Single-molecule stepping and structural dynamics of myosin X.
about
Myosin-X and diseaseActin structure-dependent stepping of myosin 5a and 10 during processive movementDirect Microtubule-Binding by Myosin-10 Orients Centrosomes toward Retraction Fibers and Subcortical Actin Clouds.The myosin X motor is optimized for movement on actin bundles.Antiparallel coiled-coil-mediated dimerization of myosin XMouse myosin-19 is a plus-end-directed, high-duty ratio molecular motorLever-arm mechanics of processive myosinsSingle molecule optical measurements of orientation and rotations of biological macromoleculesMyosin-X functions in polarized epithelial cells.Differential regulation of myosin X movements by its cargos, DCC and neogenin.A Combination of Diffusion and Active Translocation Localizes Myosin 10 to the Filopodial TipActivated full-length myosin-X moves processively on filopodia with large steps toward diverse two-dimensional directionsMyosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load.The stepping pattern of myosin X is adapted for processive motility on bundled actin.Use of fluorescent techniques to study the in vitro movement of myosinsFuture challenges in single-molecule fluorescence and laser trap approaches to studies of molecular motors.Myosin-X: a MyTH-FERM myosin at the tips of filopodiaMyosin X regulates neuronal radial migration through interacting with N-cadherinMyosin X dimerization and its impact on cellular functions.Myosin VI has a one track mind versus myosin Va when moving on actin bundles or at an intersection.Tropomyosin is essential for processive movement of a class V myosin from budding yeastVarious Themes of Myosin Regulation.Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection.Myosin X and its motorless isoform differentially modulate dendritic spine development by regulating trafficking and retention of vasodilator-stimulated phosphoprotein.Calmodulin in complex with the first IQ motif of myosin-5a functions as an intact calcium sensor.Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.Fluorescence anisotropy and resonance energy transfer: powerful tools for measuring real time protein dynamics in a physiological environment.Principles of unconventional myosin function and targeting.Role of water in protein folding, oligomerization, amyloidosis and miniprotein.Structural Basis of Cargo Recognition by Unconventional Myosins in Cellular Trafficking.Kinetic Adaptations of Myosins for Their Diverse Cellular FunctionsMechanics and Activation of Unconventional Myosins.Deconvolution of Camera Instrument Response Functions.MyTH4-FERM myosins in the assembly and maintenance of actin-based protrusions.Three-Dimensional Localization of Single Molecules for Super-Resolution Imaging and Single-Particle Tracking.Mesoscopic analysis of motion and conformation of cross-bridges.Myosin tails and single α-helical domains.The path to visualization of walking myosin V by high-speed atomic force microscopy.Tracking single particles and elongated filaments with nanometer precision.Robustness of the rotary catalysis mechanism of F1-ATPase.
P2860
Q26825835-C874372C-DBC9-4CDB-A80C-B8E1967250F6Q27306218-22446AEC-D837-4C8D-9F77-8269A1813041Q27314555-5E097DB0-8E76-4810-8C16-A231AED5F5E9Q27333243-D261E8BC-A673-461D-8CE4-81E89F8551BBQ27673659-7ABE430F-48BE-4469-B08A-050AD1B31074Q28585827-BC3182E3-4325-4800-8841-E26695AFBBB5Q28743071-90CEE0CC-360A-481C-9AC3-8D0B3DA00FC5Q30398533-FFFB5D51-AFB5-4A6E-BE56-1CF4BC2E2C69Q30513859-67EB4910-C4AB-446E-B0E4-9B2FF18D021AQ30514794-4F0CF0D0-9C5F-407A-A03C-9A09C3627A80Q30826156-00457449-E7B0-422D-8ADE-C265AE1E51BEQ30841590-CDCBF476-6CE8-42B4-8CBF-8D973E6A81FBQ33607079-97070BA4-938A-4398-8C24-76163BFA6E63Q34134758-46ECD159-6117-49FE-AF23-28A18DDE44F7Q34262470-3C6660F7-C47D-49A9-9171-986F45FD2EC8Q34511756-CABC6714-FF39-4294-9A0F-B4115002AA3DQ35576442-A1E74269-C593-4838-915B-A428D1D1CFCAQ35964174-D4E451A2-8BA9-4605-8354-DA0C5588336FQ36378456-ADF11D21-DAEC-46E8-98C6-55E074081D5FQ36542334-878C18AC-E5F6-47EF-B0B8-F6FDE57F1638Q36604050-825D6223-E118-45CB-8D0E-0332E1CEC38AQ36880297-466ED9BB-2A42-469D-BD8B-766F0BF97EABQ37000324-4D8F207A-0A01-4539-B1D6-AFD1ACB93B93Q37226406-C1A93CAA-D019-46A2-98AE-8690F3D38C9EQ37323208-3E209CF7-D472-454E-88A9-C56B9826DA22Q37578155-35D95DBD-5756-4ABB-A4EE-AA2A190CD862Q37802709-F0883EEC-98C5-4852-8B76-1D5B795C3C1FQ37884613-3DEA679E-6324-46D0-A80D-6D222E92AA3BQ38237445-6F5C6027-D0C9-4409-A939-1933FB033E72Q38722191-D4FC599E-28E9-4C85-96C7-FF81B39D0DDEQ38756098-D2B28BA7-0492-4233-92CB-A0BE539EC27CQ38803208-65865AEA-7B44-4CC4-B188-8152B93A1648Q38868853-1EDE582C-B921-4777-8787-C4F41EFA67BCQ39005661-C5D2EEDB-7A19-4D04-8844-E3F580337388Q39115388-B8C763C3-E5B9-4249-B17B-5064D7914254Q39310881-C03EF883-8860-4575-BAE7-A2BF2EC5DF5CQ41530183-C3F548AE-8048-4606-9ABB-1D54BB43EEFAQ41825148-BB851D6A-585E-4FCB-904D-DE1D083D9E5FQ41893028-CF341EE2-69C4-48B8-9371-5FE6F52EA8EEQ41893427-67CE7E6F-D076-4078-9617-736143E4D049
P2860
Single-molecule stepping and structural dynamics of myosin X.
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Single-molecule stepping and structural dynamics of myosin X.
@ast
Single-molecule stepping and structural dynamics of myosin X.
@en
type
label
Single-molecule stepping and structural dynamics of myosin X.
@ast
Single-molecule stepping and structural dynamics of myosin X.
@en
prefLabel
Single-molecule stepping and structural dynamics of myosin X.
@ast
Single-molecule stepping and structural dynamics of myosin X.
@en
P2093
P2860
P356
P1476
Single-molecule stepping and structural dynamics of myosin X.
@en
P2093
Felix Ruhnow
Mark E Arsenault
Mitsuo Ikebe
Osamu Sato
Yale E Goldman
P2860
P2888
P304
P356
10.1038/NSMB.1785
P577
2010-04-04T00:00:00Z