Effect of temperature on relaxation rate and Ca2+, Mg2+ dissociation rates from parvalbumin of frog muscle fibres.
about
Crystal structure of the EF-hand parvalbumin at atomic resolution (0.91 Å) and at low temperature (100 K). Evidence for conformational multistates within the hydrophobic coreHydration-coupled dynamics in proteins studied by neutron scattering and NMR: the case of the typical EF-hand calcium-binding parvalbumin.Intracellular EDTA mimics parvalbumin in the promotion of skeletal muscle relaxation.Optimal range for parvalbumin as relaxing agent in adult cardiac myocytes: gene transfer and mathematical modeling.Noncanonical EF-hand motif strategically delays Ca2+ buffering to enhance cardiac performanceParvalbumin isoforms for enhancing cardiac diastolic function.Engineering Parvalbumin for the Heart: Optimizing the Mg Binding Properties of Rat β-ParvalbuminParvalbumin gene transfer corrects diastolic dysfunction in diseased cardiac myocytes.Trading force for speed: why superfast crossbridge kinetics leads to superlow forcesKinetic control of Ca(II) signaling: tuning the ion dissociation rates of EF-hand Ca(II) binding sites.Ca²⁺-pumping impairment during repetitive fatiguing contractions in single myofibers: role of cross-bridge cycling.Designing heart performance by gene transfer.Intracellular calcium movements during relaxation and recovery of superfast muscle fibers of the toadfish swimbladder.A review of the thermal sensitivity of the mechanics of vertebrate skeletal muscle.Energetics of contraction.Cardiac-directed parvalbumin transgene expression in mice shows marked heart rate dependence of delayed Ca2+ buffering action.Molecular tuning of ion binding to calcium signaling proteins.Millisecond time-resolved changes occurring in Ca2+-regulated myosin filaments upon relaxation.Engineering competitive magnesium binding into the first EF-hand of skeletal troponin C.Calcium removal kinetics of the sarcoplasmic reticulum ATPase in skeletal muscle.Differences in Ca2+ buffering properties between excitatory and inhibitory hippocampal neurons from the rat
P2860
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P2860
Effect of temperature on relaxation rate and Ca2+, Mg2+ dissociation rates from parvalbumin of frog muscle fibres.
description
1992 nî lūn-bûn
@nan
1992 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
Effect of temperature on relax ...... albumin of frog muscle fibres.
@ast
Effect of temperature on relax ...... albumin of frog muscle fibres.
@en
Effect of temperature on relax ...... albumin of frog muscle fibres.
@nl
type
label
Effect of temperature on relax ...... albumin of frog muscle fibres.
@ast
Effect of temperature on relax ...... albumin of frog muscle fibres.
@en
Effect of temperature on relax ...... albumin of frog muscle fibres.
@nl
prefLabel
Effect of temperature on relax ...... albumin of frog muscle fibres.
@ast
Effect of temperature on relax ...... albumin of frog muscle fibres.
@en
Effect of temperature on relax ...... albumin of frog muscle fibres.
@nl
P2093
P1476
Effect of temperature on relax ...... albumin of frog muscle fibres.
@en
P2093
P304
P356
10.1113/JPHYSIOL.1992.SP019092
P407
P577
1992-04-01T00:00:00Z