Dystrophin's tandem calponin-homology domains: is the case closed? - Wikidata - wikimedia - TriplyDB

Dystrophin's tandem calponin-homology domains: is the case closed?

Dystrophin's tandem calponin-homology domains: is the case closed?

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Flexibility in the N-terminal actin-binding domain: clues from in silico mutations and molecular dynamics.Circularly polarised luminescence and circular dichroism of l- and d-oligopeptides with multiple pyrenes.

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Dystrophin's tandem calponin-homology domains: is the case closed?

http://www.wikidata.org/entity/Q41412648

description

2012 nî lūn-bûn

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

@zh-hk

2012年論文

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2012年論文

@zh-tw

2012年论文

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2012年论文

@zh

2012年论文

@zh-cn

name

Dystrophin's tandem calponin-homology domains: is the case closed?

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type

label

Dystrophin's tandem calponin-homology domains: is the case closed?

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prefLabel

Dystrophin's tandem calponin-homology domains: is the case closed?

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J.BPJ.2012.09.037

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Biophysical Journal

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Dystrophin's tandem calponin-homology domains: is the case closed?

@en

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Neville R Kallenbach

http://www.w3.org/2001/XMLSchema#string

Roberto Dominguez

http://www.w3.org/2001/XMLSchema#string

P2860

The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy

Actin binding proteins: regulation of cytoskeletal microfilaments

Pyrene: a probe to study protein conformation and conformational changes.

Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates.

Functional plasticity of CH domains.

Large-scale opening of utrophin's tandem calponin homology (CH) domains upon actin binding by an induced-fit mechanism

Emerging strategies for cell and gene therapy of the muscular dystrophies

Novel structural insights into F-actin-binding and novel functions of calponin homology domains.

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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1818-1819

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scholarly article

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10.1016/J.BPJ.2012.09.037

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9

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103

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2012-11-01T00:00:00Z

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23199908

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3491714

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