Biochemical characterization of the small heat shock protein IbpB from Escherichia coli. (Q33857365)

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3 December 2019

title

Biochemical characterization of the small heat shock protein IbpB from Escherichia coli (English)

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3 December 2019

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1

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3 December 2019

author name string

F Baneyx

series ordinal

2

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3 December 2019

language of work or name

English

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publication date

1 April 1999

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Journal of Biological Chemistry

3 December 2019

published in

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volume

274

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3 December 2019

issue

15

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3 December 2019

page(s)

9937-9945

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Molecular chaperones and protein folding in plants

3 December 2019

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Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation

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A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein

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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

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Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

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Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli

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Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli.

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The small heat-shock protein, αb-crystallin, has a variable quaternary structure

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.274.15.9937

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10187768%20AND%20SRC:MED&resulttype=core&format=json

3 December 2019

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