The SAH domain extends the functional length of the myosin lever
about
Myosin-X and diseaseThe myosin superfamily at a glance.Lever-arm mechanics of processive myosinsHarnessing the unique structural properties of isolated α-helices.The Inner Centromere Protein (INCENP) Coil Is a Single α-Helix (SAH) Domain That Binds Directly to Microtubules and Is Important for Chromosome Passenger Complex (CPC) Localization and Function in Mitosis.Structured post-IQ domain governs selectivity of myosin X for fascin-actin bundles.Cargo binding activates myosin VIIA motor function in cellsStable single α-helices are constant force springs in proteinsA method for multiprotein assembly in cells reveals independent action of kinesins in complexA Combination of Diffusion and Active Translocation Localizes Myosin 10 to the Filopodial TipCoupling of two non-processive myosin 5c dimers enables processive stepping along actin filaments.Myosin-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 myosinsMyo1c mutations associated with hearing loss cause defects in the interaction with nucleotide and actin.Detailed tuning of structure and intramolecular communication are dispensable for processive motion of myosin VI.Drosophila melanogaster myosin-18 represents a highly divergent motor with actin tethering propertiesMyosin-X: a MyTH-FERM myosin at the tips of filopodiaInteractions of Yeast Dynein with Dynein Light Chain and Dynactin: GENERAL IMPLICATIONS FOR INTRINSICALLY DISORDERED DUPLEX SCAFFOLDS IN MULTIPROTEIN ASSEMBLIESDistribution and evolution of stable single α-helices (SAH domains) in myosin motor proteinsMyosin X dimerization and its impact on cellular functions.Kinetic characterization of nonmuscle myosin IIb at the single molecule levelMammalian myosin-18A, a highly divergent myosin.Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection.Dimerization of mammalian kinesin-3 motors results in superprocessive motionCoiled coils and SAH domains in cytoskeletal molecular motors.Kinetic Adaptations of Myosins for Their Diverse Cellular FunctionsMechanics and Activation of Unconventional Myosins.Lever arm extension of myosin VI is unnecessary for the adjacent binding state.Myosin VI must dimerize and deploy its unusual lever arm in order to perform its cellular roles.Functional and Structural Characterization of Novel Type of Linker Connecting Capsid and Nucleocapsid Protein Domains in Murine Leukemia Virus.Dynein achieves processive motion using both stochastic and coordinated stepping.Helicity of short E-R/K peptides.Local and macroscopic electrostatic interactions in single α-helices.Myosin tails and single α-helical domains.The path to visualization of walking myosin V by high-speed atomic force microscopy.Characterization of long and stable de novo single alpha-helix domains provides novel insight into their stability.Cardiomyopathy mutations in the tail of β-cardiac myosin modify the coiled-coil structure and affect integration into thick filaments in muscle sarcomeres in adult cardiomyocytes.The winch model can explain both coordinated and uncoordinated stepping of cytoplasmic dynein.The Shaker-1 Mouse Myosin VIIa Deafness Mutation Results in a Severely Reduced Rate of the ATP Hydrolysis Step.
P2860
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P2860
The SAH domain extends the functional length of the myosin lever
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 15 December 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
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name
The SAH domain extends the functional length of the myosin lever
@en
The SAH domain extends the functional length of the myosin lever
@en-gb
The SAH domain extends the functional length of the myosin lever.
@nl
type
label
The SAH domain extends the functional length of the myosin lever
@en
The SAH domain extends the functional length of the myosin lever
@en-gb
The SAH domain extends the functional length of the myosin lever.
@nl
prefLabel
The SAH domain extends the functional length of the myosin lever
@en
The SAH domain extends the functional length of the myosin lever
@en-gb
The SAH domain extends the functional length of the myosin lever.
@nl
P2093
P2860
P356
P1154
2-s2.0-76049109811
P1476
The SAH domain extends the functional length of the myosin lever
@en
P2093
Eva Forgacs
Howard D White
James R Sellers
Justin E Molloy
Peter J Knight
Rachel E Farrow
Scott M Jackson
Takeshi Sakamoto
Thomas G Baboolal
Yasuharu Takagi
P2860
P304
22193-22198
P356
10.1073/PNAS.0909851106
P407
P577
2009-12-15T00:00:00Z