Preferential substrate binding orientation by the molecular chaperone HscA. (Q44853354)

6 December 2017

title

Preferential substrate binding orientation by the molecular chaperone HscA. (English)

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6 December 2017

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Tim L Tapley

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6 December 2017

Larry E Vickery

series ordinal

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6 December 2017

language of work or name

English

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publication date

20 April 2004

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Journal of Biological Chemistry

6 December 2017

published in

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6 December 2017

volume

279

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6 December 2017

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6 December 2017

page(s)

28435-28442

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A gene encoding a DnaK/hsp70 homolog in Escherichia coli

6 December 2017

cites work

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Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU.

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21 January 2018

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21 January 2018

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

21 January 2018

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Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

21 January 2018

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21 January 2018

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Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

21 January 2018

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IscU as a Scaffold for Iron−Sulfur Cluster Biosynthesis: Sequential Assembly of [2Fe-2S] and [4Fe-4S] Clusters in IscU†

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M400803200

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6 December 2017

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