HistCite - Publications by GA Petsko

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#	Date / Author / Journal	LCS	GCS	LCR	CR
51	105 FARBER GK, GLASFELD A, TIRABY G, RINGE D, et al. CRYSTALLOGRAPHIC STUDIES OF THE MECHANISM OF XYLOSE ISOMERASE BIOCHEMISTRY. 1989 SEP 5; 28 (18): 7289-7297	7	104	4	56
52	106 DELPOZO AM, POSPISCHIL MA, UENO H, MANNING JM, et al. EFFECTS OF D-SERINE ON BACTERIAL D-AMINO-ACID TRANSAMINASE - ACCUMULATION OF AN INTERMEDIATE AND INACTIVATION OF THE ENZYME BIOCHEMISTRY. 1989 OCT 31; 28 (22): 8798-8803	0	13	2	28
53	114 STODDARD BL, BRUHNKE J, PORTER N, RINGE D, et al. STRUCTURE AND ACTIVITY OF 2 PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN BIOCHEMISTRY. 1990 MAY 22; 29 (20): 4871-4879	4	47	1	28
54	117 LOLIS E, ALBER T, DAVENPORT RC, ROSE D, et al. STRUCTURE OF YEAST TRIOSEPHOSPHATE ISOMERASE AT 1.9-A RESOLUTION BIOCHEMISTRY. 1990 JUL 17; 29 (28): 6609-6618	11	208	9	75
55	118 LOLIS E, PETSKO GA CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE AND 2-PHOSPHOGLYCOLATE AT 2.5-A RESOLUTION - IMPLICATIONS FOR CATALYSIS BIOCHEMISTRY. 1990 JUL 17; 29 (28): 6619-6625	4	162	9	51
56	121 STODDARD BL, BRUHNKE J, KOENIGS P, PORTER N, et al. PHOTOLYSIS AND DEACYLATION OF INHIBITED CHYMOTRYPSIN BIOCHEMISTRY. 1990 SEP 4; 29 (35): 8042-8051	1	40	1	29
57	123 STODDARD BL, HOWELL PL, RINGE D, PETSKO GA THE 2.1-A RESOLUTION STRUCTURE OF IRON SUPEROXIDE-DISMUTASE FROM PSEUDOMONAS-OVALIS BIOCHEMISTRY. 1990 SEP 25; 29 (38): 8885-8893	2	123	4	44
58	127 DANISHEFSKY AT, ONNUFER JJ, PETSKO GA, RINGE D ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA-COLI ASPARTATE-AMINOTRANSFERASE BIOCHEMISTRY. 1991 FEB 19; 30 (7): 1980-1985	0	40	1	37
59	130 KOMIVES EA, CHANG LC, LOLIS E, TILTON RF, et al. ELECTROPHILIC CATALYSIS IN TRIOSEPHOSPHATE ISOMERASE - THE ROLE OF HISTIDINE-95 BIOCHEMISTRY. 1991 MAR 26; 30 (12): 3011-3019	8	87	3	27
60	131 STRONG RK, CAMPBELL R, ROSE DR, PETSKO GA, et al. 3-DIMENSIONAL STRUCTURE OF MURINE ANTI-PARA-AZOPHENYLARSONATE FAB-36-71 .1. X-RAY CRYSTALLOGRAPHY, SITE-DIRECTED MUTAGENESIS, AND MODELING OF THE COMPLEX WITH HAPTEN BIOCHEMISTRY. 1991 APR 16; 30 (15): 3739-3748	0	95	4	76
#	Date / Author / Journal	LCS	GCS	LCR	CR
61	132 STRONG RK, PETSKO GA, SHARON J, MARGOLIES MN 3-DIMENSIONAL STRUCTURE OF MURINE ANTI-PARA-AZOPHENYLARSONATE FAB-36-71 .2. STRUCTURAL BASIS OF HAPTEN BINDING AND IDIOTYPY BIOCHEMISTRY. 1991 APR 16; 30 (15): 3749-3757	1	42	1	33
62	133 DAVENPORT RC, BASH PA, SEATON BA, KARPLUS M, et al. STRUCTURE OF THE TRIOSEPHOSPHATE ISOMERASE PHOSPHOGLYCOLOHYDROXAMATE COMPLEX - AN ANALOG OF THE INTERMEDIATE ON THE REACTION PATHWAY BIOCHEMISTRY. 1991 JUN 18; 30 (24): 5821-5826	8	122	10	35
63	134 BASH PA, FIELD MJ, DAVENPORT RC, PETSKO GA, et al. COMPUTER-SIMULATION AND ANALYSIS OF THE REACTION PATHWAY OF TRIOSEPHOSPHATE ISOMERASE BIOCHEMISTRY. 1991 JUN 18; 30 (24): 5826-5832	5	192	7	47
