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  • Protein Structure, Tertiary  (5)
  • American Association for the Advancement of Science (AAAS)  (5)
  • American Association for the Advancement of Science
  • American Chemical Society
  • American Physical Society (APS)
  • 2005-2009  (2)
  • 2000-2004  (3)
  • 1980-1984
  • 1960-1964
  • 1935-1939
  • 1930-1934
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  • American Association for the Advancement of Science (AAAS)  (5)
  • American Association for the Advancement of Science
  • American Chemical Society
  • American Physical Society (APS)
  • Nature Publishing Group (NPG)  (1)
Years
  • 2005-2009  (2)
  • 2000-2004  (3)
  • 1980-1984
  • 1960-1964
  • 1935-1939
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  • 1
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    Parallel single-cell monitoring of receptor-triggered membrane translocation of a calcium-sensing protein module (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-09
    Description: Time courses of translocation of fluorescently conjugated proteins to the plasma membrane were simultaneously measured in thousands of individual rat basophilic leukemia cells. We found that the C2 domain---a calcium-sensing, lipid-binding protein module that is an essential regulator of protein kinase C and numerous other proteins---targeted proteins to the plasma membrane transiently if calcium was released from internal stores, and persistently in response to entry of extracellular calcium across the plasma membrane. The C2 domain translocation time courses of stimulated cells clustered into only two primary modes. Hence, the reversible recruitment of families of signaling proteins from one cellular compartment to another is a rapid bifurcation mechanism for inducing discrete states of cellular signaling networks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teruel, Mary N -- Meyer, Tobias -- CA83229/CA/NCI NIH HHS/ -- GM062144/GM/NIGMS NIH HHS/ -- HG00057/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 8;295(5561):1910-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Stanford University Medical School, 269 Campus Drive, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11884760" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins ; Calcium/*metabolism ; *Calcium Signaling ; Cell Membrane/*metabolism ; Cytosol/metabolism ; Fluorescence ; Fluorescent Dyes ; Isoenzymes/chemistry/*metabolism ; Kinetics ; Luminescent Proteins ; Platelet Activating Factor/pharmacology ; Protein Binding ; Protein Kinase C/chemistry/*metabolism ; Protein Structure, Tertiary ; *Protein Transport ; Rats ; Receptors, Cell Surface/*metabolism ; Recombinant Fusion Proteins/metabolism ; Software ; Thapsigargin/pharmacology ; Transfection ; Tumor Cells, Cultured
    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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    Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-18
    Description: The homodimeric nickel-containing CO dehydrogenase from the anaerobic bacterium Carboxydothermus hydrogenoformans catalyzes the oxidation of CO to CO2. A crystal structure of the reduced enzyme has been solved at 1.6 angstrom resolution. This structure represents the prototype for Ni-containing CO dehydrogenases from anaerobic bacteria and archaea. It contains five metal clusters of which clusters B, B', and a subunit-bridging, surface-exposed cluster D are cubane-type [4Fe-4S] clusters. The active-site clusters C and C' are novel, asymmetric [Ni-4Fe-5S] clusters. Their integral Ni ion, which is the likely site of CO oxidation, is coordinated by four sulfur ligands with square planar geometry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dobbek, H -- Svetlitchnyi, V -- Gremer, L -- Huber, R -- Meyer, O -- New York, N.Y. -- Science. 2001 Aug 17;293(5533):1281-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152 Martinsried, Germany. dobbek@biochem.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11509720" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Oxidoreductases/*chemistry/*metabolism ; Bacteria, Anaerobic/*enzymology ; Binding Sites ; Carbon Dioxide/metabolism ; Carbon Monoxide/*metabolism ; Catalysis ; Chemistry, Physical ; Crystallization ; Crystallography, X-Ray ; Dimerization ; Electron Transport ; Hydrogen Bonding ; Iron/*chemistry/metabolism ; Ligands ; Models, Molecular ; Multienzyme Complexes/*chemistry/*metabolism ; Nickel/*chemistry/metabolism ; Oxidation-Reduction ; Peptococcaceae/*enzymology ; Physicochemical Phenomena ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits ; Sulfur/*chemistry/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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  • 3
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    Neuroscience. SPARring with spines (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyer, Guido -- Brose, Nils -- New York, N.Y. -- Science. 2003 Nov 21;302(5649):1341-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Neuroscience, Max Planck Institute for Experimental Medicine, D-37075 Gottingen, Germany. gmeyer@em.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14631024" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COS Cells ; Cell Cycle ; Cells, Cultured ; Cysteine Endopeptidases/metabolism ; Dendrites/*physiology/ultrastructure ; Down-Regulation ; GTPase-Activating Proteins/chemistry/*metabolism ; Hippocampus/cytology/metabolism ; Multienzyme Complexes/metabolism ; Nerve Tissue Proteins/metabolism ; Neuronal Plasticity/*physiology ; Phosphorylation ; Proteasome Endopeptidase Complex ; Protein Kinases/*metabolism ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases ; Recombinant Proteins/metabolism ; Signal Transduction ; Synapses/*physiology ; Two-Hybrid System Techniques ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/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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  • 4
