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Richard N. Armstrong, Ph.D. - Publications

Affiliations: 
1995-2015 Chemistry Vanderbilt University, Nashville, TN 
Area:
Biochemistry, Mechanistic Enzymology
Website:
http://www.vanderbilt.edu/chemistry/faculty/armstrong.php
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91 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2017 Droege KD, Keithly ME, Sanders CR, Armstrong RN, Thompson MK. Structural Dynamics of 15-Lipoxygenase-2 via Hydrogen Deuterium Exchange. Biochemistry. PMID 28809482 DOI: 10.1021/Acs.Biochem.7B00559  0.356
2017 Spahiu L, Ålander J, Ottosson-Wadlund A, Svensson R, Lehmer C, Armstrong RN, Morgenstern R. Global Kinetic Mechanism of Microsomal Glutathione Transferase 1, insights into dynamic enzyme activation. Biochemistry. PMID 28558199 DOI: 10.1021/Acs.Biochem.7B00285  0.401
2016 Raouf J, Rafique N, Goodman MC, Idborg H, Bergqvist F, Armstrong RN, Jakobsson PJ, Morgenstern R, Spahiu L. Arg126 and Asp49 Are Essential for the Catalytic Function of Microsomal Prostaglandin E2 Synthase 1 and Ser127 Is Not. Plos One. 11: e0163600. PMID 27684486 DOI: 10.1371/Journal.Pone.0163600  0.38
2015 Shen J, Keithly ME, Armstrong RN, Higgins KA, Edmonds KA, Giedroc DP. Staphylococcus aureus CstB Is a Novel Multidomain Persulfide Dioxygenase-Sulfurtransferase Involved in Hydrogen Sulfide Detoxification. Biochemistry. 54: 4542-54. PMID 26177047 DOI: 10.1021/Acs.Biochem.5B00584  0.365
2015 Thompson MK, Keithly ME, Sulikowski GA, Armstrong RN. Diversity in fosfomycin resistance proteins Perspectives in Science. 4: 17-23. DOI: 10.1016/J.Pisc.2014.12.004  0.424
2014 Dong GQ, Calhoun S, Fan H, Kalyanaraman C, Branch MC, Mashiyama ST, London N, Jacobson MP, Babbitt PC, Shoichet BK, Armstrong RN, Sali A. Prediction of substrates for glutathione transferases by covalent docking. Journal of Chemical Information and Modeling. 54: 1687-99. PMID 24802635 DOI: 10.1021/Ci5001554  0.682
2014 Mashiyama ST, Malabanan MM, Akiva E, Bhosle R, Branch MC, Hillerich B, Jagessar K, Kim J, Patskovsky Y, Seidel RD, Stead M, Toro R, Vetting MW, Almo SC, Armstrong RN, et al. Large-scale determination of sequence, structure, and function relationships in cytosolic glutathione transferases across the biosphere. Plos Biology. 12: e1001843. PMID 24756107 DOI: 10.1371/Journal.Pbio.1001843  0.752
2014 Thompson MK, Keithly ME, Goodman MC, Hammer ND, Cook PD, Jagessar KL, Harp J, Skaar EP, Armstrong RN. Structure and function of the genomically encoded fosfomycin resistance enzyme, FosB, from Staphylococcus aureus. Biochemistry. 53: 755-65. PMID 24447055 DOI: 10.1021/bi4015852  0.403
2014 Tipton KF, Armstrong RN, Bakker BM, Bairoch A, Cornish-Bowden A, Halling PJ, Hofmeyr J, Leyh TS, Kettner C, Raushel FM, Rohwer J, Schomburg D, Steinbeck C. Standards for Reporting Enzyme Data: The STRENDA Consortium: What it aims to do and why it should be helpful Perspectives in Science. 1: 131-137. DOI: 10.1016/J.Pisc.2014.02.012  0.339
2013 Thompson MK, Keithly ME, Harp J, Cook PD, Jagessar KL, Sulikowski GA, Armstrong RN. Structural and chemical aspects of resistance to the antibiotic fosfomycin conferred by FosB from Bacillus cereus. Biochemistry. 52: 7350-62. PMID 24004181 DOI: 10.1021/Bi4009648  0.405