64	137 NEIDHART DJ, HOWELL PL, PETSKO GA, POWERS VM, et al. MECHANISM OF THE REACTION CATALYZED BY MANDELATE RACEMASE .2. CRYSTAL-STRUCTURE OF MANDELATE RACEMASE AT 2.5-A RESOLUTION - IDENTIFICATION OF THE ACTIVE-SITE AND POSSIBLE CATALYTIC RESIDUES BIOCHEMISTRY. 1991 SEP 24; 30 (38): 9264-9273	8	105	4	54
65	141 GERLT JA, KENYON GL, KOZARICH JW, NEIDHART DJ, et al. MANDELATE RACEMASE - UNDERSTANDING THE MECHANISM OF HETEROLYTIC C-H BOND-CLEAVAGE BIOCHEMISTRY. 1992 FEB 25; 31 (7): 2188-2188	0	0	0	0
66	142 JOSEPHMCCARTHY D, PETSKO GA, KARPLUS M HINGED LID MOTION OF THE TRIOSEPHOSPHATE ISOMERASE LOOP BIOCHEMISTRY. 1992 FEB 25; 31 (7): 2199-2199	0	0	0	0
67	143 TILTON RF, DEWAN JC, PETSKO GA EFFECTS OF TEMPERATURE ON PROTEIN-STRUCTURE AND DYNAMICS - X-RAY CRYSTALLOGRAPHIC STUDIES OF THE PROTEIN RIBONUCLEASE-A AT 9 DIFFERENT TEMPERATURES FROM 98-K TO 320-K BIOCHEMISTRY. 1992 MAR 10; 31 (9): 2469-2481	4	187	8	52
68	160 MITRA B, GERLT JA, BABBITT PC, KOO CW, et al. A NOVEL STRUCTURAL BASIS FOR MEMBRANE ASSOCIATION OF A PROTEIN - CONSTRUCTION OF A CHIMERIC SOLUBLE MUTANT OF (S)-MANDELATE DEHYDROGENASE FROM PSEUDOMONAS-PUTIDA BIOCHEMISTRY. 1993 DEC 7; 32 (48): 12959-12967	2	24	0	30
69	161 STOCK AM, MARTINEZHACKERT E, RASMUSSEN BF, WEST AH, et al. STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS BIOCHEMISTRY. 1993 DEC 14; 32 (49): 13375-13380	0	148	0	33
70	165 ALLEN KN, LAVIE A, FARBER GK, GLASFELD A, et al. ISOTOPIC EXCHANGE PLUS SUBSTRATE AND INHIBITION-KINETICS OF D-XYLOSE ISOMERASE DO NOT SUPPORT A PROTON-TRANSFER MECHANISM BIOCHEMISTRY. 1994 FEB 15; 33 (6): 1481-1487	4	43	3	34
#	Date / Author / Journal	LCS	GCS	LCR	CR
71	166 ALLEN KN, LAVIE A, GLASFELD A, TANADA TN, et al. ROLE OF THE DIVALENT METAL-ION IN SUGAR BINDING, RING-OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE - REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID BIOCHEMISTRY. 1994 FEB 15; 33 (6): 1488-1494	5	44	3	29
72	167 HARRISON DH, BOHREN KM, RINGE D, PETSKO GA, et al. ANION-BINDING SITE IN HUMAN ALDOSE REDUCTASE - MECHANISTIC IMPLICATIONS FOR THE BINDING OF CITRATE, CACODYLATE, AND GLUCOSE-6-PHOSPHATE BIOCHEMISTRY. 1994 MAR 1; 33 (8): 2011-2020	2	116	1	27
73	168 BOHREN KM, GRIMSHAW CE, LAI CJ, HARRISON DH, et al. TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRATE STEREOCHEMICAL SELECTIVITY IN THE REDUCTION REACTION OF HUMAN ALDOSE REDUCTASE - ENZYME-KINETICS AND CRYSTAL-STRUCTURE OF THE Y48H MUTANT ENZYME BIOCHEMISTRY. 1994 MAR 1; 33 (8): 2021-2032	3	129	1	46
74	169 JOSEPHMCCARTHY D, LOLIS E, KOMIVES EA, PETSKO GA CRYSTAL-STRUCTURE OF THE K12M/G15A TRIOSEPHOSPHATE ISOMERASE DOUBLE MUTANT AND ELECTROSTATIC ANALYSIS OF THE ACTIVE-SITE BIOCHEMISTRY. 1994 MAR 15; 33 (10): 2815-2823	3	19	10	38
