HistCite - Publications by GA Petsko

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#	Date / Author / Journal	LCS	GCS	LCR	CR
1	348 Ding XC, Rasmussen BF, Petsko GA, Ringe D Direct crystallographic observation of an acyl-enzyme intermediate in the elastase-catalyzed hydrolysis of a peptidyl ester substrate: Exploiting the "glass transition" in protein dynamics BIOORGANIC CHEMISTRY. 2006 DEC; 34 (6): 410-423	0	1	13	28
2	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
3	67 RINGE D, PETSKO GA MAPPING PROTEIN DYNAMICS BY X-RAY-DIFFRACTION PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY. 1985; 45 (3): 197-235	4	109	11	137
4	93 BURLEY SK, PETSKO GA WEAKLY POLAR INTERACTIONS IN PROTEINS ADVANCES IN PROTEIN CHEMISTRY. 1988; 39: 125-189	6	611	11	140
5	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
6	239 Petsko GA, Ringe D Observation of unstable species in enzyme-catalyzed transformations using protein crystallography CURRENT OPINION IN CHEMICAL BIOLOGY. 2000 FEB; 4 (1): 89-94	2	21	11	41
7	55 DOUZOU P, PETSKO GA PROTEINS AT WORK - STOP-ACTION PICTURES AT SUBZERO TEMPERATURES ADVANCES IN PROTEIN CHEMISTRY. 1984; 36: 245-361	4	88	10	137
8	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
9	151 PETSKO GA ART IS LONG AND TIME IS FLEETING - THE CURRENT PROBLEMS AND FUTURE-PROSPECTS FOR TIME-RESOLVED ENZYME CRYSTALLOGRAPHY PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES A-MATHEMATICAL PHYSICAL AND ENGINEERING SCIENCES. 1992 AUG 15; 340 (1657): 323-334	2	6	10	26
10	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
#	Date / Author / Journal	LCS	GCS	LCR	CR
11	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
12	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
13	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
14	287 Ringe D, Petsko GA The 'glass transition' in protein dynamics: what it is, why it occurs, and how to exploit it BIOPHYSICAL CHEMISTRY. 2003 SEP; 105 (2-3): 667-680	1	30	9	33
15	56 PETSKO GA, RINGE D FLUCTUATIONS IN PROTEIN-STRUCTURE FROM X-RAY-DIFFRACTION ANNUAL REVIEW OF BIOPHYSICS AND BIOENGINEERING. 1984; 13: 331-371	14	168	8	120
16	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
17	186 KENYON GL, GERLT JA, PETSKO GA, KOZARICH JW MANDELATE RACEMASE - STRUCTURE-FUNCTION STUDIES OF A PSEUDOSYMMETRIC ENZYME ACCOUNTS OF CHEMICAL RESEARCH. 1995 APR; 28 (4): 178-186	0	73	8	56
18	76 ALBER TC, DAVENPORT RC, GIAMMONA DA, LOLIS E, et al. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF YEAST TRIOSEPHOSPHATE ISOMERASE - WHAT CAN WE LEARN ABOUT CATALYSIS FROM A SIMPLE ENZYME COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY. 1987; 52: 603-613	10	40	7	39
19	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
20	196 JosephMcCarthy D, Petsko GA, Karplus M Use of a minimum perturbation approach to predict TIM mutant structures PROTEIN ENGINEERING. 1995 NOV; 8 (11): 1103-1115	0	8	7	23
#	Date / Author / Journal	LCS	GCS	LCR	CR
21	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
22	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
23	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
24	238 Vitkup D, Ringe D, Petsko GA, Karplus M Solvent mobility and the protein 'glass' transition NATURE STRUCTURAL BIOLOGY. 2000 JAN; 7 (1): 34-38	2	158	6	38
25	46 ALBER T, GILBERT WA, PONZI DR, PETSKO GA THE ROLE OF MOBILITY IN THE SUBSTRATE BINDING AND CATALYTIC MACHINERY OF ENZYMES CIBA FOUNDATION SYMPOSIA. 1983; 93: 4-18	1	53	5	17
26	73 KURIYAN J, WILZ S, KARPLUS M, PETSKO GA X-RAY STRUCTURE AND REFINEMENT OF CARBON-MONOXY (FE-II)-MYOGLOBIN AT 1.5-A RESOLUTION JOURNAL OF MOLECULAR BIOLOGY. 1986 NOV 5; 192 (1): 133-154	6	494	5	68
27	78 FRAUENFELDER H, HARTMANN H, KARPLUS M, KUNTZ ID, et al. THERMAL-EXPANSION OF A PROTEIN BIOCHEMISTRY. 1987 JAN 13; 26 (1): 254-261	1	149	5	27
