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  • Articles  (4)
  • American Association for the Advancement of Science (AAAS)  (4)
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  • Articles  (4)
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  • 1
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    Physical properties determining self-organization of motors and microtubules (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-12
    Description: In eukaryotic cells, microtubules and their associated motor proteins can be organized into various large-scale patterns. Using a simplified experimental system combined with computer simulations, we examined how the concentrations and kinetic parameters of the motors contribute to their collective behavior. We observed self-organization of generic steady-state structures such as asters, vortices, and a network of interconnected poles. We identified parameter combinations that determine the generation of each of these structures. In general, this approach may become useful for correlating the morphogenetic phenomena taking place in a biological system with the biophysical characteristics of its constituents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Surrey, T -- Nedelec, F -- Leibler, S -- Karsenti, E -- New York, N.Y. -- Science. 2001 May 11;292(5519):1167-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Biophysics Program, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11349149" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Antibodies ; Biopolymers/chemistry/metabolism ; *Computer Simulation ; *Drosophila Proteins ; Guanosine Triphosphate/metabolism ; Kinesin/chemistry/metabolism ; Kinetics ; Macromolecular Substances ; Microtubules/*chemistry/drug effects/*metabolism ; Models, Molecular ; Molecular Motor Proteins/*chemistry/*metabolism ; Paclitaxel/pharmacology ; Protein Structure, Quaternary/drug effects ; Tubulin/chemistry/metabolism ; Viscosity
    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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    A kinesin-like motor inhibits microtubule dynamic instability (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-03-06
    Description: The motility of molecular motors and the dynamic instability of microtubules are key dynamic processes for mitotic spindle assembly and function. We report here that one of the mitotic kinesins that localizes to chromosomes, Xklp1 from Xenopus laevis, could inhibit microtubule growth and shrinkage. This effect appeared to be mediated by a structural change in the microtubule lattice. We also found that Xklp1 could act as a fast, nonprocessive, plus end-directed molecular motor. The integration of the two properties, motility and inhibition of microtubule dynamics, in one molecule emphasizes the versatile properties of kinesin family members.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bringmann, Henrik -- Skiniotis, Georgios -- Spilker, Annina -- Kandels-Lewis, Stefanie -- Vernos, Isabelle -- Surrey, Thomas -- New York, N.Y. -- Science. 2004 Mar 5;303(5663):1519-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Biophysics Programme, European Molecular Biology Laboratory, Meyerhofstrabetae 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15001780" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Adenylyl Imidodiphosphate/metabolism/pharmacology ; Animals ; Centrosome/metabolism ; Chromosomes/metabolism ; Cryoelectron Microscopy ; Dimerization ; Kinetics ; Microtubule-Associated Proteins/chemistry/genetics/*metabolism ; Microtubules/drug effects/metabolism/*physiology/ultrastructure ; Molecular Motor Proteins/*metabolism ; Paclitaxel/pharmacology ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Tubulin/metabolism ; Xenopus Proteins/chemistry/genetics/*metabolism ; Xenopus laevis
    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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    Directional switching of the kinesin Cin8 through motor coupling (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-02-26
    Description: Kinesin motor proteins are thought to move exclusively in either one or the other direction along microtubules. Proteins of the kinesin-5 family are tetrameric microtubule cross-linking motors important for cell division and differentiation in various organisms. Kinesin-5 motors are considered to be plus-end-directed. However, here we found that purified kinesin-5 Cin8 from budding yeast could behave as a bidirectional kinesin. On individual microtubules, single Cin8 motors were minus-end-directed motors, whereas they switched to plus-end-directed motility when working in a team of motors sliding antiparallel microtubules apart. This kinesin can thus change directionality of movement depending on whether it acts alone or in an ensemble.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Roostalu, Johanna -- Hentrich, Christian -- Bieling, Peter -- Telley, Ivo A -- Schiebel, Elmar -- Surrey, Thomas -- New York, N.Y. -- Science. 2011 Apr 1;332(6025):94-9. doi: 10.1126/science.1199945. Epub 2011 Feb 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Zentrum fur Molekulare Biologie der Universitat Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282, Heidelberg 69120, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21350123" target="_blank"〉PubMed〈/a〉
    Keywords: Kinesin/*physiology ; Microtubules/physiology ; Molecular Motor Proteins/*physiology ; Recombinant Proteins ; Saccharomyces cerevisiae/physiology ; Saccharomyces cerevisiae Proteins/*physiology
    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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  • 4
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    Hemoglobin I mutation encoded at both alpha-globin loci on the same chromosome: concerted evolution in the human genome (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-12-21
    Description: Genetic analysis of an individual expressing an unexpectedly high level of hemoglobin I, an alpha-globin structural mutant, reveals that the mutation is present at both the alpha 1- and the alpha 2-globin gene loci. Kindred analysis confirms that the two affected genes are located in cis. The most likely explanation for this finding is that a recent conversion event occurred within the human alpha-globin gene cluster.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liebhaber, S A -- Rappaport, E F -- Cash, F E -- Ballas, S K -- Schwartz, E -- Surrey, S -- AM 16691/AM/NIADDK NIH HHS/ -- AM 33975/AM/NIADDK NIH HHS/ -- HL 28157/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1984 Dec 21;226(4681):1449-51.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6505702" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Genes ; Globins/*genetics ; *Hemoglobins ; Hemoglobins, Abnormal/*genetics ; Humans ; *Mutation ; Nucleic Acid Hybridization ; Recombination, Genetic
    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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