The Function of Ile-X-Ile Motif in the Oligomerization and Chaperone-Like Activity of Small Heat Shock Protein AgsA at Room Temperature.

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The Function of Ile-X-Ile Motif in the Oligomerization and Chaperone-Like Activity of Small Heat Shock Protein AgsA at Room Temperature.

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

@zh-hans

2016年学术文章

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2016年学术文章

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2016年學術文章

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2016年學術文章

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name

The Function of Ile-X-Ile Moti ...... tein AgsA at Room Temperature.

@en

The Function of Ile-X-Ile Moti ...... tein AgsA at Room Temperature.

@nl

type

Item

label

The Function of Ile-X-Ile Moti ...... tein AgsA at Room Temperature.

@en

The Function of Ile-X-Ile Moti ...... tein AgsA at Room Temperature.

@nl

prefLabel

The Function of Ile-X-Ile Moti ...... tein AgsA at Room Temperature.

@en

The Function of Ile-X-Ile Moti ...... tein AgsA at Room Temperature.

@nl

P1476

The Function of Ile-X-Ile Moti ...... tein AgsA at Room Temperature.

@en

P2093

Chao Shi

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

Kaiming Zhang

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

Lixin Huang

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

Qiuhu Zhou

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

Xiaodong Shi

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

Zhenzhan Chang

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

P2860

Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif

A new heat shock gene, AgsA, which encodes a small chaperone involved in suppressing protein aggregation in Salmonella enterica serovar typhimurium

Crystal structure and assembly of a eukaryotic small heat shock protein

Changes in the quaternary structure and function of MjHSP16.5 attributable to deletion of the IXI motif and introduction of the substitution, R107G, in the -crystallin domain

Crystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5

Crystal structure of a small heat-shock protein

Influence of the C-terminal residues on oligomerization of alpha A-crystallin

Investigation of the chaperone function of the small heat shock protein-AgsA.

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state.

P2888

s10930-016-9681-y

P304

401-406

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P31

scholarly article

P356

10.1007/S10930-016-9681-Y

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

P433

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

P478

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

P577

2016-11-04T00:00:00Z

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

P698

27812886

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

P921

molecular chaperones