Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

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Comparative Analysis of the Structure and Function of AAA+ Motors ClpA, ClpB, and Hsp104: Common Threads and Disparate Functions.

P2860

Q41220996-7AB5A457-CDA1-4962-AFAA-F04995E1B5EF

P2860

Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

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http://www.wikidata.org/entity/Q42380663

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2017 nî lūn-bûn

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2017年の論文

@ja

2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

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2017年論文

@zh-tw

2017年论文

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2017年论文

@zh

2017年论文

@zh-cn

name

Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

@en

Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

@nl

type

Item

label

Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

@en

Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

@nl

prefLabel

Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

@en

Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

@nl

P1476

Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures

@en

P2093

Clarissa L Weaver

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

Elizabeth A Sweeny

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

Elizabeth C Duran

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

JiaBei Lin

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

Korrie L Mack

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

P2860

Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease

The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state

Structure and mechanism of the hexameric MecA-ClpC molecular machine

Elements in nucleotide sensing and hydrolysis of the AAA+ disaggregation machine ClpB: a structure-based mechanistic dissection of a molecular motor

Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation

Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides.

Protein disaggregation mediated by heat-shock protein Hsp104.

AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes

P304

2071-2075

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scholarly article

P356

10.1021/ACS.BIOCHEM.7B00225

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

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English

P433

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

P478

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

P50

James Shorter

Aaron L. Lucius

Meredith Jackrel

P577

2017-04-10T00:00:00Z

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28379007

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P932

5649362

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Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

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P2860

P2860

Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932