2012 Lamers AP, Keithly ME, Kim K, Cook PD, Stec DF, Hines KM, Sulikowski GA, Armstrong RN. Synthesis of bacillithiol and the catalytic selectivity of FosB-type fosfomycin resistance proteins. Organic Letters. 14: 5207-9. PMID 23030527 DOI: 10.1021/Ol302327T  0.316
2012 Prage EB, Morgenstern R, Jakobsson PJ, Stec DF, Voehler MW, Armstrong RN. Observation of two modes of inhibition of human microsomal prostaglandin E synthase 1 by the cyclopentenone 15-deoxy-Δ(12,14)-prostaglandin J(2). Biochemistry. 51: 2348-56. PMID 22356188 DOI: 10.1021/Bi2019332  0.721
2012 Preininger AM, Kaya AI, Gilbert JA, Busenlehner LS, Armstrong RN, Hamm HE. Myristoylation exerts direct and allosteric effects on Gα conformation and dynamics in solution. Biochemistry. 51: 1911-24. PMID 22329346 DOI: 10.1021/Bi201472C  0.378
2011 Gerlt JA, Allen KN, Almo SC, Armstrong RN, Babbitt PC, Cronan JE, Dunaway-Mariano D, Imker HJ, Jacobson MP, Minor W, Poulter CD, Raushel FM, Sali A, Shoichet BK, Sweedler JV. The Enzyme Function Initiative. Biochemistry. 50: 9950-62. PMID 21999478 DOI: 10.1021/Bi201312U  0.374
2011 Prage EB, Pawelzik SC, Busenlehner LS, Kim K, Morgenstern R, Jakobsson PJ, Armstrong RN. Location of inhibitor binding sites in the human inducible prostaglandin E synthase, MPGES1. Biochemistry. 50: 7684-93. PMID 21805999 DOI: 10.1021/Bi2010448  0.735
2011 Stourman NV, Branch MC, Schaab MR, Harp JM, Ladner JE, Armstrong RN. Structure and function of YghU, a nu-class glutathione transferase related to YfcG from Escherichia coli. Biochemistry. 50: 1274-81. PMID 21222452 DOI: 10.1021/Bi101861A  0.697
2010 Wadington MC, Ladner JE, Stourman NV, Harp JM, Armstrong RN. Correction to Analysis of the Structure and Function of YfcG fromEscherichia coliReveals an Efficient and Unique Disulfide Bond Reductase Biochemistry. 49: 10765-10765. DOI: 10.1021/Bi101851X  0.31
2009 Wadington MC, Ladner JE, Stourman NV, Harp JM, Armstrong RN. Analysis of the structure and function of YfcG from Escherichia coli reveals an efficient and unique disulfide bond reductase. Biochemistry. 48: 6559-61. PMID 19537707 DOI: 10.1021/Bi9008825  0.449
2009 Alander J, Lengqvist J, Holm PJ, Svensson R, Gerbaux P, Heuvel RH, Hebert H, Griffiths WJ, Armstrong RN, Morgenstern R. Microsomal glutathione transferase 1 exhibits one-third-of-the-sites-reactivity towards glutathione. Archives of Biochemistry and Biophysics. 487: 42-8. PMID 19416719 DOI: 10.1016/J.Abb.2009.04.009  0.437
2008 Kinsley N, Sayed Y, Mosebi S, Armstrong RN, Dirr HW. Characterization of the binding of 8-anilinonaphthalene sulfonate to rat class Mu GST M1-1. Biophysical Chemistry. 137: 100-4. PMID 18703268 DOI: 10.1016/J.Bpc.2008.07.008  0.397
2008 Busenlehner LS, Brändén G, Namslauer I, Brzezinski P, Armstrong RN. Structural elements involved in proton translocation by cytochrome c oxidase as revealed by backbone amide hydrogen-deuterium exchange of the E286H mutant. Biochemistry. 47: 73-83. PMID 18052347 DOI: 10.1021/Bi701643A  0.394
2007 Fillgrove KL, Pakhomova S, Schaab MR, Newcomer ME, Armstrong RN. Structure and mechanism of the genomically encoded fosfomycin resistance protein, FosX, from Listeria monocytogenes. Biochemistry. 46: 8110-20. PMID 17567049 DOI: 10.1021/Bi700625P  0.49
2007 Rigsby RE, Brown DW, Dawson E, Lybrand TP, Armstrong RN. A model for glutathione binding and activation in the fosfomycin resistance protein, FosA. Archives of Biochemistry and Biophysics. 464: 277-83. PMID 17537395 DOI: 10.1016/J.Abb.2007.04.035  0.491
