(Q27732843)

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Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

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Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis (English)

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M C O'Brien

1

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K M Flaherty

series ordinal

2

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D B McKay

series ordinal

3

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language of work or name

English

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publication date

5 July 1996

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published in

Journal of Biological Chemistry

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volume

271

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issue

27

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page(s)

15874-8

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cites work

Protein folding in the cell

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https://api.crossref.org/works/10.1074%2FJBC.271.27.15874

retrieved

21 January 2018

An enzyme that removes clathrin coats: purification of an uncoating ATPase

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https://api.crossref.org/works/10.1074%2FJBC.271.27.15874

retrieved

21 January 2018

Hsc70-binding peptides selected from a phage display peptide library that resemble organellar targeting sequences

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.271.27.15874

retrieved

21 January 2018

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

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https://api.crossref.org/works/10.1074%2FJBC.271.27.15874

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21 January 2018

DNA sequencing with chain-terminating inhibitors

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https://api.crossref.org/works/10.1074%2FJBC.271.27.15874

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21 January 2018

Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis

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21 January 2018

A graphics model building and refinement system for macromolecules

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21 January 2018

Crystallographic R factor refinement by molecular dynamics

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21 January 2018

ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.

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21 January 2018

How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity

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21 January 2018

Peptide-binding specificity of the molecular chaperone BiP

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21 January 2018

Identifiers

DOI

10.1074/JBC.271.27.15874

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PubMed ID

8663302

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ResearchGate publication ID

14538197

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(Q27732843)

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

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