HistCite - Publications by GA Petsko

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#	Date / Author / Journal	LCS	GCS	LCR	CR
51	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
52	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
53	48 MOWBRAY SL, PETSKO GA THE X-RAY STRUCTURE OF THE PERIPLASMIC GALACTOSE BINDING-PROTEIN FROM SALMONELLA-TYPHIMURIUM AT 3.0-A RESOLUTION JOURNAL OF BIOLOGICAL CHEMISTRY. 1983; 258 (13): 7991-7997	0	39	2	44
54	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
55	192 SCHIERING N, TAO X, ZENG HY, MURPHY JR, et al. STRUCTURES OF THE APO-ACTIVATED AND THE METAL ION-ACTIVATED FORMS OF THE DIPHTHERIA TOX REPRESSOR FROM CORYNEBACTERIUM-DIPHTHERIAE PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1995 OCT 10; 92 (21): 9843-9850	0	59	1	44
56	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
57	45 SEATON BA, HEAD JF, LORD RC, PETSKO GA STUDIES OF CALMODULIN STRUCTURE - LASER RAMAN-SPECTROSCOPY OF BIOMOLECULES BIOCHEMISTRY. 1983; 22 (4): 973-978	1	18	1	43
58	246 Heymont J, Berenfeld L, Collins J, Kaganovich A, et al. TEP1, the yeast homolog of the human tumor suppressor gene PTEN/MMAC1/TEP1, is linked to the phosphatidylinositol pathway and plays a role in the developmental process of sporulation PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2000 NOV 7; 97 (23): 12672-12677	0	7	0	43
59	324 Pozharski E, Moulin A, Hewagama A, Shanafelt AB, et al. Diversity in hapten recognition: Structural study of an anti-cocaine antibody M82G2 JOURNAL OF MOLECULAR BIOLOGY. 2005 JUN 10; 349 (3): 570-582	0	3	1	43
60	365 Liu DL, Pozharski E, Lepore BW, Fu MM, et al. Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-Amino-4, 5-dihydro-2-thiophenecarboxylic acid reveals "A tale of two mechanisms" BIOCHEMISTRY. 2007 SEP 18; 46 (37): 10517-10527	0	0	2	43
#	Date / Author / Journal	LCS	GCS	LCR	CR
61	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
62	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
63	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
64	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
65	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
66	82 CASAL JI, AHERN TJ, DAVENPORT RC, PETSKO GA, et al. SUBUNIT INTERFACE OF TRIOSEPHOSPHATE ISOMERASE - SITE-DIRECTED MUTAGENESIS AND CHARACTERIZATION OF THE ALTERED ENZYME BIOCHEMISTRY. 1987 MAR 10; 26 (5): 1258-1264	6	57	3	40
67	87 KOZELKA J, ARCHER S, PETSKO GA, LIPPARD SJ, et al. MOLECULAR MECHANICS MODELING OF OLIGONUCLEOTIDE ADDUCTS OF THE ANTITUMOR DRUG CIS-DIAMMINEDICHLOROPLATINUM(II) BIOPOLYMERS. 1987 AUG; 26 (8): 1245-1271	0	76	2	40
68	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
69	303 Holyoak T, Kettner CA, Petsko GA, Fuller RS, et al. Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases BIOCHEMISTRY. 2004 MAR 9; 43 (9): 2412-2421	0	19	3	40
70	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
#	Date / Author / Journal	LCS	GCS	LCR	CR
71	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
72	221 Zavodszky P, Kardos J, Svingor A, Petsko GA Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1998 JUN 23; 95 (13): 7406-7411	3	234	1	39
73	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
74	377 Liu D, Momb J, Thomas PW, Moulin A, et al. Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures BIOCHEMISTRY. 2008 JUL 22; 47 (29): 7706-7714	1	1	4	39