2007 Thompson LC, Ladner JE, Codreanu SG, Harp J, Gilliland GL, Armstrong RN. 2-Hydroxychromene-2-carboxylic acid isomerase: a kappa class glutathione transferase from Pseudomonas putida. Biochemistry. 46: 6710-22. PMID 17508726 DOI: 10.1021/Bi700356U  0.701
2007 Busenlehner LS, Alander J, Jegerscöhld C, Holm PJ, Bhakat P, Hebert H, Morgenstern R, Armstrong RN. Location of substrate binding sites within the integral membrane protein microsomal glutathione transferase-1. Biochemistry. 46: 2812-22. PMID 17297922 DOI: 10.1021/Bi6023385  0.513
2006 Busenlehner LS, Salomonsson L, Brzezinski P, Armstrong RN. Mapping protein dynamics in catalytic intermediates of the redox-driven proton pump cytochrome c oxidase. Proceedings of the National Academy of Sciences of the United States of America. 103: 15398-403. PMID 17023543 DOI: 10.1073/Pnas.0601451103  0.338
2006 Thompson LC, Walters J, Burke J, Parsons JF, Armstrong RN, Dirr HW. Double mutation at the subunit interface of glutathione transferase rGSTM1-1 results in a stable, folded monomer. Biochemistry. 45: 2267-73. PMID 16475815 DOI: 10.1021/Bi0519506  0.394
2005 Rigsby RE, Fillgrove KL, Beihoffer LA, Armstrong RN. Fosfomycin resistance proteins: a nexus of glutathione transferases and epoxide hydrolases in a metalloenzyme superfamily. Methods in Enzymology. 401: 367-79. PMID 16399398 DOI: 10.1016/S0076-6879(05)01023-2  0.331
2005 Codreanu SG, Thompson LC, Hachey DL, Dirr HW, Armstrong RN. Influence of the dimer interface on glutathione transferase structure and dynamics revealed by amide H/D exchange mass spectrometry. Biochemistry. 44: 10605-12. PMID 16060669 DOI: 10.1021/Bi050836K  0.704
2005 Walsby CJ, Telser J, Rigsby RE, Armstrong RN, Hoffman BM. Enzyme control of small-molecule coordination in FosA as revealed by 31P pulsed ENDOR and ESE-EPR. Journal of the American Chemical Society. 127: 8310-9. PMID 15941264 DOI: 10.1021/Ja044094E  0.38
2005 Busenlehner LS, Armstrong RN. Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry. Archives of Biochemistry and Biophysics. 433: 34-46. PMID 15581564 DOI: 10.1016/J.Abb.2004.09.002  0.43
2004 Rigsby RE, Rife CL, Fillgrove KL, Newcomer ME, Armstrong RN. Phosphonoformate: a minimal transition state analogue inhibitor of the fosfomycin resistance protein, FosA. Biochemistry. 43: 13666-73. PMID 15504029 DOI: 10.1021/Bi048767H  0.662
2004 Busenlehner LS, Codreanu SG, Holm PJ, Bhakat P, Hebert H, Morgenstern R, Armstrong RN. Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase 1. Biochemistry. 43: 11145-52. PMID 15366924 DOI: 10.1021/Bi048716K  0.674
2004 Svensson R, Alander J, Armstrong RN, Morgenstern R. Kinetic characterization of thiolate anion formation and chemical catalysis of activated microsomal glutathione transferase 1. Biochemistry. 43: 8869-77. PMID 15236595 DOI: 10.1021/Bi0492511  0.418
2004 Pakhomova S, Rife CL, Armstrong RN, Newcomer ME. Structure of fosfomycin resistance protein FosA from transposon Tn2921. Protein Science : a Publication of the Protein Society. 13: 1260-5. PMID 15075406 DOI: 10.1110/Ps.03585004  0.692
2004 Ladner JE, Parsons JF, Rife CL, Gilliland GL, Armstrong RN. Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1. Biochemistry. 43: 352-61. PMID 14717589 DOI: 10.1021/Bi035832Z  0.705
