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  • Articles  (122)
  • Temperature  (63)
  • Binding Sites  (61)
  • American Association for the Advancement of Science (AAAS)  (107)
  • Springer  (15)
  • Elsevier
  • 2020-2024
  • 1995-1999  (122)
  • 1997  (122)
Collection
  • Articles  (122)
Source
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (107)
  • Springer  (15)
  • Elsevier
  • Wiley-Blackwell  (1)
Years
  • 2020-2024
  • 1995-1999  (122)
Year
Journal
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  • 1
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    Photochemically driven collapse of Titan's atmosphere (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-01-31
    Description: Saturn's giant moon Titan has a thick (1.5 bar) nitrogen atmosphere, which has a temperature structure that is controlled by the absorption of solar and thermal radiation by methane, hydrogen, and organic aerosols into which methane is irreversibly converted by photolysis. Previous studies of Titan's climate evolution have been done with the assumption that the methane abundance was maintained against photolytic depletion throughout Titan's history, either by continuous supply from the interior or by buffering by a surface or near surface reservoir. Radiative-convective and radiative-saturated equilibrium models of Titan's atmosphere show that methane depletion may have allowed Titan's atmosphere to cool so that nitrogen, its main constituent, condenses onto the surface, collapsing Titan into a Triton-like frozen state with a thin atmosphere.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lorenz, R D -- McKay, C P -- Lunine, J I -- New York, N.Y. -- Science. 1997 Jan 31;275(5300):642-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Planetary Sciences, Lunar and Planetary Laboratory, University of Arizona, Tucson 85721, USA.rlorenz@pl.arizona.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9005844" target="_blank"〉PubMed〈/a〉
    Keywords: Atmosphere ; *Evolution, Planetary ; *Extraterrestrial Environment ; *Methane ; *Nitrogen ; Photolysis ; *Saturn ; Temperature
    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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  • 2
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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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  • 3
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    Discrete determinants in transfer RNA for editing and aminoacylation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-23
    Description: During translation errors of aminoacylation are corrected in editing reactions which ensure that an amino acid is stably attached to its corresponding transfer RNA (tRNA). Previous studies have not shown whether the tRNA nucleotides needed for effecting translational editing are the same as or distinct from those required for aminoacylation, but several considerations have suggested that they are the same. Here, designed tRNAs that are highly active for aminoacylation but are not active in translational editing are presented. The editing reaction can be controlled by manipulation of nucleotides at the corner of the L-shaped tRNA. In contrast, these manipulations do not affect aminoacylation. These results demonstrate the segregation of nucleotide determinants for the editing and aminoacylation functions of tRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hale, S P -- Auld, D S -- Schmidt, E -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 May 23;276(5316):1250-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9157882" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Escherichia coli ; Molecular Sequence Data ; Nucleic Acid Conformation ; *RNA Editing ; RNA, Transfer/*metabolism ; RNA, Transfer, Ile/chemistry/metabolism ; RNA, Transfer, Val/chemistry/metabolism
    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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  • 4
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    Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-18
    Description: The crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coli DnaK [heat shock protein 70 (Hsp70)] was determined at 2.8 angstrom resolution. A dimer of GrpE binds asymmetrically to a single molecule of DnaK. The structure of the nucleotide-free ATPase domain in complex with GrpE resembles closely that of the nucleotide-bound mammalian Hsp70 homolog, except for an outward rotation of one of the subdomains of the protein. This conformational change is not consistent with tight nucleotide binding. Two long alpha helices extend away from the GrpE dimer and suggest a role for GrpE in peptide release from DnaK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrison, C J -- Hayer-Hartl, M -- Di Liberto, M -- Hartl, F -- Kuriyan, J -- New York, N.Y. -- Science. 1997 Apr 18;276(5311):431-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratories of Molecular Biophysics and Howard Hughes Medical Institute, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9103205" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphatases/*chemistry/metabolism ; Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Crystallography, X-Ray ; Dimerization ; *Escherichia coli Proteins ; HSP70 Heat-Shock Proteins/*chemistry/metabolism ; Heat-Shock Proteins/*chemistry/metabolism ; Hydrogen Bonding ; Models, Molecular ; Molecular Chaperones/*chemistry/metabolism ; Molecular Sequence Data ; *Protein Conformation ; Protein Structure, Secondary
    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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  • 5
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    Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-21
    Description: Many neuropeptides and peptide hormones require amidation at the carboxyl terminus for activity. Peptidylglycine alpha-amidating monooxygenase (PAM) catalyzes the amidation of these diverse physiological regulators. The amino-terminal domain of the bifunctional PAM protein is a peptidylglycine alpha-hydroxylating monooxygenase (PHM) with two coppers that cycle through cupric and cuprous oxidation states. The anomalous signal of the endogenous coppers was used to determine the structure of the catalytic core of oxidized rat PHM with and without bound peptide substrate. These structures strongly suggest that the PHM reaction proceeds via activation of substrate by a copper-bound oxygen species. The mechanistic and structural insight gained from the PHM structures can be directly extended to dopamine beta-monooxygenase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prigge, S T -- Kolhekar, A S -- Eipper, B A -- Mains, R E -- Amzel, L M -- DK32949/DK/NIDDK NIH HHS/ -- GM44692/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 Nov 14;278(5341):1300-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biophysical Chemistry, Johns Hopkins School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9360928" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Catalysis ; Copper/chemistry/metabolism ; Crystallography, X-Ray ; Dipeptides/metabolism ; Dopamine beta-Hydroxylase/chemistry/metabolism ; Electrons ; Hydroxylation ; Ligands ; Mixed Function Oxygenases/*chemistry/metabolism ; Models, Molecular ; *Multienzyme Complexes ; Oxidation-Reduction ; Oxygen/metabolism ; Peptides/metabolism ; *Protein Conformation ; Protein Structure, Secondary ; Rats