28	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
29	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
30	226 Hasson MS, Schlichting I, Moulai J, Taylor K, et al. Evolution of an enzyme active site: The structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1998 SEP 1; 95 (18): 10396-10401	1	56	5	36
#	Date / Author / Journal	LCS	GCS	LCR	CR
31	306 Fenn TD, Ringe D, Petsko GA Xylose isomerase in substrate and inhibitor Michaelis States: Atomic resolution studies of a metal-mediated hydride shift BIOCHEMISTRY. 2004 JUN 1; 43 (21): 6464-6474	0	19	5	41
32	66 PETSKO GA PREPARATION OF ISOMORPHOUS HEAVY-ATOM DERIVATIVES METHODS IN ENZYMOLOGY. 1985; 114: 147-156	1	46	4	19
33	77 KURIYAN J, KARPLUS M, PETSKO GA ESTIMATION OF UNCERTAINTIES IN X-RAY REFINEMENT RESULTS BY USE OF PERTURBED STRUCTURES PROTEINS-STRUCTURE FUNCTION AND GENETICS. 1987; 2 (1): 1-12	2	17	4	25
34	97 NICKBARG EB, DAVENPORT RC, PETSKO GA, KNOWLES JR TRIOSEPHOSPHATE ISOMERASE - REMOVAL OF A PUTATIVELY ELECTROPHILIC HISTIDINE RESIDUE RESULTS IN A SUBTLE CHANGE IN CATALYTIC MECHANISM BIOCHEMISTRY. 1988 AUG 9; 27 (16): 5948-5960	12	95	4	53
35	98 TILTON RF, PETSKO GA A STRUCTURE OF SPERM WHALE MYOGLOBIN AT A NITROGEN GAS-PRESSURE OF 145 ATMOSPHERES BIOCHEMISTRY. 1988 AUG 23; 27 (17): 6574-6582	0	21	4	47
36	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
37	108 BURLEY SK, PETSKO GA ELECTROSTATIC INTERACTIONS IN AROMATIC OLIGOPEPTIDES CONTRIBUTE TO PROTEIN STABILITY TRENDS IN BIOTECHNOLOGY. 1989 DEC; 7 (12): 354-359	0	29	4	31
38	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
39	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
40	135 STODDARD BL, KOENIGS P, PORTER N, PETRATOS K, et al. OBSERVATION OF THE LIGHT-TRIGGERED BINDING OF PYRONE TO CHYMOTRYPSIN BY LAUE X-RAY CRYSTALLOGRAPHY PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1991 JUL; 88 (13): 5503-5507	1	43	4	25
#	Date / Author / Journal	LCS	GCS	LCR	CR
41	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
42	158 PETSKO GA, KENYON GL, GERLT JA, RINGE D, et al. ON THE ORIGIN OF ENZYMATIC SPECIES TRENDS IN BIOCHEMICAL SCIENCES. 1993 OCT; 18 (10): 372-376	3	81	4	23
43	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
44	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
45	247 Petsko GA Structural basis of thermostability in hyperthermophilic proteins, or "there's more than one way to skin a cat" HYPERTHERMOPHILIC ENZYMES, PT C. 2001; 334: 469-478	0	57	4	37
46	288 Holyoak T, Fenn TD, Wilson MA, Moulin AG, et al. Malonate: a versatile cryoprotectant and stabilizing solution for salt-grown macromolecular crystals ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. 2003 DEC; 59: 2356-2358	1	16	4	8
47	302 Wilson MA, St Amour CV, Collins JL, Ringe D, et al. The 1.8-angstrom resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/Pfpl superfamily PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2004 FEB 10; 101 (6): 1531-1536	3	21	4	47
48	309 Yang J, Wang Y, Woolridge EM, Arora V, et al. Crystal structure of 3-carboxy-cis, cis-muconate lactonizing enzyme from Pseudomonas putida, a fumarase class II type cycloisomerase: Enzyme evolution in parallel pathways BIOCHEMISTRY. 2004 AUG 17; 43 (32): 10424-10434	0	7	4	46
49	328 Wilson MA, Ringe D, Petsko GA The atomic resolution crystal structure of the YajL (ThiJ) protein from Escherichia coli: A close prokaryotic homologue of the Parkinsonism-associated protein DJ-1 JOURNAL OF MOLECULAR BIOLOGY. 2005 OCT 28; 353 (3): 678-691	0	8	4	70
50	366 Liu DL, Thomas PW, Momb J, Hoang QYQ, et al. Structure and specificity of a quorum-quenching lactonase (AiiB) from Agrobacterium tumefaciens BIOCHEMISTRY. 2007 OCT 23; 46 (42): 11789-11799	2	4	4	52

