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  • Kinetics
  • American Association for the Advancement of Science (AAAS)  (10)
  • American Association for the Advancement of Science
  • American Association of Petroleum Geologists (AAPG)
  • American Physical Society
  • Elsevier
  • 1995-1999  (10)
  • 1990-1994
  • 1996  (10)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (10)
  • American Association for the Advancement of Science
  • American Association of Petroleum Geologists (AAPG)
  • American Physical Society
  • Elsevier
    • +
Years
  • 1995-1999  (10)
  • 1990-1994
Year
  • 1
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    Amide cleavage by a ribozyme: correction (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-04-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joyce, G F -- Dai, X -- De Mesmaeker, A -- New York, N.Y. -- Science. 1996 Apr 5;272(5258):18-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8600526" target="_blank"〉PubMed〈/a〉
    Keywords: Amides/*metabolism ; Kinetics ; RNA, Catalytic/*metabolism ; Ribonucleosides/metabolism
    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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    Catalytic role of 2'-hydroxyl groups within a group II intron active site (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-08
    Description: Domain 5 is an essential active-site component of group II intron ribozymes. The role of backbone substituents in D5 function was explored through synthesis of a series of derivatives containing deoxynucleotides at each position along the D5 strand. Kinetic screens revealed that eight 2'-hydroxyl groups were likely to be critical for activity of D5. Through two separate methods, including competitive inhibition and direct kinetic analysis, effects on binding and chemistry were distinguished. Depending on their function, important 2'-hydroxyl groups lie on opposite faces of the molecule, defining distinct loci for molecular recognition and catalysis by D5.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abramovitz, D L -- Friedman, R A -- Pyle, A M -- GM41371/GM/NIGMS NIH HHS/ -- GM50313/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1996 Mar 8;271(5254):1410-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8596912" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Binding Sites ; Catalysis ; Exons ; Hydrogen Bonding ; Hydroxyl Radical/chemistry ; *Introns ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides/chemistry/metabolism ; RNA/metabolism ; RNA, Catalytic/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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  • 3
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    Protein folding monitored at individual residues during a two-dimensional NMR experiment (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-15
    Description: An approach is described to monitor directly at the level of individual residues the formation of structure during protein folding. A two-dimensional heteronuclear nuclear magnetic resonance (NMR) spectrum was recorded after the rapid initiation of the refolding of a protein labeled with nitrogen-15. The intensities and line shapes of the cross peaks in the spectrum reflected the kinetic time course of the folding events that occurred during the spectral accumulation. The method was used to demonstrate the cooperative nature of the acquisition of the native main chain fold of apo bovine alpha-lactalbumin. The general approach, however, should be applicable to the investigation of a wide range of chemical reactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Balbach, J -- Forge, V -- Lau, W S -- van Nuland, N A -- Brew, K -- Dobson, C M -- New York, N.Y. -- Science. 1996 Nov 15;274(5290):1161-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford OX1 3QT, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8895458" target="_blank"〉PubMed〈/a〉
    Keywords: Circular Dichroism ; Fourier Analysis ; Hydrogen-Ion Concentration ; Kinetics ; Lactalbumin/*chemistry ; *Magnetic Resonance Spectroscopy ; Nitrogen Isotopes ; *Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Spectrometry, Fluorescence
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  • 4
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    Enhanced dissociation of HLA-DR-bound peptides in the presence of HLA-DM (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-10-25
    Description: Human leukocyte antigen (HLA)-DM is a critical participant in antigen presentation that catalyzes the release of class II-associated invariant chain-derived peptides (CLIP) from newly synthesized class II histocompatibility molecules, freeing the peptide-binding site for acquisition of antigenic peptides. The mechanism for the selective release of CLIP but not other peptides is unknown. DM was found to enhance the rate of peptide dissociation to an extent directly proportional to the intrinsic rate of peptide dissociation from HLA-DR, regardless of peptide sequence. Thus, CLIP is rapidly released in the presence of DM, because its intrinsic rate of dissociation is relatively high. In antigen presentation, DM has the potential to markedly enhance the rate of peptide exchange, favoring the presentation of peptides with slower intrinsic rates of dissociation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, D A -- Evavold, B D -- Jensen, P E -- AI30554/AI/NIAID NIH HHS/ -- AI33614/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1996 Oct 25;274(5287):618-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA 30322, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8849454" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigen Presentation ; Antigens, Differentiation, B-Lymphocyte/*metabolism ; Binding Sites ; HLA-D Antigens/*metabolism ; HLA-DR Antigens/immunology/*metabolism ; Histocompatibility Antigens Class II/*metabolism ; Humans ; Kinetics ; Molecular Sequence Data ; Peptides/immunology/*metabolism ; Recombinant Fusion Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 5
