Facilitated cross-bridge interactions with thin filaments by familial hypertrophic cardiomyopathy mutations in α-tropomyosin.
about
Ca(2+)-regulatory function of the inhibitory peptide region of cardiac troponin I is aided by the C-terminus of cardiac troponin T: Effects of familial hypertrophic cardiomyopathy mutations cTnI R145G and cTnT R278C, alone and in combination, on filPersistence length of human cardiac α-tropomyosin measured by single molecule direct probe microscopy.Micromechanical thermal assays of Ca2+-regulated thin-filament function and modulation by hypertrophic cardiomyopathy mutants of human cardiac troponinFluorescent Protein-Based Ca2+ Sensor Reveals Global, Divalent Cation-Dependent Conformational Changes in Cardiac Troponin CCongenital myopathy-causing tropomyosin mutations induce thin filament dysfunction via distinct physiological mechanisms.Slowed Dynamics of Thin Filament Regulatory Units Reduces Ca(2+)-Sensitivity of Cardiac Biomechanical Function.Role of cardiac troponin I carboxy terminal mobile domain and linker sequence in regulating cardiac contraction.The functional significance of the last 5 residues of the C-terminus of cardiac troponin I.Predicting Effects of Tropomyosin Mutations on Cardiac Muscle Contraction through Myofilament Modeling.Transmission of stability information through the N-domain of tropomyosin is interrupted by a stabilizing mutation (A109L) in the hydrophobic core of the stability control region (residues 97-118).Tropomyosin flexural rigidity and single ca(2+) regulatory unit dynamics: implications for cooperative regulation of cardiac muscle contraction and cardiomyocyte hypertrophy.Familial hypertrophic cardiomyopathy related E180G mutation increases flexibility of human cardiac α-tropomyosin.α-Tropomyosin with a D175N or E180G mutation in only one chain differs from tropomyosin with mutations in both chains.Investigating the effects of tropomyosin mutations on its flexibility and interactions with filamentous actin using molecular dynamics simulation.
P2860
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P2860
Facilitated cross-bridge interactions with thin filaments by familial hypertrophic cardiomyopathy mutations in α-tropomyosin.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Facilitated cross-bridge inter ...... hy mutations in α-tropomyosin.
@ast
Facilitated cross-bridge inter ...... hy mutations in α-tropomyosin.
@en
type
label
Facilitated cross-bridge inter ...... hy mutations in α-tropomyosin.
@ast
Facilitated cross-bridge inter ...... hy mutations in α-tropomyosin.
@en
prefLabel
Facilitated cross-bridge inter ...... hy mutations in α-tropomyosin.
@ast
Facilitated cross-bridge inter ...... hy mutations in α-tropomyosin.
@en
P2093
P2860
P356
P1476
Facilitated cross-bridge inter ...... thy mutations in α-tropomyosin
@en
P2093
Goran Mihajlović
Justin R Grubich
Lisa A Compton
Nicolas M Brunet
Thomas M Asbury
Victor F Miller
P2860
P304
P356
10.1155/2011/435271
P577
2011-12-01T00:00:00Z