Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.

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The Interaction between the Third Type III Domain from Fibronectin and Anastellin Involves β-Strand Exchange.Protein unfolding under isometric tension-what force can integrins generate, and can it unfold FNIII domains?Does iris(in) bring bad news or good news?

P2860

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P2860

Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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Spontaneous Unfolding-Refoldin ...... UNFOLDING RATHER THAN FOLDING.

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Spontaneous Unfolding-Refoldin ...... UNFOLDING RATHER THAN FOLDING.

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type

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Spontaneous Unfolding-Refoldin ...... UNFOLDING RATHER THAN FOLDING.

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Spontaneous Unfolding-Refoldin ...... UNFOLDING RATHER THAN FOLDING.

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prefLabel

Spontaneous Unfolding-Refoldin ...... UNFOLDING RATHER THAN FOLDING.

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Spontaneous Unfolding-Refoldin ...... UNFOLDING RATHER THAN FOLDING.

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P1476

Spontaneous Unfolding-Refoldin ...... UNFOLDING RATHER THAN FOLDING.

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P2093

Harold P Erickson

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

Riddhi Shah

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

Terrence G Oas

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

Tomoo Ohashi

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

P2860

Crystal structure of a heparin- and integrin-binding segment of human fibronectin.

Tissue sulfhydryl groups

Force-induced unfolding of fibronectin in the extracellular matrix of living cells

Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis

The Structure of Irisin Reveals a Novel Intersubunit -Sheet Fibronectin Type III (FNIII) Dimer: IMPLICATIONS FOR RECEPTOR ACTIVATION

2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region

Fibronectin in extended and compact conformations. Electron microscopy and sedimentation analysis

Structure and unfolding of the third type III domain from human fibronectin

Hydrogen exchange and structural dynamics of proteins and nucleic acids

The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.

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955-966

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scholarly article

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10.1074/JBC.M116.760371

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English

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292

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2016-11-30T00:00:00Z

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27909052

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refolding

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Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.

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P2860

P2860

Spontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.

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P2860

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P932