Allosteric disulfides: Sophisticated molecular structures enabling flexible protein regulation
نویسندگان
چکیده
منابع مشابه
Identification of allosteric disulfides from labile bonds in X-ray structures
Protein disulfide bonds link pairs of cysteine sulfur atoms and are either structural or functional motifs. The allosteric disulfides control the function of the protein in which they reside when cleaved or formed. Here, we identify potential allosteric disulfides in all Protein Data Bank X-ray structures from bonds that are present in some molecules of a protein crystal but absent in others, o...
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29 Roche, P. C., Ryan, R. J. and McCormick, D. J. (1992) Endocrinology (Baltimore) 131,268-274 Atassi, M. Z., Manshouri, T. and Sakata, S. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 3613-3617 Dattatreyamurty, B. and Reichert, L. E., Jr. (1992) Mol. Cell. Endocrinol. 87, 917 Acher, R. (1993) Regul. Pept. 45, 1-13 Yamano, Y., Ohyama, K., Chaki, S., Guo, D.-F. and Inagami, T. (1992) Riochem. Biophys...
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The redox state of cellular thiols is widely studied because it was recently linked to many different diseases and pathologies. In this work we quantified the concentrations of protein disulfides (PSSP) and thiol-protein mixed disulfides (XSSP) in rat tissues (liver, kidney and heart) and cells (Raw 264.7) by an improved method of XSSP and PSSP determination after oxidative stress induced by di...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2019
ISSN: 0021-9258
DOI: 10.1074/jbc.rev118.005604