2003 Fillgrove KL, Pakhomova S, Newcomer ME, Armstrong RN. Mechanistic diversity of fosfomycin resistance in pathogenic microorganisms. Journal of the American Chemical Society. 125: 15730-1. PMID 14677948 DOI: 10.1021/Ja039307Z  0.429
2003 Rife CL, Parsons JF, Xiao G, Gilliland GL, Armstrong RN. Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli. Proteins. 53: 777-82. PMID 14635120 DOI: 10.1002/Prot.10452  0.642
2002 Codreanu SG, Ladner JE, Xiao G, Stourman NV, Hachey DL, Gilliland GL, Armstrong RN. Local protein dynamics and catalysis: detection of segmental motion associated with rate-limiting product release by a glutathione transferase. Biochemistry. 41: 15161-72. PMID 12484753 DOI: 10.1021/Bi026776P  0.689
2002 Hornby JA, Codreanu SG, Armstrong RN, Dirr HW. Molecular recognition at the dimer interface of a class mu glutathione transferase: role of a hydrophobic interaction motif in dimer stability and protein function. Biochemistry. 41: 14238-47. PMID 12450388 DOI: 10.1021/Bi020548D  0.712
2002 Rife CL, Pharris RE, Newcomer ME, Armstrong RN. Crystal structure of a genomically encoded fosfomycin resistance protein (FosA) at 1.19 A resolution by MAD phasing off the L-III edge of Tl(+). Journal of the American Chemical Society. 124: 11001-3. PMID 12224946 DOI: 10.1021/Ja026879V  0.667
2002 Luo JK, Hornby JA, Wallace LA, Chen J, Armstrong RN, Dirr HW. Impact of domain interchange on conformational stability and equilibrium folding of chimeric class micro glutathione transferases. Protein Science : a Publication of the Protein Society. 11: 2208-17. PMID 12192076 DOI: 10.1110/Ps.0208002  0.301
2002 Smoukov SK, Telser J, Bernat BA, Rife CL, Armstrong RN, Hoffman BM. EPR study of substrate binding to the Mn(II) active site of the bacterial antibiotic resistance enzyme FosA: a better way to examine Mn(II). Journal of the American Chemical Society. 124: 2318-26. PMID 11878987 DOI: 10.1021/Ja012480F  0.67
2002 Codreanu SG, Hachey DL, Armstrong RN. Changes in M1-1 GST structure and dynamics due to mutations at the dimer interface probed by amide hydrogen exchange/MS Proceedings 50th Asms Conference On Mass Spectrometry and Allied Topics. 265-266.  0.611
2001 Bernat BA, Armstrong RN. Elementary steps in the acquisition of Mn2+ by the fosfomycin resistance protein (FosA). Biochemistry. 40: 12712-8. PMID 11601996 DOI: 10.1021/Bi0114832  0.373
2001 Morgenstern R, Svensson R, Bernat BA, Armstrong RN. Kinetic analysis of the slow ionization of glutathione by microsomal glutathione transferase MGST1. Biochemistry. 40: 3378-84. PMID 11258959 DOI: 10.1021/Bi0023394  0.431
2001 Cao M, Bernat BA, Wang Z, Armstrong RN, Helmann JD. FosB, a cysteine-dependent fosfomycin resistance protein under the control of sigma(W), an extracytoplasmic-function sigma factor in Bacillus subtilis. Journal of Bacteriology. 183: 2380-3. PMID 11244082 DOI: 10.1128/Jb.183.7.2380-2383.2001  0.309
2001 Rife CL, Armstrong RN. Structural investigations of the glutathione transferases Chemico-Biological Interactions. 133: 43-48.  0.601
2001 Armstrong RN, Rife C, Wang Z. Structure, mechanism and evolution of thiol transferases Chemico-Biological Interactions. 133: 167-169.  0.593
2000 Armstrong RN, Cassidy CS. New structural and chemical insight into the catalytic mechanism of epoxide hydrolases. Drug Metabolism Reviews. 32: 327-38. PMID 11139132 DOI: 10.1081/Dmr-100102337  0.398
