The N-terminal actin-binding tandem calponin-homology (CH) domain of dystrophin is in a closed conformation in solution and when bound to F-actin.
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In vivo epidermal migration requires focal adhesion targeting of ACF7F-actin clustering and cell dysmotility induced by the pathological W148R missense mutation of filamin B at the actin-binding domainMissense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function.Dystrophin hydrophobic regions in the pathogenesis of Duchenne and Becker muscular dystrophies.Dystrophin and Spectrin, Two Highly Dissimilar Sisters of the Same Family.Spectraplakin family proteins - cytoskeletal crosslinkers with versatile roles.Dystrophin's tandem calponin-homology domains: is the case closed?Flexibility in the N-terminal actin-binding domain: clues from in silico mutations and molecular dynamics.
P2860
Q27704925-73273B7D-F35A-4F20-AAB7-B3024146BB9BQ30354586-411BCB73-9E26-4C58-A003-94A9E84D4C96Q30368050-27BDD597-94EE-4136-B3EB-02C58B560608Q35749826-A9587562-54E4-46B5-BDF6-C74833E1E16FQ39094614-5B1777D5-7DC6-48AA-880B-4F2154DC6446Q39416143-FD04787B-F1B2-4605-BFF9-C041E2C9B3A3Q41412648-AB182892-5517-4D4A-A584-27EED3AA38F8Q41529085-45FF0030-56C4-48BF-B747-C2B1866D9BBC
P2860
The N-terminal actin-binding tandem calponin-homology (CH) domain of dystrophin is in a closed conformation in solution and when bound to F-actin.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
The N-terminal actin-binding t ...... ion and when bound to F-actin.
@en
type
label
The N-terminal actin-binding t ...... ion and when bound to F-actin.
@en
prefLabel
The N-terminal actin-binding t ...... ion and when bound to F-actin.
@en
P2860
P1433
P1476
The N-terminal actin-binding t ...... tion and when bound to F-actin
@en
P2093
Surinder M Singh
P2860
P304
P356
10.1016/J.BPJ.2012.08.066
P407
P577
2012-11-01T00:00:00Z