75	30 FRAUENFELDER H, PETSKO GA, TSERNOGLOU D TEMPERATURE-DEPENDENT X-RAY-DIFFRACTION AS A PROBE OF PROTEIN STRUCTURAL DYNAMICS NATURE. 1979; 280 (5723): 558-563	12	865	2	38
76	68 BURLEY SK, PETSKO GA AROMATIC-AROMATIC INTERACTION - A MECHANISM OF PROTEIN-STRUCTURE STABILIZATION SCIENCE. 1985; 229 (4708): 23-28	9	1313	0	38
77	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
78	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
79	363 Munih P, Moulin A, Stamper CC, Bennett B, et al. X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica JOURNAL OF INORGANIC BIOCHEMISTRY. 2007 AUG; 101 (8): 1099-1107	0	0	2	38
80	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
#	Date / Author / Journal	LCS	GCS	LCR	CR
81	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
82	205 Vitkup D, Petsko GA, Karplus M A comparison between molecular dynamics and X-ray results for dissociated CO in myoglobin NATURE STRUCTURAL BIOLOGY. 1997 MAR; 4 (3): 202-208	1	57	2	37
83	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
84	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
85	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
86	240 Jeffrey CJ, Gloss LM, Petsko GA, Ringe D The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase PROTEIN ENGINEERING. 2000 FEB; 13 (2): 105-112	1	10	0	36
87	31 FRAUENFELDER H, PETSKO GA STRUCTURAL DYNAMICS OF LIGANDED MYOGLOBIN BIOPHYSICAL JOURNAL. 1980; 32 (1): 465-483	4	49	3	35
88	111 ROSE DR, STRONG RK, MARGOLIES MN, GEFTER ML, et al. CRYSTAL-STRUCTURE OF THE ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-ARSONATE MONOCLONAL-ANTIBODY 36-71 AT 2.9-A RESOLUTION PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1990 JAN; 87 (1): 338-342	2	33	0	35
89	115 SCHLICHTING I, ALMO SC, RAPP G, WILSON K, et al. TIME-RESOLVED X-RAY CRYSTALLOGRAPHIC STUDY OF THE CONFORMATIONAL CHANGE IN HA-RAS P21 PROTEIN ON GTP HYDROLYSIS NATURE. 1990 MAY 24; 345 (6273): 309-315	5	382	1	35
90	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
#	Date / Author / Journal	LCS	GCS	LCR	CR
91	343 Das C, Hoang QQ, Kreinbring CA, Luchansky SJ, et al. Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2006 MAR 21; 103 (12): 4675-4680	1	21	0	35
92	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
93	174 MATTOS C, PETSKO GA, KARPLUS M ANALYSIS OF 2-RESIDUE TURNS IN PROTEINS JOURNAL OF MOLECULAR BIOLOGY. 1994 MAY 20; 238 (5): 733-747	0	43	1	34
94	180 BABBITT PC, MRACHKO GT, HASSON MS, HUISMAN GW, et al. FUNCTIONALLY DIVERSE ENZYME SUPERFAMILY THAT ABSTRACTS THE ALPHA-PROTONS OF CARBOXYLIC-ACIDS SCIENCE. 1995 FEB 24; 267 (5201): 1159-1161	4	107	1	34
95	234 Hadfield A, Kryger G, Ouyang J, Petsko GA, et al. Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis JOURNAL OF MOLECULAR BIOLOGY. 1999 JUN 18; 289 (4): 991-1002	1	34	1	34
96	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
97	11 BANNER DW, BLOOMER AC, PETSKO GA, PHILLIPS DC, et al. STRUCTURE OF CHICKEN MUSCLE TRIOSE PHOSPHATE ISOMERASE DETERMINED CRYSTALLOGRAPHICALLY AT 2.5A RESOLUTION USING AMINO-ACID SEQUENCE DATA NATURE. 1975; 255 (5510): 609-614	24	561	2	33
98	102 BRUNGER AT, KARPLUS M, PETSKO GA CRYSTALLOGRAPHIC REFINEMENT BY SIMULATED ANNEALING - APPLICATION TO CRAMBIN ACTA CRYSTALLOGRAPHICA SECTION A. 1989 JAN 1; 45: 50-61	2	287	2	33
99	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
100	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