2000 Armstrong RN. Mechanistic diversity in a metalloenzyme superfamily. Biochemistry. 39: 13625-32. PMID 11076500 DOI: 10.1021/Bi001814V  0.387
2000 Hornby JA, Luo JK, Stevens JM, Wallace LA, Kaplan W, Armstrong RN, Dirr HW. Equilibrium folding of dimeric class mu glutathione transferases involves a stable monomeric intermediate. Biochemistry. 39: 12336-44. PMID 11015213 DOI: 10.1021/Bi000176D  0.41
2000 Stevens JM, Armstrong RN, Dirr HW. Electrostatic interactions affecting the active site of class sigma glutathione S-transferase. The Biochemical Journal. 347: 193-7. PMID 10727418 DOI: 10.1042/0264-6021:3470193  0.431
1999 Bernat BA, Laughlin LT, Armstrong RN. Elucidation of a monovalent cation dependence and characterization of the divalent cation binding site of the fosfomycin resistance protein (FosA). Biochemistry. 38: 7462-9. PMID 10360943 DOI: 10.1021/Bi990391Y  0.43
1998 Armstrong RN. Mechanistic imperatives for the evolution of glutathione transferases. Current Opinion in Chemical Biology. 2: 618-23. PMID 9818188 DOI: 10.1016/S1367-5931(98)80093-8  0.406
1998 Stevens JM, Hornby JA, Armstrong RN, Dirr HW. Class sigma glutathione transferase unfolds via a dimeric and a monomeric intermediate: impact of subunit interface on conformational stability in the superfamily. Biochemistry. 37: 15534-41. PMID 9799517 DOI: 10.1021/Bi981044B  0.43
1998 Xiao G, Parsons JF, Tesh K, Armstrong RN, Gilliland GL. Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine. Journal of Molecular Biology. 281: 323-39. PMID 9698551 DOI: 10.1006/Jmbi.1998.1935  0.426
1998 Laughlin LT, Bernat BA, Armstrong RN. Mechanistic imperative for the evolution of a metalloglutathione transferase of the vicinal oxygen chelate superfamily. Chemico-Biological Interactions. 111: 41-50. PMID 9679542 DOI: 10.1016/S0009-2797(97)00150-6  0.422
1998 Parsons JF, Xiao G, Gilliland GL, Armstrong RN. Enzymes harboring unnatural amino acids: mechanistic and structural analysis of the enhanced catalytic activity of a glutathione transferase containing 5-fluorotryptophan. Biochemistry. 37: 6286-94. PMID 9572843 DOI: 10.1021/Bi980219E  0.472
1998 Tzeng HF, Laughlin LT, Armstrong RN. Semifunctional site-specific mutants affecting the hydrolytic half-reaction of microsomal epoxide hydrolase. Biochemistry. 37: 2905-11. PMID 9485442 DOI: 10.1021/bi9727388  0.335
1998 Laughlin LT, Tzeng HF, Lin S, Armstrong RN. Mechanism of microsomal epoxide hydrolase. Semifunctional site-specific mutants affecting the alkylation half-reaction. Biochemistry. 37: 2897-904. PMID 9485441 DOI: 10.1021/bi972737f  0.349
1997 Bernat BA, Laughlin LT, Armstrong RN. Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases. Biochemistry. 36: 3050-5. PMID 9115979 DOI: 10.1021/Bi963172A  0.429
1997 Armstrong RN. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chemical Research in Toxicology. 10: 2-18. PMID 9074797 DOI: 10.1021/Tx960072X  0.368
1996 Ji X, von Rosenvinge EC, Johnson WW, Armstrong RN, Gilliland GL. Location of a potential transport binding site in a sigma class glutathione transferase by x-ray crystallography. Proceedings of the National Academy of Sciences of the United States of America. 93: 8208-13. PMID 8710848 DOI: 10.1073/Pnas.93.16.8208  0.405
