Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers.
about
Structural changes in isometrically contracting insect flight muscle trapped following a mechanical perturbationThe significance of regulatory light chain phosphorylation in cardiac physiologyEffect of active shortening on the rate of ATP utilisation by rabbit psoas muscle fibresControl of myosin-I force sensing by alternative splicingA maximum entropy analysis of protein orientations using fluorescence polarization data from multiple probes.Polarized fluorescence depletion reports orientation distribution and rotational dynamics of muscle cross-bridges.Regulatory and essential light chains of myosin rotate equally during contraction of skeletal muscle.Changes in orientation of actin during contraction of muscleKinetics of cardiac thin-filament activation probed by fluorescence polarization of rhodamine-labeled troponin C in skinned guinea pig trabeculaeStructure and dynamics of the kinesin-microtubule interaction revealed by fluorescence polarization microscopy.Conformational changes between the active-site and regulatory light chain of myosin as determined by luminescence resonance energy transfer: the effect of nucleotides and actin.Past, present and future experiments on muscle.Familial hypertrophic cardiomyopathy can be characterized by a specific pattern of orientation fluctuations of actin molecules .Cross-bridge kinetics in myofibrils containing familial hypertrophic cardiomyopathy R58Q mutation in the regulatory light chain of myosinHolding two heads together: stability of the myosin II rod measured by resonance energy transfer between the headsSteady-state fluorescence polarization studies of the orientation of myosin regulatory light chains in single skeletal muscle fibers using pure isomers of iodoacetamidotetramethylrhodamine.Model-independent analysis of the orientation of fluorescent probes with restricted mobility in muscle fibers.Structural changes in the actin-myosin cross-bridges associated with force generation induced by temperature jump in permeabilized frog muscle fibersCaATP as a substrate to investigate the myosin lever arm hypothesis of force generation.Bifunctional rhodamine probes of Myosin regulatory light chain orientation in relaxed skeletal muscle fibers.Myosin regulatory domain orientation in skeletal muscle fibers: application of novel electron paramagnetic resonance spectral decomposition and molecular modeling methodsThe force exerted by a muscle cross-bridge depends directly on the strength of the actomyosin bond.Rotation of the lever arm of Myosin in contracting skeletal muscle fiber measured by two-photon anisotropy.Force generation in single conventional actomyosin complexes under high dynamic loadCoordination of the two heads of myosin during muscle contractionRevealingly odd couplesEvidence for pre- and post-power stroke of cross-bridges of contracting skeletal myofibrils.The spatial distribution of actin and mechanical cycle of myosin are different in right and left ventricles of healthy mouse heartsApplication of surface plasmon coupled emission to study of muscleStrain-dependent kinetics of the myosin working stroke, and how they could be probed with optical-trap experiments.Recent X-ray diffraction studies of muscle contraction and their implications.Effect of a myosin regulatory light chain mutation K104E on actin-myosin interactions.Using optical tweezers to relate the chemical and mechanical cross-bridge cycles.A Novel Method of Determining the Functional Effects of a Minor Genetic Modification of a Protein.Comparison of orientation and rotational motion of skeletal muscle cross-bridges containing phosphorylated and dephosphorylated myosin regulatory light chain.Detection of electrophile-sensitive proteins.Site-directed spectroscopic probes of actomyosin structural dynamics.Phosphorylation of myosin regulatory light chain has minimal effect on kinetics and distribution of orientations of cross bridges of rabbit skeletal muscle.Mesoscopic analysis of motion and conformation of cross-bridges.Influence of ionic strength on the actomyosin reaction steps in contracting skeletal muscle fibers.
P2860
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P2860
Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Fluorescence polarization tran ...... ain in skeletal muscle fibers.
@ast
Fluorescence polarization tran ...... ain in skeletal muscle fibers.
@en
Fluorescence polarization tran ...... ain in skeletal muscle fibers.
@nl
type
label
Fluorescence polarization tran ...... ain in skeletal muscle fibers.
@ast
Fluorescence polarization tran ...... ain in skeletal muscle fibers.
@en
Fluorescence polarization tran ...... ain in skeletal muscle fibers.
@nl
prefLabel
Fluorescence polarization tran ...... ain in skeletal muscle fibers.
@ast
Fluorescence polarization tran ...... ain in skeletal muscle fibers.
@en
Fluorescence polarization tran ...... ain in skeletal muscle fibers.
@nl
P2093
P2860
P1433
P1476
Fluorescence polarization tran ...... ain in skeletal muscle fibers.
@en
P2093
C Sabido-David
J E Corrie
S C Hopkins
Y E Goldman
P2860
P304
P356
10.1016/S0006-3495(98)78016-6
P407
P577
1998-06-01T00:00:00Z