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  • 1
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    Differential regulation of dynein and kinesin motor proteins by tau (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-01-19
    Description: Dynein and kinesin motor proteins transport cellular cargoes toward opposite ends of microtubule tracks. In neurons, microtubules are abundantly decorated with microtubule-associated proteins (MAPs) such as tau. Motor proteins thus encounter MAPs frequently along their path. To determine the effects of tau on dynein and kinesin motility, we conducted single-molecule studies of motor proteins moving along tau-decorated microtubules. Dynein tended to reverse direction, whereas kinesin tended to detach at patches of bound tau. Kinesin was inhibited at about a tenth of the tau concentration that inhibited dynein, and the microtubule-binding domain of tau was sufficient to inhibit motor activity. The differential modulation of dynein and kinesin motility suggests that MAPs can spatially regulate the balance of microtubule-dependent axonal transport.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2866193/" 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/PMC2866193/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dixit, Ram -- Ross, Jennifer L -- Goldman, Yale E -- Holzbaur, Erika L F -- GM-48661/GM/NIGMS NIH HHS/ -- P01 AR051174/AR/NIAMS NIH HHS/ -- P01 AR051174-050002/AR/NIAMS NIH HHS/ -- P01-AR-051174/AR/NIAMS NIH HHS/ -- R01 GM048661/GM/NIGMS NIH HHS/ -- R01 GM048661-16/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2008 Feb 22;319(5866):1086-9. doi: 10.1126/science.1152993. Epub 2008 Jan 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18202255" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/metabolism ; Animals ; Axonal Transport ; Dyneins/chemistry/*metabolism ; Kinesin/chemistry/*metabolism ; Mice ; Mice, Transgenic ; Microscopy, Fluorescence ; Microtubules/*metabolism ; Models, Neurological ; Neurons/metabolism/physiology ; Protein Binding ; Protein Isoforms/metabolism ; Recombinant Fusion Proteins/metabolism ; tau Proteins/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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  • 2
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    Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-07
    Description: Myosin V is a dimeric molecular motor that moves processively on actin, with the center of mass moving approximately 37 nanometers for each adenosine triphosphate hydrolyzed. We have labeled myosin V with a single fluorophore at different positions in the light-chain domain and measured the step size with a standard deviation of 〈1.5 nanometers, with 0.5-second temporal resolution, and observation times of minutes. The step size alternates between 37 + 2x nm and 37 - 2x, where x is the distance along the direction of motion between the dye and the midpoint between the two heads. These results strongly support a hand-over-hand model of motility, not an inchworm model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yildiz, Ahmet -- Forkey, Joseph N -- McKinney, Sean A -- Ha, Taekjip -- Goldman, Yale E -- Selvin, Paul R -- AR26846/AR/NIAMS NIH HHS/ -- AR44420/AR/NIAMS NIH HHS/ -- GM65367/GM/NIGMS NIH HHS/ -- PHS 5 T32 GM08276/PH/PHPPO CDC HHS/ -- R01 GM065367/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2061-5. Epub 2003 Jun 5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Biophysics and Computational Biology, University of Illinois, Urbana-Champaign, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12791999" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*metabolism/ultrastructure ; Actins/metabolism ; Adenosine Triphosphate/metabolism ; Binding Sites ; Calmodulin ; Carbocyanines/metabolism ; Catalytic Domain ; Dna ; Fluorescence ; Fluorescent Dyes/metabolism ; Kinetics ; Mathematics ; Microscopy, Fluorescence ; *Models, Biological ; Molecular Motor Proteins/chemistry/*metabolism ; Myosin Light Chains/chemistry/metabolism ; Myosin Type V/chemistry/*metabolism ; Protein Structure, Tertiary ; Rhodamines/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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    Andrew Fielding Huxley (1917-2012) (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-06-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldman, Yale E -- Franzini-Armstrong, Clara -- Armstrong, Clay M -- England -- Nature. 2012 Jun 27;486(7404):474. doi: 10.1038/486474a.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA. goldmany@yahoo.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22739307" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/physiology ; Biophysics/*history ; Electric Conductivity ; Great Britain ; History, 20th Century ; Muscle Contraction/physiology ; Neurophysiology/*history ; Nobel Prize
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 4
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    Phosphate release and force generation in skeletal muscle fibers (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-06-14
