Suramin inhibits Hsp104 ATPase and disaggregase activity

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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity Mechanistic Insights into Hsp104 Potentiation.Engineering therapeutic protein disaggregases.Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.

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Suramin inhibits Hsp104 ATPase and disaggregase activity

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http://www.wikidata.org/entity/Q28543672

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2014 nî lūn-bûn

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2014 թուականին հրատարակուած գիտական յօդուած

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2014 թվականին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Suramin inhibits Hsp104 ATPase and disaggregase activity

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Suramin inhibits Hsp104 ATPase and disaggregase activity

@en

Suramin inhibits Hsp104 ATPase and disaggregase activity

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type

Item

label

Suramin inhibits Hsp104 ATPase and disaggregase activity

@ast

Suramin inhibits Hsp104 ATPase and disaggregase activity

@en

Suramin inhibits Hsp104 ATPase and disaggregase activity

@nl

prefLabel

Suramin inhibits Hsp104 ATPase and disaggregase activity

@ast

Suramin inhibits Hsp104 ATPase and disaggregase activity

@en

Suramin inhibits Hsp104 ATPase and disaggregase activity

@nl

P1476

Suramin inhibits Hsp104 ATPase and disaggregase activity

@en

P2093

Laura M Castellano

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

Mariana P Torrente

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

P2860

A Common Mechanism Underlying Promiscuous Inhibitors from Virtual and High-Throughput Screening

Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion disease

Directed molecular screening for RecA ATPase inhibitors

A current analysis of chemotherapy strategies for the treatment of human African trypanosomiasis

The Trypanocidal Drug Suramin and Other Trypan Blue Mimetics Are Inhibitors of Pyruvate Kinases and Bind to the Adenosine Site

The Molecular Mechanism of Hsp100 Chaperone Inhibition by the Prion Curing Agent Guanidinium Chloride

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

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

HSP104 required for induced thermotolerance.

Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.

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e110115

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scholarly article

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1932491

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10.1371/JOURNAL.PONE.0110115

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P407

English

P433

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

P478

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

P50

James Shorter

P577

2014-01-01T00:00:00Z

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P5875

266682095

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P698

25299406

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P932

4192545

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Suramin inhibits Hsp104 ATPase and disaggregase activity

about

P2860

P2860

Suramin inhibits Hsp104 ATPase and disaggregase activity

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P3181

P356

P407

P433

P478

P50

P577

P5875

P698

P932

P3181

P356

P1433

P1476

P2093

P2860

P304

P31

P3181

P356

P407

P433

P478

P50

P577

P5875

P698

P932