75	170 JOSEPHMCCARTHY D, ROST LE, KOMIVES EA, PETSKO GA CRYSTAL-STRUCTURE OF THE MUTANT YEAST TRIOSEPHOSPHATE ISOMERASE IN WHICH THE CATALYTIC BASE GLUTAMIC-ACID-165 IS CHANGED TO ASPARTIC-ACID BIOCHEMISTRY. 1994 MAR 15; 33 (10): 2824-2829	4	25	6	31
76	171 ZHANG ZD, SUGIO S, KOMIVES EA, LIU KD, et al. CRYSTAL-STRUCTURE OF RECOMBINANT CHICKEN TRIOSEPHOSPHATE ISOMERASE PHOSPHOGLYCOLOHYDROXAMATE COMPLEX AT 1.8-ANGSTROM RESOLUTION BIOCHEMISTRY. 1994 MAR 15; 33 (10): 2830-2837	3	48	12	53
77	173 LAVIE A, ALLEN KN, PETSKO GA, RINGE D X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS BIOCHEMISTRY. 1994 MAY 10; 33 (18): 5469-5480	6	80	5	42
78	175 DING XC, RASMUSSEN BF, PETSKO GA, RINGE D DIRECT STRUCTURAL OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE BIOCHEMISTRY. 1994 AUG 9; 33 (31): 9285-9293	5	47	6	45
79	181 MITRA B, KALLARAKAL AT, KOZARICH JW, GERLT JA, et al. MECHANISM OF THE REACTION CATALYZED BY MANDELATE RACEMASE - IMPORTANCE OF ELECTROPHILIC CATALYSIS BY GLUTAMIC-ACID-317 BIOCHEMISTRY. 1995 MAR 7; 34 (9): 2777-2787	3	49	4	36
80	182 KALLARAKAL AT, MITRA B, KOZARICH JW, GERLT JA, et al. MECHANISM OF THE REACTION CATALYZED BY MANDELATE RACEMASE - STRUCTURE AND MECHANISTIC PROPERTIES OF THE K166R MUTANT BIOCHEMISTRY. 1995 MAR 7; 34 (9): 2788-2797	3	43	2	23
#	Date / Author / Journal	LCS	GCS	LCR	CR
81	184 MATTOS C, GIAMMONA DA, PETSKO GA, RINGE D STRUCTURAL-ANALYSIS OF THE ACTIVE-SITE OF PORCINE PANCREATIC ELASTASE BASED ON THE X-RAY CRYSTAL-STRUCTURES OF COMPLEXES WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS BIOCHEMISTRY. 1995 MAR 14; 34 (10): 3193-3203	3	18	2	25
82	185 ALLEN KN, LAVIE A, PETSKO GA, RINGE D DESIGN, SYNTHESIS, AND CHARACTERIZATION OF A POTENT XYLOSE ISOMERASE INHIBITOR, D-THREONOHYDROXAMIC ACID, AND HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHIC STRUCTURE OF THE ENZYME-INHIBITOR COMPLEX BIOCHEMISTRY. 1995 MAR 21; 34 (11): 3742-3749	0	40	5	37
83	190 SUGIO S, PETSKO GA, MANNING JM, SODA K, et al. CRYSTAL-STRUCTURE OF A D-AMINO-ACID AMINOTRANSFERASE - HOW THE PROTEIN CONTROLS STEREOSELECTIVITY BIOCHEMISTRY. 1995 AUG 1; 34 (30): 9661-9669	2	101	3	39
84	194 KOMIVES EA, LOUGHEED JC, LIU K, SUGIO S, et al. THE STRUCTURAL BASIS FOR PSEUDOREVERSION OF THE E165D LESION BY THE SECONDARY S96P MUTATION IN TRIOSEPHOSPHATE ISOMERASE DEPENDS ON THE POSITIONS OF ACTIVE-SITE WATER-MOLECULES BIOCHEMISTRY. 1995 OCT 17; 34 (41): 13612-13621	3	12	9	41
85	199 Schafer SL, Barrett WC, Kallarakal AT, Mitra B, et al. Mechanism of the reaction catalyzed by mandelate racemase: Structure and mechanistic properties of the D270N mutant BIOCHEMISTRY. 1996 MAY 7; 35 (18): 5662-5669	0	22	3	27
86	202 Komives EA, Lougheed JC, Zhang ZD, Sugio S, et al. The structural basis for pseudoreversion of the H95N lesion by the secondary S96P Mutation in triosephosphate isomerase BIOCHEMISTRY. 1996 DEC 3; 35 (48): 15474-15484	1	7	7	29