    Description: Rapid laser pulse-induced photolysis of an adenosine triphosphate precursor in muscle fibers abruptly initiated cycling of the cross-bridges. The accompanying changes in tension and stiffness were related to elementary mechanochemical events of the energy-transducing mechanism. When inorganic phosphate was present at millimolar concentrations during liberation of adenosine triphosphate in the absence of calcium, relaxation was accelerated. Steady active tension in the presence of calcium was decreased but the approach to final tension was more rapid. These results suggest that, during energy transduction, formation of the dominant force-generating cross-bridge state is coupled to release of inorganic phosphate in a reaction that is readily reversible.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hibberd, M G -- Dantzig, J A -- Trentham, D R -- Goldman, Y E -- AM00745/AM/NIADDK NIH HHS/ -- HL15835/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jun 14;228(4705):1317-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3159090" target="_blank"〉PubMed〈/a〉
    Keywords: Actomyosin/*metabolism ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/metabolism ; Animals ; Calcium/physiology ; In Vitro Techniques ; *Muscle Contraction ; Muscles/*physiology ; Phosphates/*metabolism ; Rabbits ; 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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  • 5
    Electronic Resource
    Electronic Resource
    Holmium laser temperature-jump apparatus for kinetic studies of muscle contraction (1989)
    [S.l.] : American Institute of Physics (AIP)
    Review of Scientific Instruments 60 (1989), S. 231-236 
    Details
    ISSN: 1089-7623
    Source: AIP Digital Archive
    Topics: Physics , Electrical Engineering, Measurement and Control Technology
    Notes: A solid-state holmium3+ –YLF laser-based temperature-jump apparatus has been designed, constructed, and used to produce sudden 2–10 °C temperature increases in aqueous media. This temperature jump technique can be used to perturb biological macromolecular assemblies, such as single skeletal muscle fibers, without their disruption and sufficiently rapidly to elicit biologically relevant kinetic information.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.1140414
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  • 6
    Electronic Resource
    Electronic Resource
    Special Topic: Molecular Mechanism of Muscle Contraction (1987)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Physiology 49 (1987), S. 629-636 
    Details
    ISSN: 0066-4278
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ph.49.030187.003213
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  • 7
    Electronic Resource
    Electronic Resource
    Kinetics of the Actomyosin ATPase in Muscle Fibers (1987)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Physiology 49 (1987), S. 637-654 
    Details
    ISSN: 0066-4278
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Medicine , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ph.49.030187.003225
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  • 8
    Electronic Resource
    Electronic Resource
    Dynamic measurement of myosin light-chain-domain tilt and twist in muscle contraction (1999)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 400 (1999), S. 425-430 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A new method is described for measuring motions of protein domains in their native environment on the physiological timescale. Pairs of cysteines are introduced into the domain at sites chosen from its static structure and are crosslinked by a bifunctional rhodamine. Domain orientation in a ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/22704
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  • 9
    Electronic Resource
    Electronic Resource
    Kinetics of smooth and skeletal muscle activation by laser pulse photolysis of caged inositol 1,4,5-trisphosphate (1987)
    [s.l.] : Nature Publishing Group
    Nature 327 (1987), S. 249-252 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Skeletal-muscle contraction is activated by Ca2* released from the sarcoplasmic reticulum (SR) following electrical depolarization of the cell-surface membrane6. Smooth-muscle contraction is generally thought to be activated by myosin light-chain phos-phorylation7 that in turn depends on the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/327249a0
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  • 10
    Electronic Resource
    Electronic Resource
    Relaxation of muscle fibres by photolysis of caged ATP (1982)
    [s.l.] : Nature Publishing Group
    Nature 300 (1982), S. 701-705 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A novel method has been developed for studying the reaction kinetics of the force-generating mechanism in muscle. Inert photolabile precursors of ATP or ADP are incorporated into muscle fibres having their surface membrane barrier removed. The nucleotide is then rapidly liberated by laser pulse ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/300701a0
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