S Clarke

发表

Protein methylation.

S. Clarke, S Clarke, Steven Clarke, 1993, Current opinion in cell biology.

Metabolism of S-adenosyl-L-methionine in intact human erythrocytes.

B H Morimoto, S. Clarke, S Clarke, 1986, Biochimica et Biophysica Acta.

PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells*

H R Herschman, K. Williams, S. Clarke, 2000, The Journal of Biological Chemistry.

Membrane receptors for aspartate and serine in bacterial chemotaxis.

D E Koshland, D. Koshland, S. Clarke, 1979, The Journal of biological chemistry.

Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation.

S. Clarke, T. Geiger, S Clarke, 1987, The Journal of biological chemistry.

S-adenosyl-L-methionine synthetase from human erythrocytes: role in the regulation of cellular S-adenosylmethionine levels.

S. Clarke, K L Oden, S Clarke, 1983, Biochemistry.

Neighboring side chain effects on asparaginyl and aspartyl degradation: an ab initio study of the relationship between peptide conformation and backbone NH acidity.

K N Houk, K. Houk, S. Clarke, 2001, Journal of the American Chemical Society.

Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins.

S. Clarke, R. Stephenson, S Clarke, 1989, The Journal of biological chemistry.

Protein carboxyl methyltransferases: two distinct classes of enzymes.

S. Clarke, S Clarke, 1985, Annual review of biochemistry.

Enzymatic methylation of band 3 anion transporter in intact human erythrocytes.

S. Clarke, L. Lou, S Clarke, 1987, Biochemistry.

RNA and protein interactions modulated by protein arginine methylation.

S. Clarke, S Clarke, J D Gary, 1998, Progress in nucleic acid research and molecular biology.

Chemical modifications of deposited amyloid-beta peptides.

S. Clarke, A. Roher, J. Lowenson, 1999, Methods in enzymology.

Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast.

S. Clarke, S Clarke, H R Kalhor, 2001, Archives of biochemistry and biophysics.

Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease.

M J Ball, M. Ball, I. Reardon, 1993, The Journal of biological chemistry.

beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease.

M J Ball, M. Ball, S. Clarke, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Protein isoprenylation and methylation at carboxyl-terminal cysteine residues.

S. Clarke, S Clarke, 1992, Annual review of biochemistry.

Recognition of D-aspartyl residues in polypeptides by the erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase. Implications for the repair hypothesis.

S. Clarke, J. Lowenson, S Clarke, 1992, The Journal of biological chemistry.