87	204 Shaw JP, Petsko GA, Ringe D Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-angstrom resolution BIOCHEMISTRY. 1997 FEB 11; 36 (6): 1329-1342	1	144	4	64
88	216 Harrison DHT, Bohren KM, Petsko GA, Ringe D, et al. The Alrestatin double-decker: Binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant BIOCHEMISTRY. 1997 DEC 23; 36 (51): 16134-16140	0	42	2	25
89	223 Hasson MS, Muscate A, McLeish MJ, Polovnikova LS, et al. The crystal structure of benzoylformate decarboxylase at 1.6 angstrom resolution: Diversity of catalytic residues in thiamin diphosphate-dependent enzymes BIOCHEMISTRY. 1998 JUL 14; 37 (28): 9918-9930	1	100	2	76
90	227 Morollo AA, Petsko GA, Ringe D Structure of a Michaelis complex analogue: Propionate binds in the substrate carboxylate site of alanine racemase BIOCHEMISTRY. 1999 MAR 16; 38 (11): 3293-3301	0	32	2	40
#	Date / Author / Journal	LCS	GCS	LCR	CR
91	228 Zhang ZD, Komives EA, Sugio S, Blacklow SC, et al. The role of water in the catalytic efficiency of triosephosphate isomerase BIOCHEMISTRY. 1999 APR 6; 38 (14): 4389-4397	1	28	11	44
92	236 De Paola CC, Bennett B, Holz RC, Ringe D, et al. L-butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: A case of arrested development BIOCHEMISTRY. 1999 JUL 13; 38 (28): 9048-9053	2	28	0	42
93	243 McMillan FM, Cahoon M, White A, Hedstrom L, et al. Crystal structure at 2.4 A resolution of Borrelia burgdorferi inosine 5 '-monophosphate dehydrogenase: Evidence of a substrate-induced hinged-lid motion by loop 6 BIOCHEMISTRY. 2000 APR 18; 39 (15): 4533-4542	2	26	1	52
94	249 Petsko GA, Collins J How new enzymes evolve from old ones. BIOCHEMISTRY. 2001 JUL 24; 40 (29): 8633-8633	0	0	0	0
95	250 Petsko GA Structural enzymology over the last 40 years. BIOCHEMISTRY. 2001 JUL 24; 40 (29): 8642-8642	0	0	0	0
96	251 Ringe D, Petsko GA, Desmarais W, Holz RC Bridged bimetallic enzymes: Two heads are better than one. BIOCHEMISTRY. 2001 JUL 24; 40 (29): 8661-8661	0	0	0	0
97	258 Hadfield A, Shammas C, Kryger G, Ringe D, et al. Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase BIOCHEMISTRY. 2001 DEC 4; 40 (48): 14475-14483	0	20	1	27
98	261 Bahnson BJ, Anderson VE, Petsko GA Structural mechanism of enoyl-CoA hydratase: Three atoms from a single water are added in either an E1cb stepwise or concerted fashion BIOCHEMISTRY. 2002 FEB 26; 41 (8): 2621-2629	0	32	0	46
99	267 Gan L, Petsko GA, Hedstrom L Crystal structure of a ternary complex of Tritrichomonas foetus inosine 5 '-monophosphate dehydrogenase: NAD(+) orients the active site loop for catalysis BIOCHEMISTRY. 2002 NOV 5; 41 (44): 13309-13317	1	19	1	34
100	281 Gan L, Seyedsayamdost MR, Shuto S, Matsuda A, et al. The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase BIOCHEMISTRY. 2003 FEB 4; 42 (4): 857-863	0	17	2	39