Date / Author / Journal

LCS

GCS

LCR

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

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

48 MOWBRAY SL, PETSKO GA

THE X-RAY STRUCTURE OF THE PERIPLASMIC GALACTOSE BINDING-PROTEIN FROM SALMONELLA-TYPHIMURIUM AT 3.0-A RESOLUTION

JOURNAL OF BIOLOGICAL CHEMISTRY. 1983; 258 (13): 7991-7997

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

192 SCHIERING N, TAO X, ZENG HY, MURPHY JR, et al.

STRUCTURES OF THE APO-ACTIVATED AND THE METAL ION-ACTIVATED FORMS OF THE DIPHTHERIA TOX REPRESSOR FROM CORYNEBACTERIUM-DIPHTHERIAE

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1995 OCT 10; 92 (21): 9843-9850

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

45 SEATON BA, HEAD JF, LORD RC, PETSKO GA

STUDIES OF CALMODULIN STRUCTURE - LASER RAMAN-SPECTROSCOPY OF BIOMOLECULES

BIOCHEMISTRY. 1983; 22 (4): 973-978

246 Heymont J, Berenfeld L, Collins J, Kaganovich A, et al.

TEP1, the yeast homolog of the human tumor suppressor gene PTEN/MMAC1/TEP1, is linked to the phosphatidylinositol pathway and plays a role in the developmental process of sporulation

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2000 NOV 7; 97 (23): 12672-12677

324 Pozharski E, Moulin A, Hewagama A, Shanafelt AB, et al.

Diversity in hapten recognition: Structural study of an anti-cocaine antibody M82G2

JOURNAL OF MOLECULAR BIOLOGY. 2005 JUN 10; 349 (3): 570-582

365 Liu DL, Pozharski E, Lepore BW, Fu MM, et al.

Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-Amino-4, 5-dihydro-2-thiophenecarboxylic acid reveals "A tale of two mechanisms"

BIOCHEMISTRY. 2007 SEP 18; 46 (37): 10517-10527

Date / Author / Journal

LCS

GCS

LCR

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

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

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

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

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

82 CASAL JI, AHERN TJ, DAVENPORT RC, PETSKO GA, et al.

SUBUNIT INTERFACE OF TRIOSEPHOSPHATE ISOMERASE - SITE-DIRECTED MUTAGENESIS AND CHARACTERIZATION OF THE ALTERED ENZYME

BIOCHEMISTRY. 1987 MAR 10; 26 (5): 1258-1264

87 KOZELKA J, ARCHER S, PETSKO GA, LIPPARD SJ, et al.

MOLECULAR MECHANICS MODELING OF OLIGONUCLEOTIDE ADDUCTS OF THE ANTITUMOR DRUG CIS-DIAMMINEDICHLOROPLATINUM(II)

BIOPOLYMERS. 1987 AUG; 26 (8): 1245-1271

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

303 Holyoak T, Kettner CA, Petsko GA, Fuller RS, et al.

Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases

BIOCHEMISTRY. 2004 MAR 9; 43 (9): 2412-2421

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

Date / Author / Journal

LCS

GCS

LCR

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

221 Zavodszky P, Kardos J, Svingor A, Petsko GA

Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1998 JUN 23; 95 (13): 7406-7411

