Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon-mediated inhibition of actin filament velocity
about
Invited review: cross-bridge regulation by thin filament-associated proteinsTyrosine Phosphorylation of Caldesmon Is Required for Binding to the Shc{middle dot}Grb2 ComplexDifferential effects of caldesmon on the intermediate conformational states of polymerizing actin.The role of caldesmon and its phosphorylation by ERK on the binding force of unphosphorylated myosin to actin.Caldesmon and the regulation of cytoskeletal functions.Ablation of smooth muscle caldesmon affects the relaxation kinetics of arterial musclecGMP-dependent protein kinase Iβ regulates breast cancer cell migration and invasion via interaction with the actin/myosin-associated protein caldesmon.Caldesmon inhibits nonmuscle cell contractility and interferes with the formation of focal adhesions.Smooth muscle signalling pathways in health and disease.Amino acid mutations in the caldesmon COOH-terminal functional domain increase force generation in bladder smooth muscle.Smooth muscle caldesmon modulates peristalsis in the wild type and non-innervated zebrafish intestine.Diversification of caldesmon-linked actin cytoskeleton in cell motility.Modes of caldesmon binding to actin: sites of caldesmon contact and modulation of interactions by phosphorylation.Caldesmon regulates axon extension through interaction with myosin II.Diabetes decreases rabbit bladder smooth muscle contraction while increasing levels of myosin light chain phosphorylation.Role of cAMP-dependent protein kinase A activity in endothelial cell cytoskeleton rearrangement.Isoform switching from SM-B to SM-A myosin results in decreased contractility and altered expression of thin filament regulatory proteins.Twitchin from molluscan catch muscle: primary structure and relationship between site-specific phosphorylation and mechanical function.A caldesmon peptide activates smooth muscle via a mechanism similar to ERK-mediated phosphorylation.
P2860
Q28609856-5C6D7599-34E1-4975-BE14-34E076F64480Q29029818-DA3BCA26-633F-443E-AF33-A9391F4773B8Q33581475-FF10D79B-15B1-49B9-A16D-9A641D373275Q34194260-2B100142-12B5-4424-8170-F5E72394948DQ34284851-237EEC33-894F-44AF-9BA8-253837FC8B64Q36581995-B4555779-33FC-42B2-B2F0-89B9C9D9F98DQ36825244-C8152969-3150-4F24-8D8D-EDCEEAD9F39AQ36915358-899917FF-DA02-47D1-8A69-9F7FBE294C78Q37217197-23A12756-9219-437E-9ED3-EA8212BCBA49Q37342112-421E84EB-E110-4196-98E3-863FBC69D01BQ37573647-98CB6307-6042-4C4F-BE9A-4B886288D3DDQ37847039-4D650C1D-5CA9-490D-95D7-BA4C45BD553AQ38449013-80F11F8C-9461-45C4-BF70-806229248A51Q40810539-4EFE8ACE-E347-408E-8607-D2F6F978B3F0Q42463192-97A073FF-C066-4FBF-B36E-E3F18773BD00Q43606177-76B0DD83-DEBD-4D3D-BDDF-E8ADF23F5CA4Q44894340-4F918CCD-9657-447A-94DE-1E267BD1DAE8Q48245693-EF67D388-66AE-4905-A717-E192CF2ED652Q53560302-00879E6C-EA60-4F9B-9A38-DE8EC0448169
P2860
Both N-terminal myosin-binding and C-terminal actin-binding sites on smooth muscle caldesmon are required for caldesmon-mediated inhibition of actin filament velocity
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Both N-terminal myosin-binding ...... ion of actin filament velocity
@ast
Both N-terminal myosin-binding ...... ion of actin filament velocity
@en
type
label
Both N-terminal myosin-binding ...... ion of actin filament velocity
@ast
Both N-terminal myosin-binding ...... ion of actin filament velocity
@en
prefLabel
Both N-terminal myosin-binding ...... ion of actin filament velocity
@ast
Both N-terminal myosin-binding ...... ion of actin filament velocity
@en
P2093
P2860
P356
P1476
Both N-terminal myosin-binding ...... ion of actin filament velocity
@en
P2093
P2860
P304
11899-11904
P356
10.1073/PNAS.94.22.11899
P407
P577
1997-10-01T00:00:00Z