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    The crystal structure of [Fe]-hydrogenase reveals the geometry of the active site (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-07-26
    Description: Biological formation and consumption of molecular hydrogen (H2) are catalyzed by hydrogenases, of which three phylogenetically unrelated types are known: [NiFe]-hydrogenases, [FeFe]-hydrogenases, and [Fe]-hydrogenase. We present a crystal structure of [Fe]-hydrogenase at 1.75 angstrom resolution, showing a mononuclear iron coordinated by the sulfur of cysteine 176, two carbon monoxide (CO) molecules, and the sp2-hybridized nitrogen of a 2-pyridinol compound with back-bonding properties similar to those of cyanide. The three-dimensional arrangement of the ligands is similar to that of thiolate, CO, and cyanide ligated to the low-spin iron in binuclear [NiFe]- and [FeFe]-hydrogenases, although the enzymes have evolved independently and the CO and cyanide ligands are not found in any other metalloenzyme. The related iron ligation pattern of hydrogenases exemplifies convergent evolution and presumably plays an essential role in H2 activation. This finding may stimulate the ongoing synthesis of catalysts that could substitute for platinum in applications such as fuel cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shima, Seigo -- Pilak, Oliver -- Vogt, Sonja -- Schick, Michael -- Stagni, Marco S -- Meyer-Klaucke, Wolfram -- Warkentin, Eberhard -- Thauer, Rudolf K -- Ermler, Ulrich -- New York, N.Y. -- Science. 2008 Jul 25;321(5888):572-5. doi: 10.1126/science.1158978.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Terrestrische Mikrobiologie and Laboratorium fur Mikrobiologie, Fachbereich Biologie, Philipps-Universitat Marburg, Karl-von-Frisch-Strasse, D-35043 Marburg, Germany. shima@mpi-marburg.mpg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18653896" target="_blank"〉PubMed〈/a〉
    Keywords: Apoenzymes/chemistry ; Binding Sites ; Carbon Monoxide/chemistry ; Catalytic Domain ; Coenzymes/chemistry ; Crystallography, X-Ray ; Cyanides/chemistry/metabolism ; Dimerization ; Evolution, Molecular ; Holoenzymes/chemistry ; Hydrogen/chemistry/*metabolism ; Hydrogenase/*chemistry/isolation & purification/metabolism ; Iron/chemistry ; Ligands ; Methane/biosynthesis ; Methanococcales/*enzymology ; Models, Molecular ; Oxidation-Reduction ; Protein Structure, Secondary ; Protein Structure, Tertiary
    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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    Conformational switch of syntaxin-1 controls synaptic vesicle fusion (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-08-16
    Description: During synaptic vesicle fusion, the soluble N-ethylmaleimide-sensitive factor-attachment protein receptor (SNARE) protein syntaxin-1 exhibits two conformations that both bind to Munc18-1: a "closed" conformation outside the SNARE complex and an "open" conformation in the SNARE complex. Although SNARE complexes containing open syntaxin-1 and Munc18-1 are essential for exocytosis, the function of closed syntaxin-1 is unknown. We generated knockin/knockout mice that expressed only open syntaxin-1B. Syntaxin-1B(Open) mice were viable but succumbed to generalized seizures at 2 to 3 months of age. Binding of Munc18-1 to syntaxin-1 was impaired in syntaxin-1B(Open) synapses, and the size of the readily releasable vesicle pool was decreased; however, the rate of synaptic vesicle fusion was dramatically enhanced. Thus, the closed conformation of syntaxin-1 gates the initiation of the synaptic vesicle fusion reaction, which is then mediated by SNARE-complex/Munc18-1 assemblies.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3235364/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3235364/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gerber, Stefan H -- Rah, Jong-Cheol -- Min, Sang-Won -- Liu, Xinran -- de Wit, Heidi -- Dulubova, Irina -- Meyer, Alexander C -- Rizo, Josep -- Arancillo, Marife -- Hammer, Robert E -- Verhage, Matthijs -- Rosenmund, Christian -- Sudhof, Thomas C -- NS051262/NS/NINDS NIH HHS/ -- NS37200/NS/NINDS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Sep 12;321(5895):1507-10. doi: 10.1126/science.1163174. Epub 2008 Aug 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390-9111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18703708" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Epilepsy/etiology ; Excitatory Postsynaptic Potentials ; Membrane Fusion ; Mice ; Mice, Knockout ; Munc18 Proteins/metabolism ; Mutation ; Protein Conformation ; Protein Structure, Tertiary ; SNARE Proteins/metabolism ; Sucrose/metabolism ; Synapses/physiology ; Synaptic Vesicles/*physiology/ultrastructure ; Syntaxin 1/*chemistry/genetics/*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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