Kinetic studies of calcium binding to regulatory complexes from skeletal muscle.
about
Activation of fast skeletal muscle troponin as a potential therapeutic approach for treating neuromuscular diseasesEffects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin CStriated muscle regulation of isometric tension by multiple equilibria.Comparison of simulated and measured calcium sparks in intact skeletal muscle fibers of the frogKinetics 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 cIdentification of troponin I and actin, alpha cardiac muscle 1 as potential biomarkers for hearts of electrically stimulated chickens.Regulation of skeletal muscle tension redevelopment by troponin C constructs with different Ca2+ affinities.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.Effects of actin-myosin kinetics on the calcium sensitivity of regulated thin filaments.The roles of troponin C isoforms in the mechanical function of Drosophila indirect flight muscleMeasurement of calcium dissociation rates from troponin C in rigor skeletal myofibrils.Kinetic mechanism of the Ca2+-dependent switch-on and switch-off of cardiac troponin in myofibrils.The kinetic cycle of cardiac troponin C: calcium binding and dissociation at site II trigger slow conformational rearrangements.Extra calcium on shortening in barnacle muscle. Is the decrease in calcium binding related to decreased cross-bridge attachment, force, or length?The dynamics of actin and myosin association and the crossbridge model of muscle contraction.Differences between cardiac and skeletal troponin interaction with the thin filament probed by troponin exchange in skeletal myofibrilsThe molecular basis of the steep force-calcium relation in heart muscleThe Ca2+ sensitizer CK-2066260 increases myofibrillar Ca2+ sensitivity and submaximal force selectively in fast skeletal muscle.Structural dynamics of troponin during activation of skeletal muscle.Switch action of troponin on muscle thin filament as revealed by spin labeling and pulsed EPR.An x-ray diffraction study on early structural changes in skeletal muscle contraction.The structural and functional effects of the familial hypertrophic cardiomyopathy-linked cardiac troponin C mutation, L29QTwo-step ligand binding and cooperativity. A model to describe the cooperative binding of myosin subfragment 1 to regulated actinKinetics of contractile activation in voltage clamped frog skeletal muscle fibers.Calcium signals recorded from cut frog twitch fibers containing antipyrylazo III.Kinetic mechanism of Ca²⁺-controlled changes of skeletal troponin I in psoas myofibrils.The effects of reported Ca2+ sensitisers on the rates of Ca2+ release from cardiac troponin C and the troponin-tropomyosin complex.Effects of deletion of tropomyosin overlap on regulated actomyosin subfragment 1 ATPaseCalcium signals recorded from cut frog twitch fibers containing tetramethylmurexide.A quantitative analysis of cardiac myocyte relaxation: a simulation study.Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils.Regulation of Contraction by the Thick Filaments in Skeletal Muscle.Thin-filament regulation of force redevelopment kinetics in rabbit skeletal muscle fibres.
P2860
Q28260224-B4C9EA67-CB81-447C-9FB7-4833ECD91959Q28287686-6D55BB7E-A852-4926-ADB4-2BBCD35E001CQ30974507-58551B4B-E799-413F-B10F-4C8BBDC14647Q33184210-75C5A8BF-82F4-4969-9E16-E4411C644D28Q33947371-2EF028D3-1183-4D98-82E3-1547912FAC41Q34122148-2F7A59F7-9968-4568-A702-3AC8E6413D10Q34170456-2E5562B4-DDB1-451C-A603-0E7E92E06450Q34171762-9678C2D8-2AE9-4FBD-ACB8-CF817BB201EDQ34385850-9955A549-1014-452D-9220-B82AF038152AQ34517038-3D11A58E-01C9-4E7E-BA01-CEAC94A8215AQ35302171-F17EC4D8-4DD1-4010-9B54-FEF0FB1E7236Q36176605-610FB2D1-00CE-484E-A714-1CCB31C026A0Q36280726-B410CFE1-E312-40A6-AC63-89EF563D1F42Q36433930-FE28998D-C920-4C28-B1B9-EF4896A7E49BQ37079269-B7ADBCEC-C2FE-4EAA-AA2F-7FD7F92BD6D4Q37263401-724F072F-1EB6-485B-BF6F-8EC06AD3457AQ37652027-0717EDF7-8579-4821-9C32-650E6DF6CE82Q37672278-C58C7D36-6140-4D79-8D99-153B468806F4Q37674400-97F469D7-F17A-4385-869C-AD4B90F2EEC0Q40075726-DB2F60C4-2765-4B44-9520-099B0C706158Q40229332-87A26530-40DF-44C3-B22C-B4DE3C5F133FQ40572286-D34B201E-149B-40CF-82BB-E6B4DB1FCB79Q41172090-CE8D616A-58F1-4FE8-8E97-30E1B7B8E622Q41784813-A3AF01A5-8358-472C-9553-ED978D1216C4Q41860014-44A7D043-E5A0-431C-9431-D1581A02788EQ41866091-99C0DD1A-DDB7-434F-9DD1-85C652567600Q42563335-DA5DAB18-F949-4817-8421-C4630FDA5E4BQ42835794-CB67BC13-FD53-4B42-8C25-8D950223763FQ42975768-761C1046-4C0D-4A4A-B734-27861E5EC7C0Q43203647-D401DE3D-4290-49A2-BA62-AE7D98F3A169Q44560762-7A893796-578F-4DC3-B766-DA465ACD22EDQ47270685-4EF62624-F947-4EF9-A0A0-825151A09FDBQ51925705-F204403F-0E75-4998-9A56-C1F8A8D3EFE6
P2860
Kinetic studies of calcium binding to regulatory complexes from skeletal muscle.
description
1985 nî lūn-bûn
@nan
1985年の論文
@ja
1985年学术文章
@wuu
1985年学术文章
@zh
1985年学术文章
@zh-cn
1985年学术文章
@zh-hans
1985年学术文章
@zh-my
1985年学术文章
@zh-sg
1985年學術文章
@yue
1985年學術文章
@zh-hant
name
Kinetic studies of calcium binding to regulatory complexes from skeletal muscle.
@en
Kinetic studies of calcium binding to regulatory complexes from skeletal muscle.
@nl
type
label
Kinetic studies of calcium binding to regulatory complexes from skeletal muscle.
@en
Kinetic studies of calcium binding to regulatory complexes from skeletal muscle.
@nl
prefLabel
Kinetic studies of calcium binding to regulatory complexes from skeletal muscle.
@en
Kinetic studies of calcium binding to regulatory complexes from skeletal muscle.
@nl
P1476
Kinetic studies of calcium binding to regulatory complexes from skeletal muscle
@en
P2093
Rosenfeld SS
P304
P407
P577
1985-01-01T00:00:00Z