ClpB chaperone passively threads soluble denatured proteins through its central pore.
about
The Symbiotic Performance of Chickpea Rhizobia Can Be Improved by Additional Copies of the clpB Chaperone GeneEscherichia coli ClpB is a non-processive polypeptide translocase.Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.Bi-allelic CLPB mutations cause cataract, renal cysts, nephrocalcinosis and 3-methylglutaconic aciduria, a novel disorder of mitochondrial protein disaggregation.Dynamic structural states of ClpB involved in its disaggregation function.
P2860
ClpB chaperone passively threads soluble denatured proteins through its central pore.
description
2014 nî lūn-bûn
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2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
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2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
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2014年の論文
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年学术文章
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2014年學術文章
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name
ClpB chaperone passively threads soluble denatured proteins through its central pore.
@ast
ClpB chaperone passively threads soluble denatured proteins through its central pore.
@en
ClpB chaperone passively threads soluble denatured proteins through its central pore.
@nl
type
label
ClpB chaperone passively threads soluble denatured proteins through its central pore.
@ast
ClpB chaperone passively threads soluble denatured proteins through its central pore.
@en
ClpB chaperone passively threads soluble denatured proteins through its central pore.
@nl
prefLabel
ClpB chaperone passively threads soluble denatured proteins through its central pore.
@ast
ClpB chaperone passively threads soluble denatured proteins through its central pore.
@en
ClpB chaperone passively threads soluble denatured proteins through its central pore.
@nl
P2860
P356
P1433
P1476
ClpB chaperone passively threads soluble denatured proteins through its central pore.
@en
P2093
Yo-Hei Watanabe
Yosuke Nakazaki
P2860
P304
P356
10.1111/GTC.12188
P577
2014-10-07T00:00:00Z