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  • 6
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    Precursor-directed biosynthesis of erythromycin analogs by an engineered polyketide synthase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-18
    Description: A genetic block was introduced in the first condensation step of the polyketide biosynthetic pathway that leads to the formation of 6-deoxyerythronolide B (6-dEB), the macrocyclic precursor of erythromycin. Exogenous addition of designed synthetic molecules to small-scale cultures of this null mutant resulted in highly selective multimilligram production of unnatural polyketides, including aromatic and ring-expanded variants of 6-dEB. Unexpected incorporation patterns were observed, illustrating the catalytic versatility of modular polyketide synthases. Further processing of some of these scaffolds by postpolyketide enzymes of the erythromycin pathway resulted in the generation of novel antibacterials with in vitro potency comparable to that of their natural counterparts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobsen, J R -- Hutchinson, C R -- Cane, D E -- Khosla, C -- CA66736/CA/NCI NIH HHS/ -- GM22172/GM/NIGMS NIH HHS/ -- GM31925/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):367-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Stanford University, Stanford, CA 94305-5025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9219693" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Bacillus cereus/drug effects/growth & development ; Binding Sites ; Catalysis ; Cyclization ; Erythromycin/*analogs & derivatives/biosynthesis/pharmacology ; Microbial Sensitivity Tests ; Multienzyme Complexes/*genetics/*metabolism ; *Mutagenesis, Site-Directed ; Saccharopolyspora/genetics/metabolism ; Streptomyces/enzymology/genetics/*metabolism ; Transformation, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-02-28
    Description: The small guanosine triphosphatase (GTPase) Rho is implicated in the formation of stress fibers and focal adhesions in fibroblasts stimulated by extracellular signals such as lysophosphatidic acid (LPA). Rho-kinase is activated by Rho and may mediate some biological effects of Rho. Microinjection of the catalytic domain of Rho-kinase into serum-starved Swiss 3T3 cells induced the formation of stress fibers and focal adhesions, whereas microinjection of the inactive catalytic domain, the Rho-binding domain, or the pleckstrin-homology domain inhibited the LPA-induced formation of stress fibers and focal adhesions. Thus, Rho-kinase appears to mediate signals from Rho and to induce the formation of stress fibers and focal adhesions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amano, M -- Chihara, K -- Kimura, K -- Fukata, Y -- Nakamura, N -- Matsuura, Y -- Kaibuchi, K -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1308-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Signal Transduction, Nara Institute of Science and Technology, Ikoma 630-01, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036856" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Actins/*metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Binding Sites ; *Cell Adhesion ; Cell Line ; DNA, Complementary/genetics ; Enzyme Inhibitors/pharmacology ; GTP Phosphohydrolases/metabolism ; Intracellular Signaling Peptides and Proteins ; Lysophospholipids/pharmacology ; Mice ; Mutation ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Staurosporine/pharmacology ; rho-Associated Kinases
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  • 8
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    Activated acetic acid by carbon fixation on (Fe,Ni)S under primordial conditions (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-11
    Description: In experiments modeling the reactions of the reductive acetyl-coenzyme A pathway at hydrothermal temperatures, it was found that an aqueous slurry of coprecipitated NiS and FeS converted CO and CH3SH into the activated thioester CH3-CO-SCH3, which hydrolyzed to acetic acid. In the presence of aniline, acetanilide was formed. When NiS-FeS was modified with catalytic amounts of selenium, acetic acid and CH3SH were formed from CO and H2S alone. The reaction can be considered as the primordial initiation reaction for a chemoautotrophic origin of life.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huber, C -- Wachtershauser, G -- New York, N.Y. -- Science. 1997 Apr 11;276(5310):245-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Organic Chemistry and Biochemistry, Technische Universitat Munchen, Lichtenbergstrasse 4, D-85747 Garching, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9092471" target="_blank"〉PubMed〈/a〉
    Keywords: Acetic Acid/*chemistry ; Carbon Monoxide/*chemistry ; Catalysis ; Cobalt/chemistry ; *Evolution, Chemical ; Ferrous Compounds/*chemistry ; Hydrogen Sulfide/chemistry ; Hydrogen-Ion Concentration ; Hydrolysis ; Nickel/*chemistry ; *Origin of Life ; Oxidation-Reduction ; Sulfhydryl Compounds/chemistry ; Temperature
    Print ISSN: 0036-8075
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  • 9
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    New lesion found in diseased brains (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roush, W -- New York, N.Y. -- Science. 1997 Jul 4;277(5322):31-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9229767" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/metabolism/*pathology ; Amyloid beta-Peptides/immunology ; Antibodies/immunology ; Binding Sites ; Brain/*pathology ; Brain Chemistry ; Humans ; Phosphates/metabolism ; tau Proteins/immunology/metabolism
    Print ISSN: 0036-8075
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  • 10
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    Prebiotic chemistry. Where smokers rule (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-04-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crabtree, R H -- New York, N.Y. -- Science. 1997 Apr 11;276(5310):222.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Yale University Chemistry Department, New Haven, CT 06520-8107, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9132945" target="_blank"〉PubMed〈/a〉
    Keywords: Acetate-CoA Ligase/metabolism ; Acetates/*chemistry ; Acetyl Coenzyme A/chemistry ; Carbon Monoxide/chemistry ; Catalysis ; *Evolution, Chemical ; Ferrous Compounds/chemistry ; Nickel/chemistry ; *Origin of Life ; Temperature
    Print ISSN: 0036-8075
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