Date / Author / Journal

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GCS

LCR

105 FARBER GK, GLASFELD A, TIRABY G, RINGE D, et al.

CRYSTALLOGRAPHIC STUDIES OF THE MECHANISM OF XYLOSE ISOMERASE

BIOCHEMISTRY. 1989 SEP 5; 28 (18): 7289-7297

104

106 DELPOZO AM, POSPISCHIL MA, UENO H, MANNING JM, et al.

EFFECTS OF D-SERINE ON BACTERIAL D-AMINO-ACID TRANSAMINASE - ACCUMULATION OF AN INTERMEDIATE AND INACTIVATION OF THE ENZYME

BIOCHEMISTRY. 1989 OCT 31; 28 (22): 8798-8803

114 STODDARD BL, BRUHNKE J, PORTER N, RINGE D, et al.

STRUCTURE AND ACTIVITY OF 2 PHOTOREVERSIBLE CINNAMATES BOUND TO CHYMOTRYPSIN

BIOCHEMISTRY. 1990 MAY 22; 29 (20): 4871-4879

117 LOLIS E, ALBER T, DAVENPORT RC, ROSE D, et al.

STRUCTURE OF YEAST TRIOSEPHOSPHATE ISOMERASE AT 1.9-A RESOLUTION

BIOCHEMISTRY. 1990 JUL 17; 29 (28): 6609-6618

208

118 LOLIS E, PETSKO GA

CRYSTALLOGRAPHIC ANALYSIS OF THE COMPLEX BETWEEN TRIOSEPHOSPHATE ISOMERASE AND 2-PHOSPHOGLYCOLATE AT 2.5-A RESOLUTION - IMPLICATIONS FOR CATALYSIS

BIOCHEMISTRY. 1990 JUL 17; 29 (28): 6619-6625

162

121 STODDARD BL, BRUHNKE J, KOENIGS P, PORTER N, et al.

PHOTOLYSIS AND DEACYLATION OF INHIBITED CHYMOTRYPSIN

BIOCHEMISTRY. 1990 SEP 4; 29 (35): 8042-8051

123 STODDARD BL, HOWELL PL, RINGE D, PETSKO GA

THE 2.1-A RESOLUTION STRUCTURE OF IRON SUPEROXIDE-DISMUTASE FROM PSEUDOMONAS-OVALIS

BIOCHEMISTRY. 1990 SEP 25; 29 (38): 8885-8893

123

127 DANISHEFSKY AT, ONNUFER JJ, PETSKO GA, RINGE D

ACTIVITY AND STRUCTURE OF THE ACTIVE-SITE MUTANTS R386Y AND R386F OF ESCHERICHIA-COLI ASPARTATE-AMINOTRANSFERASE

BIOCHEMISTRY. 1991 FEB 19; 30 (7): 1980-1985

130 KOMIVES EA, CHANG LC, LOLIS E, TILTON RF, et al.

ELECTROPHILIC CATALYSIS IN TRIOSEPHOSPHATE ISOMERASE - THE ROLE OF HISTIDINE-95

BIOCHEMISTRY. 1991 MAR 26; 30 (12): 3011-3019

131 STRONG RK, CAMPBELL R, ROSE DR, PETSKO GA, et al.

3-DIMENSIONAL STRUCTURE OF MURINE ANTI-PARA-AZOPHENYLARSONATE FAB-36-71 .1. X-RAY CRYSTALLOGRAPHY, SITE-DIRECTED MUTAGENESIS, AND MODELING OF THE COMPLEX WITH HAPTEN

BIOCHEMISTRY. 1991 APR 16; 30 (15): 3739-3748

Date / Author / Journal

LCS

GCS

LCR

132 STRONG RK, PETSKO GA, SHARON J, MARGOLIES MN

3-DIMENSIONAL STRUCTURE OF MURINE ANTI-PARA-AZOPHENYLARSONATE FAB-36-71 .2. STRUCTURAL BASIS OF HAPTEN BINDING AND IDIOTYPY

BIOCHEMISTRY. 1991 APR 16; 30 (15): 3749-3757

133 DAVENPORT RC, BASH PA, SEATON BA, KARPLUS M, et al.

STRUCTURE OF THE TRIOSEPHOSPHATE ISOMERASE PHOSPHOGLYCOLOHYDROXAMATE COMPLEX - AN ANALOG OF THE INTERMEDIATE ON THE REACTION PATHWAY