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    Assembly of a ribonucleoprotein catalyst by tertiary structure capture (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-19
    Description: CBP2 is an RNA tertiary structure binding protein required for efficient splicing of a yeast mitochondrial group I intron. CBP2 must wait for folding of the two RNA domains that make up the catalytic core before it can bind. In a subsequent step, association of the 5' domain of the RNA is stabilized by additional interactions with the protein. Thus, CBP2 functions primarily to capture otherwise transient RNA tertiary structures. This simple one-RNA, one-protein system has revealed how the kinetic pathway of RNA folding can direct the assembly of a specific ribonucleoprotein complex. There are parallels to steps in the formation of a much more complex ribonucleoprotein, the 30S ribosomal subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weeks, K M -- Cech, T R -- New York, N.Y. -- Science. 1996 Jan 19;271(5247):345-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, Howard Hughes Medical Institute, University of Colorado, Boulder 80309-0215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8553068" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Cytochrome b Group/genetics ; Fungal Proteins/*metabolism ; *Introns ; Kinetics ; Magnesium/pharmacology ; *Nucleic Acid Conformation ; RNA Splicing ; RNA, Catalytic/chemistry/*metabolism ; RNA, Fungal/chemistry/*metabolism ; Ribonucleoproteins/*metabolism ; *Saccharomyces cerevisiae Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 6
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    Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-02-02
    Description: Hydrogen-deuterium exchange of 39 amide protons of Bacillus amyloliquefaciens ribonuclease (barnase) was analyzed by two-dimensional nuclear magnetic resonance in the presence of micromolar concentrations of the molecular chaperones GroEL and SecB. Both chaperones bound to native barnase under physiological conditions and catalyzed exchange of deeply buried amide protons with solvent. Such exchange required complete unfolding of barnase, which occurred in the complex with the chaperones. Subsequent collapse of unfolded barnase to the exchange-protected folding intermediate was markedly slowed in the presence of GroEL or SecB. Thus, both chaperones have the potential to correct misfolding in proteins by annealing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zahn, R -- Perrett, S -- Stenberg, G -- Fersht, A R -- New York, N.Y. -- Science. 1996 Feb 2;271(5249):642-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Cambridge, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8571125" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/pharmacology ; Amides ; Bacterial Proteins/*metabolism ; Catalysis ; Chaperonin 60/*metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Magnetic Resonance Spectroscopy ; Molecular Chaperones/*metabolism ; Protein Conformation ; *Protein Folding ; Protein Structure, Secondary ; *Protons ; Ribonucleases/*chemistry/metabolism ; Temperature
    Print ISSN: 0036-8075
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  • 7
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    In vitro development of primitive and definitive erythrocytes from different precursors (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: During mouse embryogenesis the production of "primitive" erythrocytes (EryP) precedes the production of "definitive" erythrocytes (EryD) in parallel with the transition of the hematopoietic site from the yolk sac to the fetal liver. On a macrophage colony-stimulating factor-deficient stromal cell line OP9, mouse embryonic stem cells were shown to give rise to EryP and EryD sequentially with a time course similar to that seen in murine ontogeny. Studies of the different growth factor requirements and limiting dilution analysis of precursor frequencies indicate that most EryP and EryD probably developed from different precursors by way of distinct differentiation pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakano, T -- Kodama, H -- Honjo, T -- New York, N.Y. -- Science. 1996 May 3;272(5262):722-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Chemistry, Faculty of Medicine, Kyoto University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614833" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Division ; Cell Line ; Cell Lineage ; Cell Separation ; Cells, Cultured ; Coculture Techniques ; Erythroid Precursor Cells/*cytology ; *Erythropoiesis ; Erythropoietin/pharmacology ; Kinetics ; Mice ; Signal Transduction ; Stem Cell Factor/physiology
    Print ISSN: 0036-8075
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  • 8
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    Thiyl radicals in ribonucleotide reductases (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-01-26
