About: Myosin V: regulation by calcium, calmodulin, and the tail domain

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description	article scientifique publié en 2004 (fr) artículu científicu espublizáu en 2004 (ast) vědecký článek publikovaný v roce 2004 (cs) 2004 թվականի մարտին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в березні 2004 (uk) 2004 թուականի Մարտին հրատարակուած գիտական յօդուած (hyw) vedecký článok (publikovaný 2004/03/15) (sk) wetenschappelijk artikel (gepubliceerd op 2004/03/15) (nl) مقالة علمية (نشرت في 15-3-2004) (ar) im März 2004 veröffentlichter wissenschaftlicher Artikel (de) scientific journal article (en)
publication date	wds:Q28588566-2CDCD3F4-635B-46A6-8F0A-146280945713
publication date	2004-03-15 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28588566-59244C85-16C0-4382-91B3-F5368A5B6484
language of work or name	English
cites work	wds:Q28588566-0A556EE6-CFFF-440C-AA1E-4E71A2F6A92B wds:Q28588566-1BA7E40E-6BC6-441E-9310-155C922B0FB6 wds:Q28588566-2980C63F-2F80-4E5B-A36B-9DD64E325098 wds:Q28588566-2C32806D-8160-4E95-97DC-12E7C6C5AF50 wds:Q28588566-3E3B530D-1129-4131-A8D6-434887B3F911 wds:Q28588566-42E67342-7E92-451E-94B6-D25677868B97 wds:Q28588566-45C06504-F7CF-47A0-A640-219BC1326A47 wds:Q28588566-46D65505-1D8C-4EE8-B680-183790B38F7C wds:Q28588566-49DD3A85-BFE4-44AC-BA52-D74265C62B68 wds:Q28588566-4CA88FB7-6B47-40DB-8DBD-880E5FA6EB81 wds:Q28588566-4E7D7C79-00CA-41DF-80CE-DCD98853016B wds:Q28588566-53262BF4-7FF5-4870-A142-8C0052085355 wds:Q28588566-5F9E9266-9E2E-418E-97EF-FED9131A6458 wds:Q28588566-60828C9D-049F-42DE-B401-7EF99BB10E6F wds:Q28588566-63EBF814-6FE4-4279-9B38-0C7453C1F09C wds:Q28588566-72B7841C-27D4-48BB-ABA4-B1A928B05FBE wds:Q28588566-74A89BDF-9B5D-4A01-9E4F-F469F8EB618D wds:Q28588566-851907E2-C2A4-4091-BE5E-605D52F7057D wds:Q28588566-87ACDED9-22E8-4DC2-91E2-7CA3A3F78FE8 wds:Q28588566-8E1B45DB-0EB6-40A6-8514-CD0F093ABB0F wds:Q28588566-98041636-F2BF-4F2D-84E2-61B0F9C58745 wds:Q28588566-9B0D6F99-3A19-4F4F-8DCA-D3C61CD08E0C wds:Q28588566-9B5E7F05-7731-47C1-9FCA-F807F645476D wds:Q28588566-A5343841-7879-4E54-AD45-B05CF83222A9 wds:Q28588566-AA5BA6B9-B2CA-46D2-8783-2B8F37186E40 wds:Q28588566-AB9A2C7E-55F0-49A7-A484-D75A4FFFC9BD wds:Q28588566-B79EBFD6-9C23-41C3-8159-796AEF8EE412 wds:Q28588566-C460DE59-0696-47F1-947F-E64790E1B777 wds:Q28588566-C5CFE5CA-CF25-48E8-BBAF-9A59AEB5BE2E wds:Q28588566-C60901EB-7AAE-49CE-A9EF-A2F16CEC401E wds:Q28588566-C6EB1E4F-85C9-4989-B109-AC8E056B3020 wds:Q28588566-C71775E7-678C-4D9F-845E-709FA4DB1003 wds:Q28588566-C8F3D735-317B-4584-994C-65C2879F949D wds:Q28588566-D0F556B9-25C4-422D-8A9C-EACD7CBEC6D5 wds:Q28588566-DB47F4AB-9A34-4823-9514-C7D67A5C8D95 wds:Q28588566-E417B8E6-E80E-4F28-A508-78F9026741C1 wds:Q28588566-E7DFFC62-3F38-4D16-9BD4-7DB509ADFE95 wds:Q28588566-EFE889BE-80FB-41DF-8CF1-44DD17A49297 wds:Q28588566-F5494399-AB82-47CE-A349-BDE5A00854E8 wds:Q28588566-F882E5AA-4796-4F6E-AE3C-ECAF6FE760B5
cites work	Blocking the Ca2+-induced conformational transitions in calmodulin with disulfide bonds Effect of ADP and ionic strength on the kinetic and motile properties of recombinant mouse myosin V Kinetic characterization of a monomeric unconventional myosin V construct. Computer-assisted tracking of actin filament motility Class V myosins. Myosin VI is a processive motor with a large step size Role of the lever arm in the processive stepping of myosin V. Identification of an organelle receptor for myosin-Va Molecular genetic dissection of mouse unconventional myosin-VA: tail region mutations The light chain composition of chicken brain myosin-Va: calmodulin, myosin-II essential light chains, and 8-kDa dynein light chain/PIN. Myosin VI is an actin-based motor that moves backwards Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains Use of site-directed mutations in the individual Ca2(+)-binding sites of calmodulin to examine Ca2(+)-induced conformational changes. Brain myosin-V is a two-headed unconventional myosin with motor activity High affinity binding of brain myosin-Va to F-actin induced by calcium in the presence of ATP. Regulation of melanosome movement in the cell cycle by reversible association with myosin V. Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions Regulated conformation of myosin V. Cell cycle regulation of myosin-V by calcium/calmodulin-dependent protein kinase II. Regulation of smooth muscle myosin Myosin-V is a processive actin-based motor A method for directly fitting the time derivative of sedimentation velocity data and an alternative algorithm for calculating sedimentation coefficient distribution functions. Kinesin's tail domain is an inhibitory regulator of the motor domain. Kinesin's IAK tail domain inhibits initial microtubule-stimulated ADP release. Formation of the compact confomer of kinesin requires a COOH-terminal heavy chain domain and inhibits microtubule-stimulated ATPase activity Intracellular coupling via limiting calmodulin A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2 High affinity Ca2+ binding sites of calmodulin are critical for the regulation of myosin Ibeta motor function. ADP inhibition of myosin V ATPase activity Myosin-V stepping kinetics: a molecular model for processivity Calcium functionally uncouples the heads of myosin VI. Ca(2+)-dependent regulation of the motor activity of myosin V. Enzymatic characterization and functional domain mapping of brain myosin-V. Myosin V exhibits a high duty cycle and large unitary displacement Analysis of the chicken fast myosin heavy chain family. Localization of isoform-specific antibody epitopes and regions of divergence Neonatal and adult myosin heavy chains form homodimers during avian skeletal muscle development Neck length and processivity of myosin V. A bent monomeric conformation of myosin from smooth muscle Myosin-Va proteolysis by Ca2+/calpain in depolarized nerve endings from rat brain
author name string	wds:Q28588566-643DE1AB-B6FD-4F75-8DD4-84247F53318C wds:Q28588566-6A36F35D-315B-4E46-AE47-06CD9E65F462 wds:Q28588566-E0AA77C9-360D-4EE1-9B65-E7ADBD9D3D3B
OpenCitations bibliographic resource ID	wds:Q28588566-3EC1362F-903C-43B8-AC62-C5F6ED6E4498

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