BIOCHEMISTRY. 1991 JUN 18; 30 (24): 5821-5826

122

134 BASH PA, FIELD MJ, DAVENPORT RC, PETSKO GA, et al.

COMPUTER-SIMULATION AND ANALYSIS OF THE REACTION PATHWAY OF TRIOSEPHOSPHATE ISOMERASE

BIOCHEMISTRY. 1991 JUN 18; 30 (24): 5826-5832

192

137 NEIDHART DJ, HOWELL PL, PETSKO GA, POWERS VM, et al.

MECHANISM OF THE REACTION CATALYZED BY MANDELATE RACEMASE .2. CRYSTAL-STRUCTURE OF MANDELATE RACEMASE AT 2.5-A RESOLUTION - IDENTIFICATION OF THE ACTIVE-SITE AND POSSIBLE CATALYTIC RESIDUES

BIOCHEMISTRY. 1991 SEP 24; 30 (38): 9264-9273

105

141 GERLT JA, KENYON GL, KOZARICH JW, NEIDHART DJ, et al.

MANDELATE RACEMASE - UNDERSTANDING THE MECHANISM OF HETEROLYTIC C-H BOND-CLEAVAGE

BIOCHEMISTRY. 1992 FEB 25; 31 (7): 2188-2188

142 JOSEPHMCCARTHY D, PETSKO GA, KARPLUS M

HINGED LID MOTION OF THE TRIOSEPHOSPHATE ISOMERASE LOOP

BIOCHEMISTRY. 1992 FEB 25; 31 (7): 2199-2199

143 TILTON RF, DEWAN JC, PETSKO GA

EFFECTS OF TEMPERATURE ON PROTEIN-STRUCTURE AND DYNAMICS - X-RAY CRYSTALLOGRAPHIC STUDIES OF THE PROTEIN RIBONUCLEASE-A AT 9 DIFFERENT TEMPERATURES FROM 98-K TO 320-K

BIOCHEMISTRY. 1992 MAR 10; 31 (9): 2469-2481

187

160 MITRA B, GERLT JA, BABBITT PC, KOO CW, et al.

A NOVEL STRUCTURAL BASIS FOR MEMBRANE ASSOCIATION OF A PROTEIN - CONSTRUCTION OF A CHIMERIC SOLUBLE MUTANT OF (S)-MANDELATE DEHYDROGENASE FROM PSEUDOMONAS-PUTIDA

BIOCHEMISTRY. 1993 DEC 7; 32 (48): 12959-12967

161 STOCK AM, MARTINEZHACKERT E, RASMUSSEN BF, WEST AH, et al.

STRUCTURE OF THE MG2+-BOUND FORM OF CHEY AND MECHANISM OF PHOSPHORYL TRANSFER IN BACTERIAL CHEMOTAXIS

BIOCHEMISTRY. 1993 DEC 14; 32 (49): 13375-13380

148

165 ALLEN KN, LAVIE A, FARBER GK, GLASFELD A, et al.

ISOTOPIC EXCHANGE PLUS SUBSTRATE AND INHIBITION-KINETICS OF D-XYLOSE ISOMERASE DO NOT SUPPORT A PROTON-TRANSFER MECHANISM

BIOCHEMISTRY. 1994 FEB 15; 33 (6): 1481-1487

Date / Author / Journal

LCS

GCS

LCR

166 ALLEN KN, LAVIE A, GLASFELD A, TANADA TN, et al.

ROLE OF THE DIVALENT METAL-ION IN SUGAR BINDING, RING-OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE - REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID

BIOCHEMISTRY. 1994 FEB 15; 33 (6): 1488-1494

167 HARRISON DH, BOHREN KM, RINGE D, PETSKO GA, et al.

ANION-BINDING SITE IN HUMAN ALDOSE REDUCTASE - MECHANISTIC IMPLICATIONS FOR THE BINDING OF CITRATE, CACODYLATE, AND GLUCOSE-6-PHOSPHATE

BIOCHEMISTRY. 1994 MAR 1; 33 (8): 2011-2020

116

168 BOHREN KM, GRIMSHAW CE, LAI CJ, HARRISON DH, et al.

TYROSINE-48 IS THE PROTON DONOR AND HISTIDINE-110 DIRECTS SUBSTRATE STEREOCHEMICAL SELECTIVITY IN THE REDUCTION REACTION OF HUMAN ALDOSE REDUCTASE - ENZYME-KINETICS AND CRYSTAL-STRUCTURE OF THE Y48H MUTANT ENZYME

