Steven G. Clarke
Steven G. Clarke
Professor of Chemistry and Biochemistry, UCLA
Verified email at - Homepage
Cited by
Cited by
Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1
DJ Klionsky, AK Abdel-Aziz, S Abdelfatah, M Abdellatif, A Abdoli, S Abel, ...
autophagy 17 (1), 1-382, 2021
Protein arginine methylation in mammals: who, what, and why
MT Bedford, SG Clarke
Molecular cell 33 (1), 1-13, 2009
Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation.
T Geiger, S Clarke
Journal of Biological Chemistry 262 (2), 785-794, 1987
Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
S Clarke
Annual review of biochemistry 61 (1), 355-386, 1992
Human PAD4 regulates histone arginine methylation levels via demethylimination
Y Wang, J Wysocka, J Sayegh, YH Lee, JR Perlin, L Leonelli, ...
Science 306 (5694), 279-283, 2004
Structural alterations in the peptide backbone of beta-amyloid core protein may account for its deposition and stability in Alzheimer's disease.
AE Roher, JD Lowenson, S Clarke, C Wolkow, R Wang, RJ Cotter, ...
Journal of Biological Chemistry 268 (5), 3072-3083, 1993
beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease.
AE Roher, JD Lowenson, S Clarke, AS Woods, RJ Cotter, E Gowing, ...
Proceedings of the National Academy of Sciences 90 (22), 10836-10840, 1993
RNA and protein interactions modulated by protein arginine methylation
JD Gary, S Clarke
Progress in nucleic acid research and molecular biology 61, 65-131, 1998
Succinimide formation from aspartyl and asparaginyl peptides as a model for the spontaneous degradation of proteins
RC Stephenson, S Clarke
Journal of Biological Chemistry 264 (11), 6164-6170, 1989
Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
RM Kagan, S Clarke
Archives of biochemistry and biophysics 310 (2), 417-427, 1994
The size and detergent binding of membrane proteins.
S Clarke
Journal of Biological Chemistry 250 (14), 5459-5469, 1975
The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
WJ Lin, JD Gary, MC Yang, S Clarke, HR Herschman
Journal of Biological Chemistry 271 (25), 15034-15044, 1996
Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases.
S Clarke, JP Vogel, RJ Deschenes, J Stock
Proceedings of the National Academy of Sciences 85 (13), 4643-4647, 1988
PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells
J Tang, A Frankel, RJ Cook, S Kim, WK Paik, KR Williams, S Clarke, ...
Journal of Biological Chemistry 275 (11), 7723-7730, 2000
PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
TL Branscombe, A Frankel, JH Lee, JR Cook, Z Yang, S Pestka, S Clarke
Journal of Biological Chemistry 276 (35), 32971-32976, 2001
Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteins
S Clarke
International journal of peptide and protein research 30 (6), 808-821, 1987
The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
A Frankel, N Yadav, J Lee, TL Branscombe, S Clarke, MT Bedford
Journal of Biological Chemistry 277 (5), 3537-3543, 2002
Protein carboxyl methyltransferases: two distinct classes of enzymes
S Clarke
Annual review of biochemistry 54 (1), 479-506, 1985
PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation
J Tang, JD Gary, S Clarke, HR Herschman
Journal of Biological Chemistry 273 (27), 16935-16945, 1998
Protein methylation
S Clarke
Current opinion in cell biology 5 (6), 977-983, 1993
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