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  • Binding Sites  (35)
  • American Association for the Advancement of Science (AAAS)  (35)
  • American Association for the Advancement of Science
  • Cell Press
  • Springer Nature
  • 2000-2004  (35)
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  • American Association for the Advancement of Science (AAAS)  (35)
  • American Association for the Advancement of Science
  • Cell Press
  • Springer Nature
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  • 2000-2004  (35)
  • 1995-1999
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  • 1
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    A natural product that lowers cholesterol as an antagonist ligand for FXR (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2002-05-04
    Beschreibung: Extracts of the resin of the guggul tree (Commiphora mukul) lower LDL (low-density lipoprotein) cholesterol levels in humans. The plant sterol guggulsterone [4,17(20)-pregnadiene-3,16-dione] is the active agent in this extract. We show that guggulsterone is a highly efficacious antagonist of the farnesoid X receptor (FXR), a nuclear hormone receptor that is activated by bile acids. Guggulsterone treatment decreases hepatic cholesterol in wild-type mice fed a high-cholesterol diet but is not effective in FXR-null mice. Thus, we propose that inhibition of FXR activation is the basis for the cholesterol-lowering activity of guggulsterone. Other natural products with specific biologic effects may modulate the activity of FXR or other relatively promiscuous nuclear hormone receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Urizar, Nancy L -- Liverman, Amy B -- Dodds, D'Nette T -- Silva, Frank Valentin -- Ordentlich, Peter -- Yan, Yingzhuo -- Gonzalez, Frank J -- Heyman, Richard A -- Mangelsdorf, David J -- Moore, David D -- New York, N.Y. -- Science. 2002 May 31;296(5573):1703-6. Epub 2002 May 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Baylor College of Medicine, 1 Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11988537" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Binding Sites ; Caco-2 Cells ; Carrier Proteins/genetics/metabolism ; Cells, Cultured ; Chenodeoxycholic Acid/pharmacology ; Cholesterol/*metabolism ; Cholesterol, Dietary/administration & dosage ; DNA/metabolism ; DNA-Binding Proteins/*antagonists & inhibitors/chemistry/genetics/*metabolism ; Hepatocytes/metabolism ; Histone Acetyltransferases ; Humans ; *Hydroxysteroid Dehydrogenases ; Hypolipidemic Agents/metabolism/*pharmacology ; Ligands ; Liver/metabolism ; *Membrane Glycoproteins ; Mice ; Nuclear Receptor Coactivator 1 ; Pregnenediones/metabolism/*pharmacology ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Receptors, Cytoplasmic and Nuclear/antagonists & inhibitors/genetics/metabolism ; Receptors, Steroid/antagonists & inhibitors/metabolism ; Transcription Factors/*antagonists & inhibitors/chemistry/genetics/*metabolism ; Transcriptional Activation/drug effects ; Transfection ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 2
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    Enzyme dynamics during catalysis (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2002-02-23
    Beschreibung: Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during catalysis at atomic resolution using nuclear magnetic resonance relaxation methods. During catalytic action of the enzyme cyclophilin A, we detect conformational fluctuations of the active site that occur on a time scale of hundreds of microseconds. The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover. The present results, together with available structural data, allow a prediction of the reaction trajectory.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eisenmesser, Elan Zohar -- Bosco, Daryl A -- Akke, Mikael -- Kern, Dorothee -- GM62117/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1520-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Brandeis University, Waltham, MA 02454, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11859194" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Catalysis ; Cyclophilin A/*chemistry/*metabolism ; Hydrogen Bonding ; Isomerism ; Kinetics ; Mathematics ; Models, Molecular ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; Protein Conformation
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 3
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    Structure of a cofactor-deficient nitrogenase MoFe protein (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2002-04-16
