| Year |
Citation |
Score |
| 2024 |
Hossain MA, Sarin R, Donnelly DP, Miller BC, Weiss A, McAlary L, Antonyuk SV, Salisbury JP, Amin J, Conway JB, Watson SS, Winters JN, Xu Y, Alam N, Brahme RR, ... ... Petsko GA, et al. Evaluating protein cross-linking as a therapeutic strategy to stabilize SOD1 variants in a mouse model of familial ALS. Plos Biology. 22: e3002462. PMID 38289969 DOI: 10.1371/journal.pbio.3002462 |
0.685 |
|
| 2021 |
Fevga C, Park Y, Lohmann E, Kievit AJ, Breedveld GJ, Ferraro F, de Boer L, van Minkelen R, Hanagasi H, Boon A, Wang W, Petsko GA, Hoang QQ, Emre M, Bonifati V. A new alpha-synuclein missense variant (Thr72Met) in two Turkish families with Parkinson's disease. Parkinsonism & Related Disorders. 89: 63-72. PMID 34229155 DOI: 10.1016/j.parkreldis.2021.06.023 |
0.608 |
|
| 2020 |
Rajan S, Jang Y, Kim CH, Kim W, Toh HT, Jeon J, Song B, Serra A, Lescar J, Yoo JY, Beldar S, Ye H, Kang C, Liu XW, Feitosa M, ... ... Petsko GA, et al. PGE1 and PGA1 bind to Nurr1 and activate its transcriptional function. Nature Chemical Biology. PMID 32451509 DOI: 10.1038/S41589-020-0553-6 |
0.32 |
|
| 2018 |
Gandhi AK, Kim WM, Sun ZJ, Huang YH, Bonsor DA, Sundberg EJ, Kondo Y, Wagner G, Kuchroo VK, Petsko G, Blumberg RS. High resolution X-ray and NMR structural study of human T-cell immunoglobulin and mucin domain containing protein-3. Scientific Reports. 8: 17512. PMID 30504845 DOI: 10.1038/S41598-018-35754-0 |
0.353 |
|
| 2018 |
Singh V, Yang J, Yin J, Cole R, Tse M, Berman DE, Small SA, Petsko G, Donowitz M. Cholera toxin inhibits SNX27-retromer mediated delivery of cargo proteins to the plasma membrane. Journal of Cell Science. PMID 30030371 DOI: 10.1242/Jcs.218610 |
0.337 |
|
| 2018 |
Tu Y, Kreinbring CA, Hill M, Liu C, Petsko GA, McCune CD, Berkowitz DB, Liu D, Ringe D. Crystal Structures of Cystathionine β-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time. Biochemistry. PMID 29630349 DOI: 10.1021/Acs.Biochem.8B00092 |
0.725 |
|
| 2018 |
Ringe D, Kreinbring C, Wilson M, Kovalevsky A, Blakeley M, Fisher Z, Lazar L, Moulin A, Novak W, Petsko G. The missing atom in function: reliability of the determination of hydrogen positions in protein structures. Acta Crystallographica Section a Foundations and Advances. 74: a30-a30. DOI: 10.1107/S0108767318099695 |
0.779 |
|
| 2017 |
Campbell BC, Petsko GA, Liu CF. Crystal Structure of Green Fluorescent Protein Clover and Design of Clover-Based Redox Sensors. Structure (London, England : 1993). PMID 29307487 DOI: 10.1016/J.Str.2017.12.006 |
0.358 |
|
| 2017 |
Wu R, Sanishvili R, Belitsky BR, Juncosa JI, Le HV, Lehrer HJ, Farley M, Silverman RB, Petsko GA, Ringe D, Liu D. PLP and GABA trigger GabR-mediated transcription regulation in Bacillus subtilis via external aldimine formation. Proceedings of the National Academy of Sciences of the United States of America. PMID 28348215 DOI: 10.1073/Pnas.1703019114 |
0.71 |
|
| 2017 |
Naffin-Olivos JL, Daab A, White A, Goldfarb NE, Milne AC, Liu D, Baikovitz J, Dunn BM, Rengarajan J, Petsko GA, Ringe D. Structure Determination of Mycobacterium tuberculosis Serine Protease Hip1 (Rv2224c). Biochemistry. PMID 28346784 DOI: 10.1021/Acs.Biochem.6B01066 |
0.766 |
|
| 2017 |
Zahniser MP, Prasad S, Kneen MM, Kreinbring CA, Petsko GA, Ringe D, McLeish MJ. Structure and mechanism of benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633, a member of the Class 3 aldehyde dehydrogenase superfamily. Protein Engineering, Design & Selection : Peds. 1-8. PMID 28338942 DOI: 10.1093/Protein/Gzx015 |
0.565 |
|
| 2017 |
Deshpande AR, Pochapsky TC, Petsko GA, Ringe D. Dual chemistry catalyzed by human acireductone dioxygenase. Protein Engineering, Design & Selection : Peds. PMID 28062648 DOI: 10.1093/Protein/Gzw078 |
0.543 |
|
| 2016 |
Liu CF, Brandt GS, Hoang QQ, Naumova N, Lazarevic V, Hwang ES, Dekker J, Glimcher LH, Ringe D, Petsko GA. Crystal structure of the DNA binding domain of the transcription factor T-bet suggests simultaneous recognition of distant genome sites. Proceedings of the National Academy of Sciences of the United States of America. 113: E6572-E6581. PMID 27791029 DOI: 10.1073/Pnas.1613914113 |
0.78 |
|
| 2016 |
Bassil F, Fernagut PO, Bezard E, Pruvost A, Leste-Lasserre T, Hoang QQ, Ringe D, Petsko GA, Meissner WG. Reducing C-terminal truncation mitigates synucleinopathy and neurodegeneration in a transgenic model of multiple system atrophy. Proceedings of the National Academy of Sciences of the United States of America. PMID 27482103 DOI: 10.1073/Pnas.1609291113 |
0.71 |
|
| 2016 |
Wang W, Nguyen LT, Burlak C, Chegini F, Guo F, Chataway T, Ju S, Fisher OS, Miller DW, Datta D, Wu F, Wu CX, Landeru A, Wells JA, Cookson MR, ... ... Petsko GA, et al. Caspase-1 causes truncation and aggregation of the Parkinson's disease-associated protein α-synuclein. Proceedings of the National Academy of Sciences of the United States of America. PMID 27482083 DOI: 10.1073/Pnas.1610099113 |
0.764 |
|
| 2016 |
Huang YH, Zhu C, Kondo Y, Anderson AC, