| Year |
Citation |
Score |
| 2010 |
Salsi E, Campanini B, Bettati S, Raboni S, Roderick SL, Cook PF, Mozzarelli A. A two-step process controls the formation of the bienzyme cysteine synthase complex. The Journal of Biological Chemistry. 285: 12813-22. PMID 20164178 DOI: 10.1074/Jbc.M109.075762 |
0.398 |
|
| 2010 |
Salsi E, Bayden AS, Spyrakis F, Amadasi A, Campanini B, Bettati S, Dodatko T, Cozzini P, Kellogg GE, Cook PF, Roderick SL, Mozzarelli A. Design of O-acetylserine sulfhydrylase inhibitors by mimicking nature. Journal of Medicinal Chemistry. 53: 345-56. PMID 19928859 DOI: 10.1021/Jm901325E |
0.365 |
|
| 2009 |
Pereira MP, Blanchard JE, Murphy C, Roderick SL, Brown ED. High-throughput screening identifies novel inhibitors of the acetyltransferase activity of Escherichia coli GlmU. Antimicrobial Agents and Chemotherapy. 53: 2306-11. PMID 19349513 DOI: 10.1128/Aac.01572-08 |
0.376 |
|
| 2008 |
Guan R, Roderick SL, Huang B, Cook PF. Roles of histidines 154 and 189 and aspartate 139 in the active site of serine acetyltransferase from Haemophilus influenzae. Biochemistry. 47: 6322-8. PMID 18498176 DOI: 10.1021/Bi800075C |
0.37 |
|
| 2007 |
Olsen LR, Vetting MW, Roderick SL. 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. PMID 17473010 DOI: 10.1110/Ps.072779707 |
0.55 |
|
| 2007 |
Andreassi JL, Bilder PW, Vetting MW, Roderick SL, Leyh TS. Crystal structure of the Streptococcus pneumoniae mevalonate kinase in complex with diphosphomevalonate. Protein Science : a Publication of the Protein Society. 16: 983-9. PMID 17400916 DOI: 10.1110/Ps.072755707 |
0.436 |
|
| 2005 |
Campanini B, Speroni F, Salsi E, Cook PF, Roderick SL, Huang B, Bettati S, Mozzarelli A. 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. PMID 15987896 DOI: 10.1110/Ps.051492805 |
0.391 |
|
| 2005 |
Roderick SL. The lac operon galactoside acetyltransferase. Comptes Rendus Biologies. 328: 568-75. PMID 15950163 DOI: 10.1016/J.Crvi.2005.03.005 |
0.415 |
|
| 2005 |
Huang B, Vetting MW, Roderick SL. The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. Journal of Bacteriology. 187: 3201-5. PMID 15838047 DOI: 10.1128/Jb.187.9.3201-3205.2005 |
0.395 |
|
| 2005 |
Vetting MW, De Carvalho LPS, Roderick SL, Blanchard JS. A novel dimeric structure of the RimL Nα-acetyltransferase from Salmonella typhimurium Journal of Biological Chemistry. 280: 22108-22114. PMID 15817456 DOI: 10.1074/Jbc.M502401200 |
0.411 |
|
| 2005 |
Vetting MW, Luiz LP, Yu M, Hegde SS, Magnet S, Roderick SL, Blanchard JS. Structure and functions of the GNAT superfamily of acetyltransferases Archives of Biochemistry and Biophysics. 433: 212-226. PMID 15581578 DOI: 10.1016/J.Abb.2004.09.003 |
0.36 |
|
| 2005 |
Johnson CM, Roderick SL, Cook PF. The serine acetyltransferase reaction: acetyl transfer from an acylpantothenyl donor to an alcohol. Archives of Biochemistry and Biophysics. 433: 85-95. PMID 15581568 DOI: 10.1016/J.Abb.2004.08.014 |
0.385 |
|
| 2004 |
Olsen LR, Huang B, Vetting MW, Roderick SL. Structure of serine acetyltransferase in complexes with CoA and its cysteine feedback inhibitor. Biochemistry. 43: 6013-9. PMID 15147185 DOI: 10.1021/Bi0358521 |
0.526 |
|
| 2004 |
Vetting MW, Magnet S, Nieves E, Roderick SL, Blanchard JS. A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones Chemistry and Biology. 11: 565-573. PMID 15123251 DOI: 10.1016/J.Chembiol.2004.03.017 |
0.41 |
|
| 2003 |
Vetting MW, Roderick SL, Yu M, Blanchard JS. Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases Protein Science. 12: 1954-1959. PMID 12930994 DOI: 10.1110/Ps.03153703 |
0.514 |
|
| 2003 |
Vetting M, Roderick SL, Hegde S, Magnet S, Blanchard JS. What can structure tell us about in vivo function? The case of aminoglycoside-resistance genes. Biochemical Society Transactions. 31: 520-2. PMID 12773148 DOI: 10.1042/Bst0310520 |
0.424 |
|
| 2002 |
Vetting MW, Hegde SS, Javid-Majd F, Blanchard JS, Roderick SL. Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates. Nature Structural Biology. 9: 653-8. PMID 12161746 DOI: 10.1038/Nsb830 |
0.44 |
|
| 2002 |
Roderick SL, Chan WW, Agate DS, Olsen LR, Vetting MW, Rajashankar KR, Cohen DE. Structure of human phosphatidylcholine transfer protein in complex with its ligand. Nature Structural Biology. 9: 507-11. PMID 12055623 DOI: 10.1038/Nsb812 |
0.404 |
|
| 2002 |
Chan WW, Roderick SL, Cohen DE. Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data. Biochimica Et Biophysica Acta. 1596: 1-5. PMID 11983415 DOI: 10.1016/S0167-4838(01)00318-1 |
0.431 |
|
| 2002 |
Wang XG, Olsen LR, Roderick SL. Structure of the lac operon galactoside acetyltransferase. Structure (London, England : 1993). 10: 581-8. PMID 11937062 DOI: 10.1016/S0969-2126(02)00741-4 |
0.452 |
|
| 2002 |
Beaman TW, Vogel KW, Drueckhammer DG, Blanchard JS, Roderick SL. Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase. Protein Science : a Publication of the Protein Society. 11: 974-9. PMID 11910040 DOI: 10.1110/Ps.4310102 |
0.467 |
|
| 2002 |
Sugantino M, Roderick SL. Crystal structure of Vat(D): an acetyltransferase that inactivates streptogramin group A antibiotics. Biochemistry. 41: 2209-16. PMID 11841212 DOI: 10.1021/Bi011991B |
0.655 |
|
| 2001 |
Olsen LR, Roderick SL. Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites Biochemistry. 40: 1913-1921. PMID 11329257 DOI: 10.1021/Bi002503N |
0.528 |
|
| 2001 |
Olsen LR, Tian Y, Roderick SL. Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: A bifunctional acetyltransferase/uridyltransferase Acta Crystallographica Section D: Biological Crystallography. 57: 296-297. PMID 11173485 DOI: 10.1107/S0907444900019119 |
0.54 |
|
| 2000 |
Feng L, Chan WW, Roderick SL, Cohen DE. High-level expression and mutagenesis of recombinant human phosphatidylcholine transfer protein using a synthetic gene: Evidence for a C-terminal membrane binding domain Biochemistry. 39: 15399-15409. PMID 11112525 DOI: 10.1021/Bi001076A |
0.331 |
|
| 2000 |
Sugantino M, Roderick SL. Expression, purification and crystallization of Enterococcus faecium streptogramin A acetyltransferase Acta Crystallographica Section D: Biological Crystallography. 56: 640-642. PMID 10771435 DOI: 10.1107/S0907444900002183 |
0.639 |
|
| 1999 |
Wang XG, Roderick SL. Expression, purification, crystallization and preliminary X-ray data of Escherichia coli galactoside acetyltransferase Acta Crystallographica Section D: Biological Crystallography. 55: 1955-1957. PMID 10531507 DOI: 10.1107/S0907444999011701 |
0.517 |
|
| 1998 |
