Mode of caldesmon binding to smooth muscle thin filament: possible projection of the amino-terminal of caldesmon from native thin filament.
about
Affinity and structure of complexes of tropomyosin and caldesmon domains.Caldesmon and the regulation of cytoskeletal functions.Higher plant myosin XI moves processively on actin with 35 nm steps at high velocityHeat treatment could affect the biochemical properties of caldesmon.The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations.Modulation of gelsolin-induced actin-filament severing by caldesmon and tropomyosin and the effect of these proteins on the actin activation of myosin Mg(2+)-ATPase activity.The calcium-binding loops of the tandem C2 domains of synaptotagmin VII cooperatively mediate calcium-dependent oligomerization.
P2860
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P2860
Mode of caldesmon binding to smooth muscle thin filament: possible projection of the amino-terminal of caldesmon from native thin filament.
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Mode of caldesmon binding to s ...... mon from native thin filament.
@ast
Mode of caldesmon binding to s ...... mon from native thin filament.
@en
Mode of caldesmon binding to s ...... mon from native thin filament.
@nl
type
label
Mode of caldesmon binding to s ...... mon from native thin filament.
@ast
Mode of caldesmon binding to s ...... mon from native thin filament.
@en
Mode of caldesmon binding to s ...... mon from native thin filament.
@nl
prefLabel
Mode of caldesmon binding to s ...... mon from native thin filament.
@ast
Mode of caldesmon binding to s ...... mon from native thin filament.
@en
Mode of caldesmon binding to s ...... mon from native thin filament.
@nl
P2860
P1433
P1476
Mode of caldesmon binding to s ...... mon from native thin filament.
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(95)80424-8
P407
P577
1995-06-01T00:00:00Z