Backbone and methyl resonance assignments of the 42 kDa human Hsc70 nucleotide binding domain in the ADP state.

about

Backbone and methyl resonance assignments of the 42 kDa human Hsc70 nucleotide binding domain in the ADP state.

Item

http://www.wikidata.org/entity/Q39325573

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh

2016年學術文章

@zh-hant

name

Backbone and methyl resonance ...... nding domain in the ADP state.

@en

Backbone and methyl resonance ...... nding domain in the ADP state.

@nl

type

Item

label

Backbone and methyl resonance ...... nding domain in the ADP state.

@en

Backbone and methyl resonance ...... nding domain in the ADP state.

@nl

prefLabel

Backbone and methyl resonance ...... nding domain in the ADP state.

@en

Backbone and methyl resonance ...... nding domain in the ADP state.

@nl

P1476

Backbone and methyl resonance ...... nding domain in the ADP state.

@en

P2093

Erik R P Zuiderweg

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

Jason E Gestwicki

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

P2860

Molecular and functional characterization of HSC54, a novel variant of human heat-shock cognate protein 70

Guidelines for the nomenclature of the human heat shock proteins

The nucleotide exchange factors of Hsp70 molecular chaperones

High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70

Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP

Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones

Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

The Amber biomolecular simulation programs

P2888

s12104-016-9711-x

P304

11-15

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

P31

scholarly article

P356

10.1007/S12104-016-9711-X

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

P433

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

P478

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

P577

2016-10-03T00:00:00Z

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

P698

27699616

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

P932

5344757

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