Beaman TW, Blanchard JS, Roderick SL. The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase. Biochemistry. 37: 10363-9. PMID 9671504 DOI: 10.1021/Bi980759B |
0.374 |
|
| 1998 |
Beaman TW, Sugantino M, Roderick SL. Structure of the hexapeptide xenobiotic acetyltransferase from Pseudomonas aeruginosa Biochemistry. 37: 6689-6696. PMID 9578552 DOI: 10.1021/Bi980106V |
0.658 |
|
| 1997 |
Tian Y, Beaman TW, Roderick SL. Purification and crystallization of Pseudomonas aeruginosa chloramphenicol acetyltransferase Proteins: Structure, Function and Genetics. 28: 298-300. PMID 9188747 DOI: 10.1002/(Sici)1097-0134(199706)28:2<298::Aid-Prot18>3.0.Co;2-D |
0.462 |
|
| 1997 |
Beaman TW, Binder DA, Blanchard JS, Roderick SL. Three-dimensional structure of tetrahydrodipicolinate N- succinyltransferase Biochemistry. 36: 489-494. PMID 9012664 DOI: 10.1021/Bi962522Q |
0.399 |
|
| 1996 |
Binder DA, Blanchard JS, Roderick SL. Crystallization and preliminary crystallographic analysis of tetrahydrodipicolinate-N-succinyltransferase Proteins: Structure, Function and Genetics. 26: 115-117. PMID 8880935 DOI: 10.1002/(Sici)1097-0134(199609)26:1<115::Aid-Prot11>3.0.Co;2-J |
0.45 |
|
| 1995 |
Pfitzner U, Raetz CRH, Roderick SL. Crystallization of UDP-N-acetylglucosamine O-acyltransferase from Escherichia coli Proteins: Structure, Function and Genetics. 22: 191-192. PMID 7567967 DOI: 10.1002/Prot.340220212 |
0.492 |
|
| 1995 |
Raetz CRH, Roderick SL. A left-handed parallel β helix in the structure of UDP-N-acetylglucosamine acyltransferase Science. 270: 997-1000. PMID 7481807 DOI: 10.1126/Science.270.5238.997 |
0.441 |
|
| 1994 |
Bazan JF, Weaver LH, Roderick SL, Huber R, Matthews BW. Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold Proceedings of the National Academy of Sciences of the United States of America. 91: 2473-2477. PMID 8146141 DOI: 10.1073/Pnas.91.7.2473 |
0.341 |
|
| 1993 |
Roderick SL. Structure of the cobalt-dependent methionine aminopeptidase from escherichia coli: A new type of proteolytic enzyme Biochemistry. 32: 3907-3912. PMID 8471602 DOI: 10.1021/Bi00066A009 |
0.363 |
|
| 1990 |
Brennan RG, Roderick SL, Takeda Y, Matthews BW. Protein-DNA conformational changes in the crystal structure of a λ Cro-operator complex Proceedings of the National Academy of Sciences of the United States of America. 87: 8165-8169. PMID 2146682 DOI: 10.1073/Pnas.87.20.8165 |
0.3 |
|
| 1989 |
Roderick SL, Fournie-Zaluski MC, Roques BP, Matthews BW. Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin Biochemistry. 28: 1493-1497. PMID 2719912 DOI: 10.1021/bi00430a011 |
0.302 |
|
| 1988 |
Roderick SL, Matthews BW. Crystallization of methionine aminopeptidase from Escherichia coli Journal of Biological Chemistry. 263: 16531. PMID 3141408 |
0.394 |
|
| 1987 |
Grant PM, Roderick SL, Grant GA, Banaszak LJ, Strauss AW. Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenase. Biochemistry. 26: 128-34. PMID 3828294 DOI: 10.1021/Bi00375A019 |
0.325 |
|
| 1986 |
Roderick SL, Banaszak LJ. The three-dimensional structure of porcine heart mitochondrial malate dehydrogenase at 3.0-A resolution. The Journal of Biological Chemistry. 261: 9461-4. PMID 3722205 |
0.305 |
|
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