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Biochemical and Biophysical Research Communications|November 15, 1985
Specific recognition of altered polypeptides by widely distributed methyltransferasesC M O'Connor, S ClarkeThe Journal of Biological Chemistry|February 25, 1984
Carboxyl methylation of cytosolic proteins in intact human erythrocytes. Identification of numerous methyl-accepting proteins including hemoglobin and carbonic anhydraseC M O'Connor, S ClarkeAnalytical Biochemistry|July 1, 1985
Analysis of erythrocyte protein methyl esters by two-dimensional gel electrophoresis under acidic separating conditionsC M O'Connor, S ClarkeThe Journal of Biological Chemistry|July 10, 1983
Methylation of erythrocyte membrane proteins at extracellular and intracellular D-aspartyl sites in vitro. Saturation of intracellular sites in vivoC M O'Connor, S ClarkeProceedings of the National Academy of Sciences of the United States of America|December 1, 1984
Mammalian brain and erythrocyte carboxyl methyltransferases are similar enzymes that recognize both D-aspartyl and L-isoaspartyl residues in structurally altered protein substratesC M O'Connor, D W Aswad, S ClarkeThe Journal of Biological Chemistry|July 25, 1987
Regulation and subcellular distribution of a protein methyltransferase and its damaged aspartyl substrate sites in developing Xenopus oocytesC M O'ConnorMolecular Reproduction and Development|December 1, 1994
Analysis of aspartic acid and asparagine metabolism in Xenopus laevis oocytes using a simple and sensitive HPLC methodC M O'ConnorJournal of Vascular Nursing : Official Publication of the Society for Peripheral Vascular Nursing|September 5, 2001
Raynaud's phenomenonC M O'connorGenomics|December 1, 1992
The L-isoaspartyl/D-aspartyl protein methyltransferase gene (PCMT1) maps to human chromosome 6q22.3-6q24 and the syntenic region of mouse chromosome 10D C MacLaren, C M O'Connor, Y R Xia, et al.Drugs|September 26, 2000
[Calcium antagonists in the treatment of heart failure. Re-evaluation of therapeutic strategies]W Gattis, C M O'ConnorPageof 101