    Description: The ribonucleoside triphosphate reductase (RTPR) from Lactobacillus leichmannii catalyzes adenosylcobalamin (AdoCbl)-dependent nucleotide reduction, as well as exchange of the 5' hydrogens of AdoCbl with solvent. A protein-based thiyl radical is proposed as an intermediate in both of these processes. In the presence of RTPR containing specifically deuterated cysteine residues, the electron paramagnetic resonance (EPR) spectrum of an intermediate in the exchange reaction and the reduction reaction, trapped by rapid freeze quench techniques, exhibits narrowed hyperfine features relative to the corresponding unlabeled RTPR. The spectrum was interpreted to represent a thiyl radical coupled to cob(II)alamin. Another proposed intermediate, 5'-deoxyadenosine, was detected by rapid acid quench techniques. Similarities in mechanism between RTPR and the Escherichia coli ribonucleotide reductase suggest that both enzymes require a thiyl radical for catalysis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Licht, S -- Gerfen, G J -- Stubbe, J -- GM 29595/GM/NIGMS NIH HHS/ -- RR00317/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1996 Jan 26;271(5248):477-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8560260" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Catalysis ; Cobamides/metabolism ; Deoxyadenosines/metabolism ; Electron Spin Resonance Spectroscopy ; *Free Radicals ; Kinetics ; Lactobacillus/enzymology ; Ligands ; Models, Chemical ; Molecular Sequence Data ; Oxidation-Reduction ; Ribonucleotide Reductases/chemistry/*metabolism ; Solvents ; Sulfhydryl Compounds/*metabolism ; Vitamin B 12/analogs & derivatives/metabolism
    Print ISSN: 0036-8075
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  • 9
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    HIV-1 dynamics in vivo: virion clearance rate, infected cell life-span, and viral generation time (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-03-15
    Description: A new mathematical model was used to analyze a detailed set of human immunodeficiency virus-type 1 (HIV-1) viral load data collected from five infected individuals after the administration of a potent inhibitor of HIV-1 protease. Productively infected cells were estimated to have, on average, a life-span of 2.2 days (half-life t 1/2 = 1.6 days), and plasma virions were estimated to have a mean life-span of 0.3 days (t 1/2 = 0.24 days). The estimated average total HIV-1 production was 10.3 x 10(9) virions per day, which is substantially greater than previous minimum estimates. The results also suggest that the minimum duration of the HIV-1 life cycle in vivo is 1.2 days on average, and that the average HIV-1 generation time--defined as the time from release of a virion until it infects another cell and causes the release of a new generation of viral particles--is 2.6 days. These findings on viral dynamics provide not only a kinetic picture of HIV-1 pathogenesis, but also theoretical principles to guide the development of treatment strategies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perelson, A S -- Neumann, A U -- Markowitz, M -- Leonard, J M -- Ho, D D -- AI27742/AI/NIAID NIH HHS/ -- N01 AI45218/AI/NIAID NIH HHS/ -- RR06555/RR/NCRR NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1996 Mar 15;271(5255):1582-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Theoretical Division, Los Alamos National Laboratory, NM 87545, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8599114" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/administration & dosage/therapeutic use ; CD4 Lymphocyte Count ; CD4-Positive T-Lymphocytes/*cytology/*virology ; Cell Survival ; HIV Infections/drug therapy/*virology ; HIV Protease Inhibitors/administration & dosage/therapeutic use ; HIV-1/drug effects/*physiology ; Half-Life ; Humans ; Kinetics ; Models, Biological ; RNA, Viral/blood ; Regression Analysis ; Ritonavir ; Thiazoles/administration & dosage/therapeutic use ; Valine/administration & dosage/analogs & derivatives/therapeutic use ; Viremia ; Virion/drug effects/*physiology ; Virus Replication
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  • 10
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    Direct measurement of coupling between dendritic spines and shafts (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-05-03
    Description: Characterization of the diffusional and electrotonic coupling of spines to the dendritic shaft is crucial to understanding neuronal integration and synaptic plasticity. Two-photon photobleaching and photorelease of fluorescein dextran were used to generate concentration gradients between spines and shafts in rat CA1 pyramidal neurons. Diffusional reequilibration was monitored with two-photon fluorescence imaging. The time course of reequilibration was exponential, with time constants in the range of 20 to 100 milliseconds, demonstrating chemical compartmentalization on such time scales. These values imply that electrical spine neck resistances are unlikely to exceed 150 megohms and more likely range from 4 to 50 megohms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Svoboda, K -- Tank, D W -- Denk, W -- New York, N.Y. -- Science. 1996 May 3;272(5262):716-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological Computation Research Department, Bell Laboratories, Lucent Technologies, Murray Hill, NJ 07974, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8614831" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Dendrites/metabolism/*physiology/ultrastructure ; Dextrans/metabolism ; Diffusion ; Electric Conductivity ; Electric Impedance ; Fluoresceins/metabolism ; Fluorescence ; In Vitro Techniques ; Kinetics ; Microscopy/methods ; Models, Neurological ; Neuronal Plasticity ; Pyramidal Cells/metabolism/*physiology/ultrastructure ; Rats
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