| Communicative interaction of myosins along an actin filament in the presence of ATP. | |
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MedLine Citation:
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PMID: 8679926 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Myosin molecules contacting an actin filament in the presence of ATP were found to regulate the filamental fluctuations due to ATP hydrolysis in a communicative manner along the filament. As an evidence of the occurrence of the communication, ATP-activated fluctuating displacements of the filament in the direction perpendicular to its longitudinal axis were identified to propagate at a finite velocity not less than about 0.2 micron/s unidirectionally along the filament. |
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Authors:
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K Hatori; H Honda; K Matsuno |
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Publication Detail:
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Type: Comparative Study; Journal Article |
Journal Detail:
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Title: Biophysical chemistry Volume: 60 ISSN: 0301-4622 ISO Abbreviation: Biophys. Chem. Publication Date: 1996 Jun |
Date Detail:
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Created Date: 1996-08-21 Completed Date: 1996-08-21 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 0403171 Medline TA: Biophys Chem Country: NETHERLANDS |
Other Details:
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Languages: eng Pagination: 149-52 Citation Subset: IM |
Affiliation:
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Department of BioEngineering, Nagaoka University of Technology, Japan. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Actins
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metabolism* Adenosine Triphosphatases / metabolism Adenosine Triphosphate / metabolism* Microfilaments / enzymology, metabolism* Myosins / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Actins; 56-65-5/Adenosine Triphosphate; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.4.1/Myosins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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