BIOCHEMISTRY. 1994 MAR 1; 33 (8): 2021-2032

129

169 JOSEPHMCCARTHY D, LOLIS E, KOMIVES EA, PETSKO GA

CRYSTAL-STRUCTURE OF THE K12M/G15A TRIOSEPHOSPHATE ISOMERASE DOUBLE MUTANT AND ELECTROSTATIC ANALYSIS OF THE ACTIVE-SITE

BIOCHEMISTRY. 1994 MAR 15; 33 (10): 2815-2823

170 JOSEPHMCCARTHY D, ROST LE, KOMIVES EA, PETSKO GA

CRYSTAL-STRUCTURE OF THE MUTANT YEAST TRIOSEPHOSPHATE ISOMERASE IN WHICH THE CATALYTIC BASE GLUTAMIC-ACID-165 IS CHANGED TO ASPARTIC-ACID

BIOCHEMISTRY. 1994 MAR 15; 33 (10): 2824-2829

171 ZHANG ZD, SUGIO S, KOMIVES EA, LIU KD, et al.

CRYSTAL-STRUCTURE OF RECOMBINANT CHICKEN TRIOSEPHOSPHATE ISOMERASE PHOSPHOGLYCOLOHYDROXAMATE COMPLEX AT 1.8-ANGSTROM RESOLUTION

BIOCHEMISTRY. 1994 MAR 15; 33 (10): 2830-2837

173 LAVIE A, ALLEN KN, PETSKO GA, RINGE D

X-RAY CRYSTALLOGRAPHIC STRUCTURES OF D-XYLOSE ISOMERASE-SUBSTRATE COMPLEXES POSITION THE SUBSTRATE AND PROVIDE EVIDENCE FOR METAL MOVEMENT DURING CATALYSIS

BIOCHEMISTRY. 1994 MAY 10; 33 (18): 5469-5480

175 DING XC, RASMUSSEN BF, PETSKO GA, RINGE D

DIRECT STRUCTURAL OBSERVATION OF AN ACYL-ENZYME INTERMEDIATE IN THE HYDROLYSIS OF AN ESTER SUBSTRATE BY ELASTASE

BIOCHEMISTRY. 1994 AUG 9; 33 (31): 9285-9293

181 MITRA B, KALLARAKAL AT, KOZARICH JW, GERLT JA, et al.

MECHANISM OF THE REACTION CATALYZED BY MANDELATE RACEMASE - IMPORTANCE OF ELECTROPHILIC CATALYSIS BY GLUTAMIC-ACID-317

BIOCHEMISTRY. 1995 MAR 7; 34 (9): 2777-2787

182 KALLARAKAL AT, MITRA B, KOZARICH JW, GERLT JA, et al.

MECHANISM OF THE REACTION CATALYZED BY MANDELATE RACEMASE - STRUCTURE AND MECHANISTIC PROPERTIES OF THE K166R MUTANT

BIOCHEMISTRY. 1995 MAR 7; 34 (9): 2788-2797

Date / Author / Journal

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LCR

184 MATTOS C, GIAMMONA DA, PETSKO GA, RINGE D

STRUCTURAL-ANALYSIS OF THE ACTIVE-SITE OF PORCINE PANCREATIC ELASTASE BASED ON THE X-RAY CRYSTAL-STRUCTURES OF COMPLEXES WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS

BIOCHEMISTRY. 1995 MAR 14; 34 (10): 3193-3203

185 ALLEN KN, LAVIE A, PETSKO GA, RINGE D

DESIGN, SYNTHESIS, AND CHARACTERIZATION OF A POTENT XYLOSE ISOMERASE INHIBITOR, D-THREONOHYDROXAMIC ACID, AND HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHIC STRUCTURE OF THE ENZYME-INHIBITOR COMPLEX

BIOCHEMISTRY. 1995 MAR 21; 34 (11): 3742-3749

190 SUGIO S, PETSKO GA, MANNING JM, SODA K, et al.

CRYSTAL-STRUCTURE OF A D-AMINO-ACID AMINOTRANSFERASE - HOW THE PROTEIN CONTROLS STEREOSELECTIVITY

BIOCHEMISTRY. 1995 AUG 1; 34 (30): 9661-9669

101

194 KOMIVES EA, LOUGHEED JC, LIU K, SUGIO S, et al.

THE STRUCTURAL BASIS FOR PSEUDOREVERSION OF THE E165D LESION BY THE SECONDARY S96P MUTATION IN TRIOSEPHOSPHATE ISOMERASE DEPENDS ON THE POSITIONS OF ACTIVE-SITE WATER-MOLECULES

