Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction.
about
Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscleSkeletal muscle myofilament adaptations to aging, disease, and disuse and their effects on whole muscle performance in older adult humansShort-range mechanical properties of skeletal and cardiac musclesBasal myosin light chain phosphorylation is a determinant of Ca2+ sensitivity of force and activation dependence of the kinetics of myocardial force developmentRegulation of human heart contractility by essential myosin light chain isoformsAltered kinetics of contraction in skeletal muscle fibers containing a mutant myosin regulatory light chain with reduced divalent cation bindingEffects of a R133W beta-tropomyosin mutation on regulation of muscle contraction in single human muscle fibresATP utilization for calcium uptake and force production in different types of human skeletal muscle fibresEffects of sarcomere length and temperature on the rate of ATP utilisation by rabbit psoas muscle fibresAltered cross-bridge characteristics following haemodynamic overload in rabbit hearts expressing V3 myosinRegulation of force development studied by photolysis of caged ADP in rabbit skinned psoas fibers.Regulation of force and unloaded sliding speed in single thin filaments: effects of regulatory proteins and calciumPKA accelerates rate of force development in murine skinned myocardium expressing alpha- or beta-tropomyosinActivation kinetics of skinned cardiac muscle by laser photolysis of nitrophenyl-EGTA.The converter domain modulates kinetic properties of Drosophila myosin.Single-myosin crossbridge interactions with actin filaments regulated by troponin-tropomyosin.Sarcomere lattice geometry influences cooperative myosin binding in muscle.Regulation of fibre contraction in a rat model of myocardial ischemia.Nebulin plays a direct role in promoting strong actin-myosin interactions.Titin-mediated control of cardiac myofibrillar function.Ca2+-independent positive molecular inotropy for failing rabbit and human cardiac muscle by alpha-myosin motor gene transfer.Left ventricular and myocardial function in mice expressing constitutively pseudophosphorylated cardiac troponin I.Coupling of adjacent tropomyosins enhances cross-bridge-mediated cooperative activation in a markov model of the cardiac thin filament.Phosphorylation-dependent power output of transgenic flies: an integrated study.Rate constant of muscle force redevelopment reflects cooperative activation as well as cross-bridge kineticsStrain-dependent modulation of phosphate transients in rabbit skeletal muscle fibers.Inhibition of cross-bridge binding to actin by caldesmon fragments in skinned skeletal muscle fibers.Calcium regulation of skeletal muscle thin filament motility in vitro.Nucleotide-dependent contractile properties of Ca(2+)-activated fast and slow skeletal muscle fibers.Kinetics of thin filament activation probed by fluorescence of N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-1,3-diazole-labeled troponin I incorporated into skinned fibers of rabbit psoas muscle: implications for regulation of muscle cEffect of Ca2+ on weak cross-bridge interaction with actin in the presence of adenosine 5'-[gamma-thio]triphosphate).Calcium regulation of thin filament movement in an in vitro motility assay.Phosphate release and force generation in cardiac myocytes investigated with caged phosphate and caged calciumMyosin regulatory light chain modulates