    Beschreibung: One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase MoFe protein, into which the cofactor is inserted in the final step of MoFe protein assembly. The MoFe protein folds as a heterotetramer containing two copies each of the homologous alpha and beta subunits. In this structure, one of the three alpha subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A predominantly positively charged funnel is revealed; this funnel is of sufficient size to accommodate insertion of the negatively charged cofactor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schmid, Benedikt -- Ribbe, Markus W -- Einsle, Oliver -- Yoshida, Mika -- Thomas, Leonard M -- Dean, Dennis R -- Rees, Douglas C -- Burgess, Barbara K -- New York, N.Y. -- Science. 2002 Apr 12;296(5566):352-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, Mail Code 147-75CH, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11951047" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Azotobacter vinelandii/*enzymology ; Binding Sites ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Hydrogen Bonding ; Models, Molecular ; Molecular Sequence Data ; Molybdoferredoxin/*chemistry/genetics/*metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Static Electricity ; Surface Properties
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 4
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    Inhibition of hepatitis B virus replication by drug-induced depletion of nucleocapsids (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2003-02-08
    Beschreibung: Chronic hepatitis B virus (HBV) infection is a major cause of liver disease. Only interferon-alpha and the nucleosidic inhibitors of the viral polymerase, 3TC and adefovir, are approved for therapy. However, these therapies are limited by the side effects of interferon and the substantial resistance of the virus to nucleosidic inhibitors. Potent new antiviral compounds suitable for monotherapy or combination therapy are highly desired. We describe non-nucleosidic inhibitors of HBV nucleocapsid maturation that possess in vitro and in vivo antiviral activity. These inhibitors have potential for future therapeutic regimens to combat chronic HBV infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deres, Karl -- Schroder, Claus H -- Paessens, Arnold -- Goldmann, Siegfried -- Hacker, Hans Jorg -- Weber, Olaf -- Kramer, Thomas -- Niewohner, Ulrich -- Pleiss, Ulrich -- Stoltefuss, Jurgen -- Graef, Erwin -- Koletzki, Diana -- Masantschek, Ralf N A -- Reimann, Anja -- Jaeger, Rainer -- Gross, Rainer -- Beckermann, Bernhard -- Schlemmer, Karl-Heinz -- Haebich, Dieter -- Rubsamen-Waigmann, Helga -- New York, N.Y. -- Science. 2003 Feb 7;299(5608):893-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Virology, Chemistry, Isotope Chemistry, Preclinical Pharmakokinetics, Toxicology, Safety Pharmacology, Bayer Research Center, Wuppertal, Germany. karl.deres.kd1@bayer-ag.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12574631" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acetylcysteine/*analogs & derivatives/pharmacology ; Amino Acid Substitution ; Antiviral Agents/chemistry/metabolism/*pharmacology ; Binding Sites ; Capsid/metabolism ; DNA Replication/drug effects ; DNA, Viral/biosynthesis ; Half-Life ; Hepatitis B Virus, Duck/drug effects/metabolism ; Hepatitis B virus/*drug effects/physiology ; Humans ; Mutation ; Nucleocapsid/*metabolism ; Pyridines/chemistry/metabolism/*pharmacology ; Pyrimidines/chemistry/metabolism/*pharmacology ; Recombinant Proteins/metabolism ; Stereoisomerism ; Triazoles/chemistry/metabolism/*pharmacology ; Tumor Cells, Cultured ; Viral Core Proteins/chemistry/genetics/metabolism ; Virus Assembly/drug effects ; Virus Replication/drug effects
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 5
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    The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2003-03-15
    Beschreibung: Enzymes provide enormous rate enhancements, unmatched by any other type of catalyst. The stabilization of high-energy states along the reaction coordinate is the crux of the catalytic power of enzymes. We report the atomic-resolution structure of a high-energy reaction intermediate stabilized in the active site of an enzyme. Crystallization of phosphorylated beta-phosphoglucomutase in the presence of the Mg(II) cofactor and either of the substrates glucose 1-phosphate or glucose 6-phosphate produced crystals of the enzyme-Mg(II)-glucose 1,6-(bis)phosphate complex, which diffracted x-rays to 1.2 and 1.4 angstroms, respectively. The structure reveals a stabilized pentacovalent phosphorane formed in the phosphoryl transfer from the C(1)O of glucose 1,6-(bis)phosphate to the nucleophilic Asp8 carboxylate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lahiri, Sushmita D -- Zhang, Guofeng -- Dunaway-Mariano, Debra -- Allen, Karen N -- GM16099/GM/NIGMS NIH HHS/ -- RR07707/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2003 Mar 28;299(5615):2067-71. Epub 2003 Mar 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, Boston University School of Medicine, Boston, MA 02118-2394, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12637673" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Catalysis ; Chemistry, Physical ; Crystallization ; Crystallography, X-Ray ; Glucose-6-Phosphate/metabolism ; Glucosephosphates/chemistry/metabolism ; Lactococcus lactis/enzymology ; Ligands ; Magnesium/chemistry ; Phosphates/chemistry ; Phosphoglucomutase/*chemistry/*metabolism ; Phosphoranes/chemistry ; Phosphorus/*chemistry ; Phosphorylation ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 6
