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pro vyhledávání: '"Scott C. Griffith"'
Publikováno v:
Journal of Biological Chemistry. 277:1058-1065
Proteinl-isoaspartate-(d-aspartate)O-methyltransferases (EC 2.1.1.77), present in a wide variety of prokaryotic and eukaryotic organisms, can initiate the conversion of abnormal l-isoaspartyl residues that arise spontaneously with age to normal l-asp
Autor:
Michael R. Sawaya, Nitika Thapar, Todd O. Yeates, Scott C. Griffith, Daniel R. Boutz, Steven Clarke, Jonathan E. Katz
Publikováno v:
Journal of Molecular Biology. 313:1103-1116
Protein l -isoaspartyl ( d -aspartyl) methyltransferases (EC 2.1.1.77) are found in almost all organisms. These enzymes catalyze the S-adenosylmethionine (AdoMet)-dependent methylation of isomerized and racemized aspartyl residues in age-damaged prot
Autor:
Scott C. Griffith
Publikováno v:
Journal of Experiential Education. 13:41-44
Autor:
Carsten Ryttersgaard, Scott C. Griffith, Duncan C. MacLaren, Todd O. Yeates, Steven Clarke, Michael R. Sawaya
Publikováno v:
The Journal of biological chemistry. 277(12)
The enzyme l-isoaspartyl methyltransferase initiates the repair of damaged proteins by recognizing and methylating isomerized and racemized aspartyl residues in aging proteins. The crystal structure of the human enzyme containing a bound S-adenosyl-l
Publikováno v:
The Journal of biological chemistry. 277(2)
Protein l-isoaspartate-(d-aspartate) O-methyltransferases (EC ), present in a wide variety of prokaryotic and eukaryotic organisms, can initiate the conversion of abnormal l-isoaspartyl residues that arise spontaneously with age to normal l-aspartyl