Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation-Reference-Cited by-同舟云学术

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Lysine acetylation can generate highly charged enzymes with increased resistance toward irreversible inactivation

Published:2008-08 Issue:8 Volume:17 Page:1446-1455
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Sci.

Author:

Shaw Bryan F.,Schneider Gregory F.,Bilgiçer Başar,Kaufman George K.,Neveu John M.,Lane William S.,Whitelegge Julian P.,Whitesides George M.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference58 articles.

1. Correlation of electrophoretic mobilities of proteins and peptides with their physicochemical properties;Basak;Anal. Biochem.,1995

2. Correlations between the charge of proteins and the number of ionizable groups they incorporate: Studies using protein charge ladders, capillary electrophoresis, and Debye-Huckel theory;Carbeck;J. Am. Chem. Soc.,1999

3. Protein misfolding, functional amyloid, and human disease;Chiti;Annu. Rev. Biochem.,2006

4. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases;Chiti;Proc. Natl. Acad. Sci.,2002

5. Rationalization of the effects of mutations on peptide and protein aggregation rates;Chiti;Nature,2003

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