The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
about
A second tubulin binding site on the kinesin-13 motor head domain is important during mitosisDiffusion of myosin V on microtubules: a fine-tuned interaction for which E-hooks are dispensableElectrostatically biased binding of kinesin to microtubulesTubulin polyglutamylation stimulates spastin-mediated microtubule severingIdentification of a strong binding site for kinesin on the microtubule using mutant analysis of tubulin.Myosin Va maneuvers through actin intersections and diffuses along microtubules.Tracking single Kinesin molecules in the cytoplasm of mammalian cells.Myosin V and Kinesin act as tethers to enhance each others' processivity.Diffusive movement of processive kinesin-1 on microtubulesDissection of kinesin's processivity.The nucleotide-binding state of microtubules modulates kinesin processivity and the ability of Tau to inhibit kinesin-mediated transport.A structural perspective on the dynamics of kinesin motors.Structural insights into WHAMM-mediated cytoskeletal coordination during membrane remodeling.A chimeric kinesin-1 head/kinesin-5 tail motor switches between diffusive and processive motilityThe motility of axonemal dynein is regulated by the tubulin code.Neck linker length determines the degree of processivity in kinesin-1 and kinesin-2 motors.Regulation of microtubule motors by tubulin isotypes and post-translational modifications.Kinesin motility is driven by subdomain dynamics.Collective Force Regulation in Anti-parallel Microtubule Gliding by Dimeric Kif15 Kinesin Motors.Kinesin Processivity Is Determined by a Kinetic Race from a Vulnerable One-Head-Bound State.E-hooks provide guidance and a soft landing for the microtubule binding domain of dynein
P2860
Q27308095-78832F62-5CD1-4A1C-B88F-DB85B86D0ED4Q27318271-36842619-0984-4493-A0B7-76F75B66146FQ27320592-593041F0-0C70-43EF-B554-A8AECD945F3CQ28504801-2F306C38-92A0-486D-A319-2FAE3D9B12B6Q30478482-C09014D8-E916-48BE-95FF-AA923115C3BBQ30479183-DFA61237-A6EA-430B-A42F-EF3321019297Q30479511-FA977AFE-8AA1-48E2-924D-9C2F33DAC288Q30481620-1B10A160-30A1-4B88-8AE9-957876128639Q30490327-3369673E-9645-465A-B660-5154C28A00A4Q33412379-37D6B92A-BCBD-46AD-A959-3CE4EA1ACD7FQ35604721-749D7863-16BA-46C9-9872-9F876D7FDDE6Q35815883-BCA992CC-12CD-4A23-B1B0-84A643641B4AQ36289077-6E82820A-6A5F-40FC-AE6E-FA168050BE84Q36554314-FA750466-6A0B-4013-81F5-D68D7A739337Q39532365-99352664-45FB-4C6B-B174-D421A2BA5DD3Q40932336-5546860F-FB79-4623-A03E-880F23F494B8Q42760701-22E1EA4C-CEF8-49B5-8FC9-8F7B00C85B97Q47095034-A2097C9E-0006-48C1-A263-9B2F559DBAE4Q47666060-AF8D9677-B61B-467E-AC36-91404009D40FQ47998090-1CAC7926-6849-4B12-8B04-E61E2D85714BQ58763345-7BBC3D23-BCEC-42EC-B621-FEF52028F987
P2860
The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
@ast
The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
@en
type
label
The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
@ast
The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
@en
prefLabel
The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
@ast
The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
@en
P2860
P1433
P1476
The E-hook of tubulin interacts with kinesin's head to increase processivity and speed.
@en
P2093
Stefan Lakämper
P2860
P304
P356
10.1529/BIOPHYSJ.104.057505
P407
P577
2005-08-12T00:00:00Z