BIOCHEMISTRY. 1995 OCT 17; 34 (41): 13612-13621

199 Schafer SL, Barrett WC, Kallarakal AT, Mitra B, et al.

Mechanism of the reaction catalyzed by mandelate racemase: Structure and mechanistic properties of the D270N mutant

BIOCHEMISTRY. 1996 MAY 7; 35 (18): 5662-5669

202 Komives EA, Lougheed JC, Zhang ZD, Sugio S, et al.

The structural basis for pseudoreversion of the H95N lesion by the secondary S96P Mutation in triosephosphate isomerase

BIOCHEMISTRY. 1996 DEC 3; 35 (48): 15474-15484

204 Shaw JP, Petsko GA, Ringe D

Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-angstrom resolution

BIOCHEMISTRY. 1997 FEB 11; 36 (6): 1329-1342

144

216 Harrison DHT, Bohren KM, Petsko GA, Ringe D, et al.

The Alrestatin double-decker: Binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant

BIOCHEMISTRY. 1997 DEC 23; 36 (51): 16134-16140

223 Hasson MS, Muscate A, McLeish MJ, Polovnikova LS, et al.

The crystal structure of benzoylformate decarboxylase at 1.6 angstrom resolution: Diversity of catalytic residues in thiamin diphosphate-dependent enzymes

BIOCHEMISTRY. 1998 JUL 14; 37 (28): 9918-9930

100

227 Morollo AA, Petsko GA, Ringe D

Structure of a Michaelis complex analogue: Propionate binds in the substrate carboxylate site of alanine racemase

BIOCHEMISTRY. 1999 MAR 16; 38 (11): 3293-3301

Date / Author / Journal

LCS

GCS

LCR

228 Zhang ZD, Komives EA, Sugio S, Blacklow SC, et al.

The role of water in the catalytic efficiency of triosephosphate isomerase

BIOCHEMISTRY. 1999 APR 6; 38 (14): 4389-4397

236 De Paola CC, Bennett B, Holz RC, Ringe D, et al.

L-butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: A case of arrested development

BIOCHEMISTRY. 1999 JUL 13; 38 (28): 9048-9053

243 McMillan FM, Cahoon M, White A, Hedstrom L, et al.

Crystal structure at 2.4 A resolution of Borrelia burgdorferi inosine 5 '-monophosphate dehydrogenase: Evidence of a substrate-induced hinged-lid motion by loop 6

BIOCHEMISTRY. 2000 APR 18; 39 (15): 4533-4542

249 Petsko GA, Collins J

How new enzymes evolve from old ones.

BIOCHEMISTRY. 2001 JUL 24; 40 (29): 8633-8633

250 Petsko GA

Structural enzymology over the last 40 years.

BIOCHEMISTRY. 2001 JUL 24; 40 (29): 8642-8642

251 Ringe D, Petsko GA, Desmarais W, Holz RC

Bridged bimetallic enzymes: Two heads are better than one.

BIOCHEMISTRY. 2001 JUL 24; 40 (29): 8661-8661

258 Hadfield A, Shammas C, Kryger G, Ringe D, et al.

Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase

BIOCHEMISTRY. 2001 DEC 4; 40 (48): 14475-14483

261 Bahnson BJ, Anderson VE, Petsko GA

Structural mechanism of enoyl-CoA hydratase: Three atoms from a single water are added in either an E1cb stepwise or concerted fashion

BIOCHEMISTRY. 2002 FEB 26; 41 (8): 2621-2629

267 Gan L, Petsko GA, Hedstrom L

Crystal structure of a ternary complex of Tritrichomonas foetus inosine 5 '-monophosphate dehydrogenase: NAD(+) orients the active site loop for catalysis

BIOCHEMISTRY. 2002 NOV 5; 41 (44): 13309-13317

100

281 Gan L, Seyedsayamdost MR, Shuto S, Matsuda A, et al.

The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase

BIOCHEMISTRY. 2003 FEB 4; 42 (4): 857-863

Publications by GA Petsko	Historiographs	Glossary HistCite Guide About Grand Totals: LCS 550, GCS 18132 Collection span: 1969 - 2008
List of All Records