A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase. (Q54603426)

1 June 2018

title

A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase. (English)

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1 June 2018

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de Crouy-Chanel A

1

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Kohiyama M

series ordinal

2

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1 June 2018

Richarme G

series ordinal

3

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language of work or name

English

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publication date

1 September 1995

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1 June 2018

Journal of Biological Chemistry

number of pages

4

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based on heuristic

inferred from page(s)

published in

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volume

270

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issue

39

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page(s)

22669-22672

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Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures

cites work

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Molecular chaperone functions of heat-shock proteins

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Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins

21 January 2018

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Identification of a protein required for disulfide bond formation in vivo

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Building bridges: disulphide bond formation in the cell

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Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.

21 January 2018

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Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate

21 January 2018

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The Escherichia coli heat shock gene htpY: mutational analysis, cloning, sequencing, and transcriptional regulation

21 January 2018

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Thioredoxin-catalyzed refolding of disulfide-containing proteins

21 January 2018

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Eukaryotic DnaJ homologs and the specificity of Hsp70 activity

21 January 2018

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Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo

21 January 2018

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DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli

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Isolation and characterization of dnaJ null mutants of Escherichia coli

21 January 2018

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Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant.

21 January 2018

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.270.39.22669

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1 June 2018

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1 June 2018