the Ca2+ dependence of the kinetics of tension development in skeletal muscle fibers.Influence of Ca2+ on force redevelopment kinetics in skinned rat myocardiumActivation of skinned trabeculae of the guinea pig induced by laser photolysis of caged ATP.Unloaded shortening of skinned muscle fibers from rabbit activated with and without Ca2+.Isometric force redevelopment of skinned muscle fibers from rabbit activated with and without Ca2+Calcium alone does not fully activate the thin filament for S1 binding to rigor myofibrils.Calmidazolium alters Ca2+ regulation of tension redevelopment rate in skinned skeletal muscle
P2860
Q24631228-C94AE7E5-7FD9-489D-A2C6-37A26E954EE8Q27026517-DC49656A-F7C8-443B-8652-893382201F54Q27692693-BFE9E53D-FF74-4B7F-AF3B-7A8DF22A6786Q28278986-44ACABC1-33ED-4131-AA3D-33903529EB92Q28286778-FF66DA2A-D175-46AD-BDD2-D42712F5E4AEQ28289634-0BB6B2FC-8CC5-4231-BBD5-ED52F08F398EQ28297814-B08D50E7-7077-4C06-9D03-695A4F063FF6Q28355819-7D165598-A022-4710-92D6-CF054748B25DQ28360339-C7940038-F1CA-46B7-904B-C1D307C95371Q28361710-001DA4C1-63F8-48F6-A980-60C1740B1100Q28367676-1D708CC9-6BAD-419E-9765-0536CCC06743Q28578662-DF3B9010-ADBA-4A7D-84FE-C7E35AEF3584Q28591008-B803224A-3D83-4CBD-911D-BB5186204B76Q30827985-FC32E208-AE5B-4AA6-9DF0-C6B3EDA06CABQ33185427-144A628D-C4B8-4C2D-87E1-B8F02C5F4A1CQ33227190-85D401B8-E819-4704-81D2-70B4BB63CB0FQ33290825-89A9E4DB-1C4F-4C77-B340-AA7B21716C24Q33538026-C0023BBC-5CF1-40DA-94EE-C77640CCF391Q33613267-94466C31-40FC-49C1-9E31-E6B8ECEAEB6EQ33639147-B731A2D0-FCA1-42AF-A4BB-7F0FD7E51D87Q33724399-0D3E1BCD-6F66-4C5C-AD33-6360D0462480Q33822294-5ADF2DDD-F2FA-4D4E-87D9-B4371D6EE3F3Q33858361-C4B7753B-7952-4560-8813-795696837E26Q33907968-F5835599-8B0E-45D0-A0B9-1807A05BE4BCQ33915124-62AD1917-1FA0-471B-8C55-13C21EBDE422Q33915329-2E247278-D7D4-4B94-952E-955857B125B6Q33915734-C48F0A25-68C7-4575-B09E-2B48C10476EDQ33915741-EF34A18E-4758-43B5-ABAA-1F9D46D83911Q33916874-1FEA8894-572C-4E04-8C83-F3ADE54A9E81Q33947371-3B093654-4C3A-4766-B0BC-69F31A5393BBQ33973089-80EA3411-C3D2-4C3A-AA43-9F4464588584Q34017653-F548A89C-BDF0-49B7-880C-85692DFCA6E1Q34017764-50695D19-72F8-4C7A-B005-9478B8F14E68Q34017769-70823C43-2B3B-4411-9DDB-288D06C3C6B5Q34017975-DBD83AEE-95EA-4771-AC4D-B38D1E4949F6Q34018863-6CCB4698-916F-43FE-B818-1AA862F95DCBQ34018883-F0AE99C9-573C-49C9-8EC7-CA21C630A639Q34018888-91452210-4FBE-49A2-B624-6CA416CC370FQ34040718-0B0DE5A3-3726-4260-959A-F2864FD9B9B5Q34041122-FA0D674E-F75A-453E-9E3E-73B4336467B8
P2860
Effect of Ca2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction.
description
1988 nî lūn-bûn
@nan
1988 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Effect of Ca2+ on cross-bridge ...... ulation of muscle contraction.
@ast
Effect of Ca2+ on cross-bridge ...... ulation of muscle contraction.
@en
Effect of Ca2+ on cross-bridge ...... ulation of muscle contraction.
@nl
type
label
Effect of Ca2+ on cross-bridge ...... ulation of muscle contraction.
@ast
Effect of Ca2+ on cross-bridge ...... ulation of muscle contraction.
@en
Effect of Ca2+ on cross-bridge ...... ulation of muscle contraction.
@nl
prefLabel
Effect of Ca2+ on cross-bridge ...... ulation of muscle contraction.
@ast
Effect of Ca2+ on cross-bridge ...... ulation of muscle contraction.
@en
Effect of Ca2+ on cross-bridge ...... ulation of muscle contraction.
@nl
P2860
P356
P1476
Effect of Ca2+ on cross-bridge ...... ulation of muscle contraction.
@en
P2093
P2860
P304
P356
10.1073/PNAS.85.9.3265
P407
P577
1988-05-01T00:00:00Z