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    Modulation of heterochromatin protein 1 dynamics in primary Mammalian cells (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2003-02-01
    Beschreibung: Heterochromatin protein 1 (HP1beta), a key component of condensed DNA, is strongly implicated in gene silencing and centromeric cohesion. Heterochromatin has been considered a static structure, stabilizing crucial aspects of nuclear organization and prohibiting access to transcription factors. We demonstrate here, by fluorescence recovery after photobleaching, that a green fluorescent protein-HP1beta fusion protein is highly mobile within both the euchromatin and heterochromatin of ex vivo resting murine T cells. Moreover, T cell activation greatly increased this mobility, indicating that such a process may facilitate (hetero)chromatin remodeling and permit access of epigenetic modifiers and transcription factors to the many genes that are consequently derepressed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Festenstein, Richard -- Pagakis, Stamatis N -- Hiragami, Kyoko -- Lyon, Debbie -- Verreault, Alain -- Sekkali, Belaid -- Kioussis, Dimitris -- New York, N.Y. -- Science. 2003 Jan 31;299(5607):719-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉CSC Gene Control Mechanisms and Disease Group, Division of Medicine, Imperial College School of Medicine, Hammersmith Campus, Du Cane Road, London W12 ONN, UK. r.festenstein@ic.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12560554" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Binding Sites ; Cells, Cultured ; Chromosomal Proteins, Non-Histone/*metabolism ; Dimerization ; Euchromatin/*metabolism ; Fluorescence ; Fluorescence Recovery After Photobleaching ; Heterochromatin/*metabolism ; Histones/metabolism ; Kinetics ; Lymphocyte Activation ; Methylation ; Mice ; Microscopy, Confocal ; T-Lymphocytes/*metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 7
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    A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2003-05-24
    Beschreibung: The capsaicin receptor (TRPV1), a heat-activated ion channel of the pain pathway, is sensitized by phosphatidylinositol-4,5-bisphosphate (PIP2) hydrolysis after phospholipase C activation. We identify a site within the C-terminal domain of TRPV1 that is required for PIP2-mediated inhibition of channel gating. Mutations that weaken PIP2-TRPV1 interaction reduce thresholds for chemical or thermal stimuli, whereas TRPV1 channels in which this region is replaced with a lipid-binding domain from PIP2-activated potassium channels remain inhibited by PIP2. The PIP2-interaction domain therefore serves as a critical determinant of thermal threshold and dynamic sensitivity range, tuning TRPV1, and thus the sensory neuron, to appropriately detect heat under normal or pathophysiological conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prescott, Elizabeth D -- Julius, David -- New York, N.Y. -- Science. 2003 May 23;300(5623):1284-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143-2140, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12764195" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Arsenicals/pharmacology ; Binding Sites ; Capsaicin/metabolism/pharmacology ; Carrier Proteins ; Hot Temperature ; Humans ; Ion Channel Gating ; Membrane Proteins ; Molecular Sequence Data ; Mutation ; Oocytes ; Patch-Clamp Techniques ; Phosphatidylinositol 4,5-Diphosphate/*metabolism ; Phosphorylation ; Potassium Channels, Inwardly Rectifying/chemistry/genetics/metabolism ; Protein Structure, Tertiary ; Rats ; Receptor, Epidermal Growth Factor/metabolism ; Receptor, trkA/metabolism ; Receptors, Drug/*chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Deletion ; Type C Phospholipases/metabolism ; Xenopus
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 8
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    Crystal structure of the potassium channel KirBac1.1 in the closed state (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2003-05-10
    Beschreibung: The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main activation gate and structural elements involved in gating. On the basis of structural evidence presented here, we suggest that gating involves coupling between the intracellular and membrane domains. This further suggests that initiation of gating by membrane or intracellular signals represents different entry points to a common mechanistic pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuo, Anling -- Gulbis, Jacqueline M -- Antcliff, Jennifer F -- Rahman, Tahmina -- Lowe, Edward D -- Zimmer, Jochen -- Cuthbertson, Jonathan -- Ashcroft, Frances M -- Ezaki, Takayuki -- Doyle, Declan A -- New York, N.Y. -- Science. 2003 Jun 20;300(5627):1922-6. Epub 2003 May 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Oxford, Department of Biochemistry, Laboratory of Molecular Biophysics, South Parks Road, Oxford OX1 3QU, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12738871" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Bacterial Proteins/*chemistry/metabolism ; Binding Sites ; Burkholderia pseudomallei/*chemistry ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Hydrophobic and Hydrophilic Interactions ; *Ion Channel Gating ; Ion Transport ; Models, Molecular ; Molecular Sequence Data ; Potassium/metabolism ; Potassium Channels, Inwardly Rectifying/*chemistry/metabolism ; Protein Conformation ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 9