Date / Author / Journal

LCS

GCS

LCR

348 Ding XC, Rasmussen BF, Petsko GA, Ringe D

Direct crystallographic observation of an acyl-enzyme intermediate in the elastase-catalyzed hydrolysis of a peptidyl ester substrate: Exploiting the "glass transition" in protein dynamics

BIOORGANIC CHEMISTRY. 2006 DEC; 34 (6): 410-423

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

67 RINGE D, PETSKO GA

MAPPING PROTEIN DYNAMICS BY X-RAY-DIFFRACTION

PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY. 1985; 45 (3): 197-235

109

137

93 BURLEY SK, PETSKO GA

WEAKLY POLAR INTERACTIONS IN PROTEINS

ADVANCES IN PROTEIN CHEMISTRY. 1988; 39: 125-189

611

140

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

239 Petsko GA, Ringe D

Observation of unstable species in enzyme-catalyzed transformations using protein crystallography

CURRENT OPINION IN CHEMICAL BIOLOGY. 2000 FEB; 4 (1): 89-94

55 DOUZOU P, PETSKO GA

PROTEINS AT WORK - STOP-ACTION PICTURES AT SUBZERO TEMPERATURES

ADVANCES IN PROTEIN CHEMISTRY. 1984; 36: 245-361

137

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

151 PETSKO GA

ART IS LONG AND TIME IS FLEETING - THE CURRENT PROBLEMS AND FUTURE-PROSPECTS FOR TIME-RESOLVED ENZYME CRYSTALLOGRAPHY

PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY OF LONDON SERIES A-MATHEMATICAL PHYSICAL AND ENGINEERING SCIENCES. 1992 AUG 15; 340 (1657): 323-334

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

Date / Author / Journal

LCS

GCS

LCR

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

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

287 Ringe D, Petsko GA

The 'glass transition' in protein dynamics: what it is, why it occurs, and how to exploit it

BIOPHYSICAL CHEMISTRY. 2003 SEP; 105 (2-3): 667-680

56 PETSKO GA, RINGE D

FLUCTUATIONS IN PROTEIN-STRUCTURE FROM X-RAY-DIFFRACTION

ANNUAL REVIEW OF BIOPHYSICS AND BIOENGINEERING. 1984; 13: 331-371

168

120

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

186 KENYON GL, GERLT JA, PETSKO GA, KOZARICH JW

MANDELATE RACEMASE - STRUCTURE-FUNCTION STUDIES OF A PSEUDOSYMMETRIC ENZYME

ACCOUNTS OF CHEMICAL RESEARCH. 1995 APR; 28 (4): 178-186

76 ALBER TC, DAVENPORT RC, GIAMMONA DA, LOLIS E, et al.

CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF YEAST TRIOSEPHOSPHATE ISOMERASE - WHAT CAN WE LEARN ABOUT CATALYSIS FROM A SIMPLE ENZYME

COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY. 1987; 52: 603-613

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

196 JosephMcCarthy D, Petsko GA, Karplus M

Use of a minimum perturbation approach to predict TIM mutant structures

PROTEIN ENGINEERING. 1995 NOV; 8 (11): 1103-1115

Date / Author / Journal

LCS

GCS

LCR

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

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

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

238 Vitkup D, Ringe D, Petsko GA, Karplus M

Solvent mobility and the protein 'glass' transition

NATURE STRUCTURAL BIOLOGY. 2000 JAN; 7 (1): 34-38

158

46 ALBER T, GILBERT WA, PONZI DR, PETSKO GA

THE ROLE OF MOBILITY IN THE SUBSTRATE BINDING AND CATALYTIC MACHINERY OF ENZYMES

CIBA FOUNDATION SYMPOSIA. 1983; 93: 4-18

73 KURIYAN J, WILZ S, KARPLUS M, PETSKO GA

X-RAY STRUCTURE AND REFINEMENT OF CARBON-MONOXY (FE-II)-MYOGLOBIN AT 1.5-A RESOLUTION

JOURNAL OF MOLECULAR BIOLOGY. 1986 NOV 5; 192 (1): 133-154

494

78 FRAUENFELDER H, HARTMANN H, KARPLUS M, KUNTZ ID, et al.

THERMAL-EXPANSION OF A PROTEIN

BIOCHEMISTRY. 1987 JAN 13; 26 (1): 254-261

149

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

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

226 Hasson MS, Schlichting I, Moulai J, Taylor K, et al.

Evolution of an enzyme active site: The structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolase

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1998 SEP 1; 95 (18): 10396-10401

Date / Author / Journal

LCS

GCS

LCR

306 Fenn TD, Ringe D, Petsko GA

Xylose isomerase in substrate and inhibitor Michaelis States: Atomic resolution studies of a metal-mediated hydride shift

BIOCHEMISTRY. 2004 JUN 1; 43 (21): 6464-6474

66 PETSKO GA

PREPARATION OF ISOMORPHOUS HEAVY-ATOM DERIVATIVES

METHODS IN ENZYMOLOGY. 1985; 114: 147-156

77 KURIYAN J, KARPLUS M, PETSKO GA

ESTIMATION OF UNCERTAINTIES IN X-RAY REFINEMENT RESULTS BY USE OF PERTURBED STRUCTURES

PROTEINS-STRUCTURE FUNCTION AND GENETICS. 1987; 2 (1): 1-12

97 NICKBARG EB, DAVENPORT RC, PETSKO GA, KNOWLES JR

TRIOSEPHOSPHATE ISOMERASE - REMOVAL OF A PUTATIVELY ELECTROPHILIC HISTIDINE RESIDUE RESULTS IN A SUBTLE CHANGE IN CATALYTIC MECHANISM

BIOCHEMISTRY. 1988 AUG 9; 27 (16): 5948-5960

98 TILTON RF, PETSKO GA

A STRUCTURE OF SPERM WHALE MYOGLOBIN AT A NITROGEN GAS-PRESSURE OF 145 ATMOSPHERES

BIOCHEMISTRY. 1988 AUG 23; 27 (17): 6574-6582

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

108 BURLEY SK, PETSKO GA

ELECTROSTATIC INTERACTIONS IN AROMATIC OLIGOPEPTIDES CONTRIBUTE TO PROTEIN STABILITY

TRENDS IN BIOTECHNOLOGY. 1989 DEC; 7 (12): 354-359

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

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

135 STODDARD BL, KOENIGS P, PORTER N, PETRATOS K, et al.

OBSERVATION OF THE LIGHT-TRIGGERED BINDING OF PYRONE TO CHYMOTRYPSIN BY LAUE X-RAY CRYSTALLOGRAPHY

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1991 JUL; 88 (13): 5503-5507

Date / Author / Journal

LCS

GCS

LCR

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

158 PETSKO GA, KENYON GL, GERLT JA, RINGE D, et al.

ON THE ORIGIN OF ENZYMATIC SPECIES

TRENDS IN BIOCHEMICAL SCIENCES. 1993 OCT; 18 (10): 372-376

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

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

247 Petsko GA

Structural basis of thermostability in hyperthermophilic proteins, or "there's more than one way to skin a cat"

HYPERTHERMOPHILIC ENZYMES, PT C. 2001; 334: 469-478

288 Holyoak T, Fenn TD, Wilson MA, Moulin AG, et al.

Malonate: a versatile cryoprotectant and stabilizing solution for salt-grown macromolecular crystals

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. 2003 DEC; 59: 2356-2358

302 Wilson MA, St Amour CV, Collins JL, Ringe D, et al.

The 1.8-angstrom resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: A member of the DJ-1/ThiJ/Pfpl superfamily

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2004 FEB 10; 101 (6): 1531-1536

309 Yang J, Wang Y, Woolridge EM, Arora V, et al.

Crystal structure of 3-carboxy-cis, cis-muconate lactonizing enzyme from Pseudomonas putida, a fumarase class II type cycloisomerase: Enzyme evolution in parallel pathways

BIOCHEMISTRY. 2004 AUG 17; 43 (32): 10424-10434

328 Wilson MA, Ringe D, Petsko GA

The atomic resolution crystal structure of the YajL (ThiJ) protein from Escherichia coli: A close prokaryotic homologue of the Parkinsonism-associated protein DJ-1

JOURNAL OF MOLECULAR BIOLOGY. 2005 OCT 28; 353 (3): 678-691

366 Liu DL, Thomas PW, Momb J, Hoang QYQ, et al.

Structure and specificity of a quorum-quenching lactonase (AiiB) from Agrobacterium tumefaciens

BIOCHEMISTRY. 2007 OCT 23; 46 (42): 11789-11799

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