Electrostatic interaction map reveals a new binding position for tropomyosin on F-actin.
about
Insight into muscle physiology through understanding mechanisms of muscle pathology.The propensity for tropomyosin twisting in the presence and absence of F-actin.Tropomyosin diffusion over actin subunits facilitates thin filament assembly.Tropomyosin Must Interact Weakly with Actin to Effectively Regulate Thin Filament Function.Distortion of the Actin A-Triad Results in Contractile Disinhibition and Cardiomyopathy.Investigating the effects of tropomyosin mutations on its flexibility and interactions with filamentous actin using molecular dynamics simulation.HCM and DCM cardiomyopathy-linked α-tropomyosin mutations influence off-state stability and crossbridge interaction on thin filaments.
P2860
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P2860
Electrostatic interaction map reveals a new binding position for tropomyosin on F-actin.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Electrostatic interaction map reveals a new binding position for tropomyosin on F-actin.
@en
type
label
Electrostatic interaction map reveals a new binding position for tropomyosin on F-actin.
@en
prefLabel
Electrostatic interaction map reveals a new binding position for tropomyosin on F-actin.
@en
P2093
P2860
P1476
Electrostatic interaction map reveals a new binding position for tropomyosin on F-actin
@en
P2093
Marek Orzechowski
Stefan Fischer
Veronika Schott
William Lehman
P2860
P2888
P304
P356
10.1007/S10974-015-9419-Z
P577
2015-08-19T00:00:00Z
P6179
1037638770