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    Structural basis of gating by the outer membrane transporter FecA (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2002-03-02
    Beschreibung: Siderophore-mediated acquisition systems facilitate iron uptake. We present the crystallographic structure of the integral outer membrane receptor FecA from Escherichia coli with and without ferric citrate at 2.5 and 2.0 angstrom resolution. FecA is composed of three distinct domains: the barrel, plug, and NH2-terminal extension. Binding of ferric citrate triggers a conformational change of the extracellular loops that close the external pocket of FecA. Ligand-induced allosteric transitions are propagated through the outer membrane by the plug domain, signaling the occupancy of the receptor in the periplasm. These data establish the structural basis of gating for receptors dependent on the cytoplasmic membrane protein TonB. By compiling available data for this family of receptors, we propose a mechanism for the energy-dependent transport of siderophores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ferguson, Andrew D -- Chakraborty, Ranjan -- Smith, Barbara S -- Esser, Lothar -- van der Helm, Dick -- Deisenhofer, Johann -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1715-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872840" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adsorption ; Bacterial Outer Membrane Proteins/chemistry/metabolism ; Bacterial Proteins/metabolism ; Binding Sites ; Biological Transport, Active ; Carrier Proteins/*chemistry/*metabolism ; Cell Membrane/metabolism ; Crystallography, X-Ray ; Escherichia coli Proteins/chemistry/metabolism ; Ferric Compounds/*metabolism ; Hydrogen Bonding ; *Ion Channel Gating ; Ligands ; Membrane Proteins/metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; *Receptors, Cell Surface ; Siderophores/*metabolism ; Static Electricity
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 10
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    Closing of the nucleotide pocket of kinesin-family motors upon binding to microtubules (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 2003-05-06
    Beschreibung: We have used adenosine diphosphate analogs containing electron paramagnetic resonance (EPR) spin moieties and EPR spectroscopy to show that the nucleotide-binding site of kinesin-family motors closes when the motor.diphosphate complex binds to microtubules. Structural analyses demonstrate that a domain movement in the switch 1 region at the nucleotide site, homologous to domain movements in the switch 1 region in the G proteins [heterotrimeric guanine nucleotide-binding proteins], explains the EPR data. The switch movement primes the motor both for the free energy-yielding nucleotide hydrolysis reaction and for subsequent conformational changes that are crucial for the generation of force and directed motion along the microtubule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Naber, Nariman -- Minehardt, Todd J -- Rice, Sarah -- Chen, Xiaoru -- Grammer, Jean -- Matuska, Marija -- Vale, Ronald D -- Kollman, Peter A -- Car, Roberto -- Yount, Ralph G -- Cooke, Roger -- Pate, Edward -- AR39643/AR/NIAMS NIH HHS/ -- AR42895/AR/NIAMS NIH HHS/ -- DK05915/DK/NIDDK NIH HHS/ -- GM29072/GM/NIGMS NIH HHS/ -- RR1081/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2003 May 2;300(5620):798-801.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of California, San Francisco, CA 94143, USA. naber@itsa.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12730601" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenine Nucleotides/*metabolism ; Adenosine Diphosphate/analogs & derivatives/metabolism ; Adenosine Triphosphate/analogs & derivatives/metabolism ; Animals ; Binding Sites ; Computer Simulation ; Crystallography, X-Ray ; *Drosophila Proteins ; Drosophila melanogaster ; Electron Spin Resonance Spectroscopy ; Humans ; Hydrogen Bonding ; Hydrolysis ; Kinesin/*chemistry/*metabolism ; Microtubules/*metabolism ; Models, Molecular ; Molecular Motor Proteins/*chemistry/*metabolism ; Molecular Probes/metabolism ; Protein Conformation ; Spin Labels
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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