Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone. (Q30857728)

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5 November 2019

title

Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone (English)

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5 November 2019

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1

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5 November 2019

author name string

Jakob U

series ordinal

2

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5 November 2019

Glocker MO

series ordinal

3

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5 November 2019

language of work or name

English

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publication date

1 June 2000

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Journal of Biological Chemistry

5 November 2019

published in

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5 November 2019

volume

275

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5 November 2019

issue

25

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5 November 2019

page(s)

18759-18766

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Chaperone activity with a redox switch

5 November 2019

cites work

1 reference

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Assignment of the inter- and intramolecular disulfide linkages in recombinant human macrophage colony stimulating factor using fast atom bombardment mass spectrometry.

21 January 2018

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Characterization of disulfide linkages and disulfide bond scrambling in recombinant human macrophage colony stimulating factor by fast-atom bombardment mass spectrometry of enzymatic digests

21 January 2018

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Selective bridging of bis-cysteinyl residues by arsonous acid derivatives as an approach to the characterization of protein tertiary structures and folding pathways by mass spectrometry

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Biochemical characterization and mass spectrometric disulfide bond mapping of periplasmic alpha-amylase MalS of Escherichia coli.

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Disulfide linkages in the in vitro refolded intermediates of recombinant human macrophage-colony-stimulating factor: analysis of the sulfhydryl alkylation of free cysteine residues by fast-atom bombardment mass spectrometry

21 January 2018

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The complete amino acid sequence and disulphide bond arrangement of oat alcohol-soluble avenin-3.

21 January 2018

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Folding of firefly (Photinus pyralis) luciferase: aggregation and reactivation of unfolding intermediates

21 January 2018

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Activation of the OxyR transcription factor by reversible disulfide bond formation

21 January 2018

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Facile, in situ matrix-assisted laser desorption ionization-mass spectrometry analysis and assignment of disulfide pairings in heteropeptide molecules

21 January 2018

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Prompt fragmentation of disulfide-linked peptides during matrix-assisted laser desorption ionization mass spectrometry

21 January 2018

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Bridge over troubled waters: sensing stress by disulfide bond formation

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2 Thiol/disulfide exchange equilibria and disulfidebond stability

21 January 2018

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Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation

21 January 2018

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A novel regulatory switch mediated by the FNR-like protein of Lactobacillus casei

21 January 2018

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RsrA, an anti-sigma factor regulated by redox change

21 January 2018

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Reactivities of the cysteine residues of the reduced pancreatic trypsin inhibitor

21 January 2018

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Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M001089200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10764757%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

1 reference