1996 Xiao G, Liu S, Ji X, Johnson WW, Chen J, Parsons JF, Stevens WJ, Gilliland GL, Armstrong RN. First-sphere and second-sphere electrostatic effects in the active site of a class mu gluthathione transferase. Biochemistry. 35: 4753-65. PMID 8664265 DOI: 10.1021/Bi960189K  0.354
1996 Tzeng HF, Laughlin LT, Lin S, Armstrong RN. The catalytic mechanism of microsomal epoxide hydrolase involves reversible formation and rate-limiting hydrolysis of the alkyl-enzyme intermediate Journal of the American Chemical Society. 118: 9436-9437. DOI: 10.1021/Ja961826X  0.382
1995 Ji X, von Rosenvinge EC, Johnson WW, Tomarev SI, Piatigorsky J, Armstrong RN, Gilliland GL. Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods. Biochemistry. 34: 5317-28. PMID 7727393 DOI: 10.1021/Bi00016A003  0.462
1995 Chen J, Armstrong RN. Stereoselective catalysis of a retro-Michael reaction by class mu glutathione transferases. Consequences for the internal distribution of products in the active site. Chemical Research in Toxicology. 8: 580-5. PMID 7548738 DOI: 10.1021/Tx00046A012  0.348
1994 Lacourciere GM, Armstrong RN. Microsomal and soluble epoxide hydrolases are members of the same family of C-X bond hydrolase enzymes. Chemical Research in Toxicology. 7: 121-4. PMID 8199297 DOI: 10.1021/Tx00038A001  0.443
1994 Ji X, Johnson WW, Sesay MA, Dickert L, Prasad SM, Ammon HL, Armstrong RN, Gilliland GL. Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene. Biochemistry. 33: 1043-52. PMID 8110735 DOI: 10.1021/Bi00171A002  0.448
1994 Ploemen JH, Johnson WW, Jespersen S, Vanderwall D, van Ommen B, van der Greef J, van Bladeren PJ, Armstrong RN. Active-site tyrosyl residues are targets in the irreversible inhibition of a class Mu glutathione transferase by 2-(S-glutathionyl)-3,5,6-trichloro-1,4-benzoquinone. The Journal of Biological Chemistry. 269: 26890-7. PMID 7929428  0.34
1994 Shan S, Armstrong RN. Rational reconstruction of the active site of a class mu glutathione S-transferase. The Journal of Biological Chemistry. 269: 32373-9. PMID 7798237  0.321
1993 Johnson WW, Liu S, Ji X, Gilliland GL, Armstrong RN. Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase. The Journal of Biological Chemistry. 268: 11508-11. PMID 8505287  0.32
1993 Lacourciere GM, Vakharia VN, Tan CP, Morris DI, Edwards GH, Moos M, Armstrong RN. Interaction of hepatic microsomal epoxide hydrolase derived from a recombinant baculovirus expression system with an azarene oxide and an aziridine substrate analogue. Biochemistry. 32: 2610-6. PMID 8383521 DOI: 10.1021/Bi00061A019  0.419
1993 Sinning I, Kleywegt GJ, Cowan SW, Reinemer P, Dirr HW, Huber R, Gilliland GL, Armstrong RN, Ji X, Board PG. Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes. Journal of Molecular Biology. 232: 192-212. PMID 8331657 DOI: 10.1006/Jmbi.1993.1376  0.437
1993 Ji X, Armstrong RN, Gilliland GL. Snapshots along the reaction coordinate of an SNAr reaction catalyzed by glutathione transferase. Biochemistry. 32: 12949-54. PMID 8241147 DOI: 10.1021/Bi00211A001  0.368
1993 Lacourciere GM, Armstrong RN. The catalytic mechanism of microsomal epoxide hydrolase involves an ester intermediate Journal of the American Chemical Society. 115: 10466-10467. DOI: 10.1021/Ja00075A115  0.329
1993 Liu S, Ji X, Gilliland GL, Stevens WJ, Armstrong RN. Second-sphere electrostatic effects in the active site of glutathione S-transferase. Observation of an on-face hydrogen bond between the side chain of threonine 13 and the π-cloud of tyrosine 6 and its influence on catalysis Journal of the American Chemical Society. 115: 7910-7911. DOI: 10.1021/Ja00070A060  0.309