234

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

377 Liu D, Momb J, Thomas PW, Moulin A, et al.

Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures

BIOCHEMISTRY. 2008 JUL 22; 47 (29): 7706-7714

30 FRAUENFELDER H, PETSKO GA, TSERNOGLOU D

TEMPERATURE-DEPENDENT X-RAY-DIFFRACTION AS A PROBE OF PROTEIN STRUCTURAL DYNAMICS

NATURE. 1979; 280 (5723): 558-563

865

68 BURLEY SK, PETSKO GA

AROMATIC-AROMATIC INTERACTION - A MECHANISM OF PROTEIN-STRUCTURE STABILIZATION

SCIENCE. 1985; 229 (4708): 23-28

1313

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

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

363 Munih P, Moulin A, Stamper CC, Bennett B, et al.

X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica

JOURNAL OF INORGANIC BIOCHEMISTRY. 2007 AUG; 101 (8): 1099-1107

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

Date / Author / Journal

LCS

GCS

LCR

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

205 Vitkup D, Petsko GA, Karplus M

A comparison between molecular dynamics and X-ray results for dissociated CO in myoglobin

NATURE STRUCTURAL BIOLOGY. 1997 MAR; 4 (3): 202-208

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

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

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

240 Jeffrey CJ, Gloss LM, Petsko GA, Ringe D

The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase

PROTEIN ENGINEERING. 2000 FEB; 13 (2): 105-112

31 FRAUENFELDER H, PETSKO GA

STRUCTURAL DYNAMICS OF LIGANDED MYOGLOBIN

BIOPHYSICAL JOURNAL. 1980; 32 (1): 465-483

111 ROSE DR, STRONG RK, MARGOLIES MN, GEFTER ML, et al.

CRYSTAL-STRUCTURE OF THE ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-ARSONATE MONOCLONAL-ANTIBODY 36-71 AT 2.9-A RESOLUTION

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 1990 JAN; 87 (1): 338-342

115 SCHLICHTING I, ALMO SC, RAPP G, WILSON K, et al.

TIME-RESOLVED X-RAY CRYSTALLOGRAPHIC STUDY OF THE CONFORMATIONAL CHANGE IN HA-RAS P21 PROTEIN ON GTP HYDROLYSIS

NATURE. 1990 MAY 24; 345 (6273): 309-315

382

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

Date / Author / Journal

LCS

GCS

LCR

343 Das C, Hoang QQ, Kreinbring CA, Luchansky SJ, et al.

Structural basis for conformational plasticity of the Parkinson's disease-associated ubiquitin hydrolase UCH-L1

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2006 MAR 21; 103 (12): 4675-4680

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

174 MATTOS C, PETSKO GA, KARPLUS M

ANALYSIS OF 2-RESIDUE TURNS IN PROTEINS

JOURNAL OF MOLECULAR BIOLOGY. 1994 MAY 20; 238 (5): 733-747

180 BABBITT PC, MRACHKO GT, HASSON MS, HUISMAN GW, et al.

FUNCTIONALLY DIVERSE ENZYME SUPERFAMILY THAT ABSTRACTS THE ALPHA-PROTONS OF CARBOXYLIC-ACIDS

SCIENCE. 1995 FEB 24; 267 (5201): 1159-1161

107

234 Hadfield A, Kryger G, Ouyang J, Petsko GA, et al.

Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis

JOURNAL OF MOLECULAR BIOLOGY. 1999 JUN 18; 289 (4): 991-1002

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

11 BANNER DW, BLOOMER AC, PETSKO GA, PHILLIPS DC, et al.

STRUCTURE OF CHICKEN MUSCLE TRIOSE PHOSPHATE ISOMERASE DETERMINED CRYSTALLOGRAPHICALLY AT 2.5A RESOLUTION USING AMINO-ACID SEQUENCE DATA

NATURE. 1975; 255 (5510): 609-614

561

102 BRUNGER AT, KARPLUS M, PETSKO GA

CRYSTALLOGRAPHIC REFINEMENT BY SIMULATED ANNEALING - APPLICATION TO CRAMBIN

ACTA CRYSTALLOGRAPHICA SECTION A. 1989 JAN 1; 45: 50-61

287

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

100

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

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