Effects of pathogenic proline mutations on myosin assembly.
about
Myosin filament assembly requires a cluster of four positive residues located in the rod domainSkip residues modulate the structural properties of the myosin rod and guide thick filament assembly.A composite approach towards a complete model of the myosin rodNovel mutations widen the phenotypic spectrum of slow skeletal/β-cardiac myosin (MYH7) distal myopathyTwo novel MYH7 proline substitutions cause Laing Distal Myopathy-like phenotypes with variable expressivity and neck extensor contracture.Biology of the cardiac myocyte in heart disease.Myosinopathies: pathology and mechanisms.Structural implications of β-cardiac myosin heavy chain mutations in human disease.Cardiomyopathy mutations in the tail of β-cardiac myosin modify the coiled-coil structure and affect integration into thick filaments in muscle sarcomeres in adult cardiomyocytes.A1603P and K1617del, Mutations in β-Cardiac Myosin Heavy Chain that Cause Laing Early-Onset Distal Myopathy, Affect Secondary Structure and Filament Formation In Vitro and In Vivo.
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Effects of pathogenic proline mutations on myosin assembly.
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
Effects of pathogenic proline mutations on myosin assembly.
@ast
Effects of pathogenic proline mutations on myosin assembly.
@en
type
label
Effects of pathogenic proline mutations on myosin assembly.
@ast
Effects of pathogenic proline mutations on myosin assembly.
@en
prefLabel
Effects of pathogenic proline mutations on myosin assembly.
@ast
Effects of pathogenic proline mutations on myosin assembly.
@en
P2093
P2860
P1476
Effects of pathogenic proline mutations on myosin assembly.
@en
P2093
Ada Buvoli
Leslie A Leinwand
Massimo Buvoli
P2860
P304
P356
10.1016/J.JMB.2011.11.042
P407
P577
2011-12-06T00:00:00Z