Slanetz, A E -- Boyd, L F -- Jelonek, M T -- Khilko, S -- al-Ramadi, B K -- Kim, Y S -- Maher, S E -- Bothwell, A L -- Margulies, D H -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):946-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Section, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052850" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biosensing Techniques ; H-2 Antigens/*metabolism ; Histocompatibility Antigen H-2D ; Kinetics ; *Major Histocompatibility Complex ; Mice ; Molecular Sequence Data ; Oligopeptides/*metabolism ; Receptors, Antigen, T-Cell, alpha-beta/*metabolism ; Solubility
    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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    Kinetic intermediates in RNA folding (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-12
    Description: The folding pathways of large, highly structured RNA molecules are largely unexplored. Insight into both the kinetics of folding and the presence of intermediates was provided in a study of the Mg(2+)-induced folding of the Tetrahymena ribozyme by hybridization of complementary oligodeoxynucleotide probes. This RNA folds via a complex mechanism involving both Mg(2+)-dependent and Mg(2+)-independent steps. A hierarchical model for the folding pathway is proposed in which formation of one helical domain (P4-P6) precedes that of a second helical domain (P3-P7). The overall rate-limiting step is formation of P3-P7, and takes place with an observed rate constant of 0.72 +/- 0.14 minute-1. The folding mechanism of large RNAs appears similar to that of many multidomain proteins in that formation of independently stable substructures precedes their association into the final conformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zarrinkar, P P -- Williamson, J R -- New York, N.Y. -- Science. 1994 Aug 12;265(5174):918-24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8052848" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Introns ; Kinetics ; Magnesium/metabolism/pharmacology ; Models, Chemical ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Nucleic Acid Hybridization ; Oligonucleotide Probes ; RNA, Catalytic/*chemistry/metabolism ; RNA, Protozoan/*chemistry ; Ribonuclease H/metabolism ; Temperature ; Tetrahymena/*genetics
    Print ISSN: 0036-8075
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  • 8
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    Stimulation of RNA polymerase II elongation by chromosomal protein HMG-14 (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-05
    Description: The high-mobility group protein 14 (HMG-14) is a non-histone chromosomal protein that is preferentially associated with transcriptionally active chromatin. To assess the effect of HMG-14 on transcription by RNA polymerase II, in vivo-assembled chromatin with elevated amounts of HMG-14 was obtained. Here it is shown that HMG-14 enhanced transcription on chromatin templates but not on DNA templates. This protein stimulated the rate of elongation by RNA polymerase II but not the level of initiation of transcription. These findings suggest that the association of HMG-14 with nucleosomes is part of the cellular process involved in the generation of transcriptionally active chromatin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ding, H F -- Rimsky, S -- Batson, S C -- Bustin, M -- Hansen, U -- GM-36667/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):796-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Genetics, Dana-Farber Cancer Institute, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8047885" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/metabolism ; HeLa Cells ; High Mobility Group Proteins/*physiology ; Humans ; Kinetics ; RNA Polymerase II/*metabolism ; Simian virus 40/genetics ; Templates, Genetic ; Transcription, Genetic/*physiology
    Print ISSN: 0036-8075
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  • 9
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    Blockage of NF-kappa B signaling by selective ablation of an mRNA target by 2-5A antisense chimeras (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-08-05
    Description: Activation of 2-5A-dependent ribonuclease by 5'-phosphorylated, 2',5'-linked oligoadenylates, known as 2-5A, is one pathway of interferon action. Unaided uptake into HeLa cells of 2-5A linked to an antisense oligonucleotide resulted in the selective ablation of messenger RNA for the double-stranded RNA (dsRNA)-dependent protein kinase PKR. Similarly, purified, recombinant human 2-5A-dependent ribonuclease was induced to selectively cleave PKR messenger RNA. Cells depleted of PKR activity were unresponsive to activation of nuclear factor-kappa B (NF-kappa B) by the dsRNA poly(I):poly(C), which provides direct evidence that PKR is a transducer for the dsRNA signaling of NF-kappa B.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maran, A -- Maitra, R K -- Kumar, A -- Dong, B -- Xiao, W -- Li, G -- Williams, B R -- Torrence, P F -- Silverman, R H -- AI 28253/AI/NIAID NIH HHS/ -- AI 34039-02/AI/NIAID NIH HHS/ -- CA 44059/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Aug 5;265(5173):789-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Cleveland Clinic Foundation, OH 44195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7914032" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine Nucleotides/chemical synthesis/*pharmacology ; Base Sequence ; Endoribonucleases/metabolism ; Enzyme Activation ; HeLa Cells ; Humans ; Kinetics ; Molecular Sequence Data ; NF-kappa B/*antagonists & inhibitors ; Oligonucleotides, Antisense/chemical synthesis/*pharmacology ; Oligoribonucleotides/chemical synthesis/*pharmacology ; Protein-Serine-Threonine Kinases/*genetics ; RNA, Messenger/drug effects ; Signal Transduction/*drug effects ; eIF-2 Kinase
    Print ISSN: 0036-8075
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  • 10
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    Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-07-29
    Description: The Escherichia coli chaperonins GroEL and GroES facilitate protein folding in an adenosine triphosphate (ATP)-dependent manner. After a single cycle of ATP hydrolysis by the adenosine triphosphatase (ATPase) activity of GroEL, the bi-toroidal GroEL formed a stable asymmetric ternary complex with GroES and nucleotide (bulletlike structures). With each subsequent turnover, ATP was hydrolyzed by one ring of GroEL in a quantized manner, completely releasing the adenosine diphosphate and GroES that were tightly bound to the other ring as a result of the previous turnover. The catalytic cycle involved formation of a symmetric complex (football-like structures) as an intermediate that accumulated before the rate-determining hydrolytic step. After one to two cycles, most of the substrate protein dissociated still in a nonnative state, which is consistent with intermolecular transfer of the substrate protein between toroids of high and low affinity. A unifying model for chaperonin-facilitated protein folding based on successive rounds of binding and release, and partitioning between committed and kinetically trapped intermediates, is proposed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Todd, M J -- Viitanen, P V -- Lorimer, G H -- New York, N.Y. -- Science. 1994 Jul 29;265(5172):659-66.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉E. I. DuPont de Nemours and Company, Central Research and Development Department, Wilmington, DE 19880.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7913555" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*metabolism ; Bacterial Proteins/*metabolism ; Binding Sites ; Chaperonin 10 ; Chaperonin 60 ; Heat-Shock Proteins/*metabolism ; Kinetics ; Models, Chemical ; *Protein Folding ; Ribulose-Bisphosphate Carboxylase/metabolism
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