Functional coevolutionary networks of the Hsp70-Hop-Hsp90 system revealed through computational analyses (Q56898426)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17267421%20AND%20SRC:MED&resulttype=core&format=json

25 December 2019

title

Functional coevolutionary networks of the Hsp70-Hop-Hsp90 system revealed through computational analyses (English)

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25 December 2019

2

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25 December 2019

author name string

Simon A A Travers

series ordinal

1

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25 December 2019

language of work or name

English

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publication date

30 January 2007

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Molecular Biology and Evolution

25 December 2019

published in

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25 December 2019

volume

24

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25 December 2019

issue

4

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25 December 2019

page(s)

1032-1044

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The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically

25 December 2019

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Mutual information in protein multiple sequence alignments reveals two classes of coevolving positions.

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

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Nuclear translocation of the Hsp70/Hsp90 organizing protein mSTI1 is regulated by cell cycle kinases.

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Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

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Hop: more than an Hsp70/Hsp90 adaptor protein

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21 January 2018

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Identifiers

DOI

10.1093/MOLBEV/MSM022

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17267421%20AND%20SRC:MED&resulttype=core&format=json

25 December 2019

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