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Fucci, L., Oliver, C. N., Coon, M. J., Stadtman, E. R. (1983) Inactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implication in protein turnover and ageing. Proceedings of the National Academy of Sciences, 80 (6) 1521-1525 doi:10.1073/pnas.80.6.1521

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Reference TypeJournal (article/letter/editorial)
TitleInactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implication in protein turnover and ageing
JournalProceedings of the National Academy of Sciences
AuthorsFucci, L.Author
Oliver, C. N.Author
Coon, M. J.Author
Stadtman, E. R.Author
Year1983 (March 1)Volume80
Issue6
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.80.6.1521Search in ResearchGate
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Mindat Ref. ID1432961Long-form Identifiermindat:1:5:1432961:4
GUID0
Full ReferenceFucci, L., Oliver, C. N., Coon, M. J., Stadtman, E. R. (1983) Inactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implication in protein turnover and ageing. Proceedings of the National Academy of Sciences, 80 (6) 1521-1525 doi:10.1073/pnas.80.6.1521
Plain TextFucci, L., Oliver, C. N., Coon, M. J., Stadtman, E. R. (1983) Inactivation of key metabolic enzymes by mixed-function oxidation reactions: Possible implication in protein turnover and ageing. Proceedings of the National Academy of Sciences, 80 (6) 1521-1525 doi:10.1073/pnas.80.6.1521
In(1983, March) Proceedings of the National Academy of Sciences Vol. 80 (6) Proceedings of the National Academy of Sciences

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Levine, R. L., Oliver, C. N., Fulks, R. M., Stadtman, E. R. (1981) Turnover of bacterial glutamine synthetase: oxidative inactivation precedes proteolysis. Proceedings of the National Academy of Sciences, 78 (4) 2120-2124 doi:10.1073/pnas.78.4.2120
Oliver, C. N., Stadtman, E. R. (1983) A proteolytic artifact associated with the lysis of bacteria by egg white lysozyme. Proceedings of the National Academy of Sciences, 80 (8) 2156-2160 doi:10.1073/pnas.80.8.2156
Smith, C. D., Carney, J. M., Starke-Reed, P. E., Oliver, C. N., Stadtman, E. R., Floyd, R. A., Markesbery, W. R. (1991) Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. Proceedings of the National Academy of Sciences, 88 (23) 10540-10543 doi:10.1073/pnas.88.23.10540
Chao, C.-C., Ma, Y.-S., Stadtman, E. R. (1997) Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems. Proceedings of the National Academy of Sciences, 94 (7) 2969-2974 doi:10.1073/pnas.94.7.2969
Brown, M. S., Segal, A., Stadtman, E. R. (1971) Modulation of Glutamine Synthetase Adenylylation and Deadenylylation Is Mediated by Metabolic Transformation of the PII-Regulatory Protein. Proceedings of the National Academy of Sciences, 68 (12) 2949-2953 doi:10.1073/pnas.68.12.2949
Nakamura, K., Stadtman, E. R. (1984) Oxidative inactivation of glutamine synthetase subunits. Proceedings of the National Academy of Sciences, 81 (7) 2011-2015 doi:10.1073/pnas.81.7.2011
Scallen, T. J., Sanghvi, A. (1983) Regulation of three key enzymes in cholesterol metabolism by phosphorylation/dephosphorylation. Proceedings of the National Academy of Sciences, 80 (9) 2477-2480 doi:10.1073/pnas.80.9.2477
Moskovitz, J., Stadtman, E. R. (2003) Selenium-deficient diet enhances protein oxidation and affects methionine sulfoxide reductase (MsrB) protein level in certain mouse tissues. Proceedings of the National Academy of Sciences, 100 (13) 7486-7490 doi:10.1073/pnas.1332607100
Goodman, D. B., Davis, W. L., Jones, R. G. (1980) Glyoxylate cycle in toad urinary bladder: possible stimulation by aldosterone. Proceedings of the National Academy of Sciences, 77 (3) 1521-1525 doi:10.1073/pnas.77.3.1521
Niedel, J. E., Kuhn, L. J., Vandenbark, G. R. (1983) Phorbol diester receptor copurifies with protein kinase C. Proceedings of the National Academy of Sciences, 80 (1) 36-40 doi:10.1073/pnas.80.1.36
Requena, J. R., Groth, D., Legname, G., Stadtman, E. R., Prusiner, S. B., Levine, R. L. (2001) Copper-catalyzed oxidation of the recombinant SHa(29-231) prion protein. Proceedings of the National Academy of Sciences, 98 (13) 7170-7175 doi:10.1073/pnas.121190898
 
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