1992 Liu S, Zhang P, Ji X, Johnson WW, Gilliland GL, Armstrong RN. Contribution of tyrosine 6 to the catalytic mechanism of isoenzyme 3-3 of glutathione S-transferase. The Journal of Biological Chemistry. 267: 4296-9. PMID 1537822  0.353
1992 Zhang P, Liu S, Shan SO, Ji X, Gilliland GL, Armstrong RN. Modular mutagenesis of exons 1, 2, and 8 of a glutathione S-transferase from the mu class. Mechanistic and structural consequences for chimeras of isoenzyme 3-3. Biochemistry. 31: 10185-93. PMID 1420140 DOI: 10.1021/Bi00157A005  0.343
1992 Ji X, Zhang P, Armstrong RN, Gilliland GL. The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolution. Biochemistry. 31: 10169-84. PMID 1420139 DOI: 10.1021/Bi00157A004  0.373
1991 Zhang PH, Graminski GF, Armstrong RN. Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis. The Journal of Biological Chemistry. 266: 19475-9. PMID 1918058  0.31
1989 Graminski GF, Zhang PH, Sesay MA, Ammon HL, Armstrong RN. Formation of the 1-(S-glutathionyl)-2,4,6-trinitrocyclohexadienate anion at the active site of glutathione S-transferase: evidence for enzymic stabilization of sigma-complex intermediates in nucleophilic aromatic substitution reactions. Biochemistry. 28: 6252-8. PMID 2789999 DOI: 10.1021/Bi00441A017  0.422
1989 Graminski GF, Kubo Y, Armstrong RN. Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase. Biochemistry. 28: 3562-8. PMID 2742854 DOI: 10.1021/Bi00434A062  0.378
1989 Graminski GF, Kubo Y, Armstrong RN. Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase [Erratum to document cited in CA110(19):169169n] Biochemistry. 28: 7138-7138. DOI: 10.1021/Bi00443A055  0.309
1988 Chen WJ, Graminski GF, Armstrong RN. Dissection of the catalytic mechanism of isozyme 4-4 of glutathione S-transferase with alternative substrates. Biochemistry. 27: 647-54. PMID 3349053 DOI: 10.1021/Bi00402A023  0.369
1983 Cobb D, Boehlert C, Lewis D, Armstrong RN. Stereoselectivity of isozyme C of glutathione S-transferase toward arene and azaarene oxides. Biochemistry. 22: 805-12. PMID 6838824 DOI: 10.1021/Bi00273A015  0.315
1979 Granot J, Kondo H, Armstrong RN, Mildvan AS, Kaiser ET. Nuclear magnetic resonance studies of the conformation of tetraamminecobalt (III)--ATP bound at the active site of bovine heart protein kinase. Biochemistry. 18: 2339-45. PMID 444460 DOI: 10.1021/Bi00578A032  0.534
1979 Armstrong RN, Kondo H, Granot J, Kaiser ET, Mildvan AS. Magnetic resonance and kinetic studies of the manganese(II) ion and substrate complexes of the catalytic subunit of adenosine 3',5'-monophosphate dependent protein kinase from bovine heart. Biochemistry. 18: 1230-8. PMID 218617 DOI: 10.1021/Bi00574A018  0.529
1979 Armstrong RN, Kondo H, Kaiser ET. Cyclic AMP-dependent ATPase activity of bovine heart protein kinase. Proceedings of the National Academy of Sciences of the United States of America. 76: 722-5. PMID 218218 DOI: 10.1073/Pnas.76.2.722  0.57
1978 Armstrong RN, Kaiser ET. Sulfhydryl group reactivity of adenosine 3',5'-monophosphate dependent protein kinase from bovine heart: a probe of holoenzyme structure. Biochemistry. 17: 2840-5. PMID 210783 DOI: 10.1021/Bi00607A022  0.543
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