Steven L. Roderick

Affiliations: 
Yeshiva University, New York, NY, United States 
Area:
Biochemistry
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"Steven Roderick"
Mean distance: 19906.5
 
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Publications

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Salsi E, Campanini B, Bettati S, et al. (2010) A two-step process controls the formation of the bienzyme cysteine synthase complex. The Journal of Biological Chemistry. 285: 12813-22
Salsi E, Bayden AS, Spyrakis F, et al. (2010) Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature. Journal of Medicinal Chemistry. 53: 345-56
Pereira MP, Blanchard JE, Murphy C, et al. (2009) High-throughput screening identifies novel inhibitors of the acetyltransferase activity of Escherichia coli GlmU. Antimicrobial Agents and Chemotherapy. 53: 2306-11
Guan R, Roderick SL, Huang B, et al. (2008) Roles of histidines 154 and 189 and aspartate 139 in the active site of serine acetyltransferase from Haemophilus influenzae. Biochemistry. 47: 6322-8
Olsen LR, Vetting MW, Roderick SL. (2007) Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products. Protein Science : a Publication of the Protein Society. 16: 1230-5
Andreassi JL, Bilder PW, Vetting MW, et al. (2007) Crystal structure of the Streptococcus pneumoniae mevalonate kinase in complex with diphosphomevalonate. Protein Science : a Publication of the Protein Society. 16: 983-9
Campanini B, Speroni F, Salsi E, et al. (2005) Interaction of serine acetyltransferase with O-acetylserine sulfhydrylase active site: evidence from fluorescence spectroscopy. Protein Science : a Publication of the Protein Society. 14: 2115-24
Roderick SL. (2005) The lac operon galactoside acetyltransferase. Comptes Rendus Biologies. 328: 568-75
Huang B, Vetting MW, Roderick SL. (2005) The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. Journal of Bacteriology. 187: 3201-5
Vetting MW, De Carvalho LPS, Roderick SL, et al. (2005) A novel dimeric structure of the RimL Nα-acetyltransferase from Salmonella typhimurium Journal of Biological Chemistry. 280: 22108-22114
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