Mass Spectrometry Unravels Disulfide Bond Formation as the Mechanism That Activates a Molecular Chaperone
Open Access
- 1 June 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (25) , 18759-18766
- https://doi.org/10.1074/jbc.m001089200
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Bridge over Troubled WatersCell, 1999
- A novel regulatory switch mediated by the FNR-like protein of Lactobacillus caseiMicrobiology, 1998
- Biochemical Characterization and Mass Spectrometric Disulfide Bond Mapping of Periplasmic α-Amylase MalS of Escherichia coliJournal of Biological Chemistry, 1997
- Effect of Nucleotides, Peptides, and Unfolded Proteins on the Self-association of the Molecular Chaperone HSC70Journal of Biological Chemistry, 1996
- A method for counting disulfide bridges in small proteins by reduction with mercaptoethanol and electrospray mass spectrometryJournal of Mass Spectrometry, 1995
- Prompt Fragmentation of Disulfide-Linked Peptides during Matrix-Assisted Laser Desorption Ionization Mass SpectrometryAnalytical Chemistry, 1994
- The Complete Amino Acid Sequence and Disulphide Bond Arrangement of Oat Alcohol‐soluble Avenin‐3European Journal of Biochemistry, 1994
- Cleavage of interchain disulfide bonds following matrix-assisted laser desorptionInternational Journal of Mass Spectrometry and Ion Processes, 1993
- Chemistry of sulfenic acids. 7. Reason for the high reactivity of sulfenic acids. Stabilization by intramolecular hydrogen bonding and electronegativity effectsThe Journal of Organic Chemistry, 1986
- Reactivities of the cysteine residues of the reduced pancreatic trypsin inhibitorJournal of Molecular Biology, 1975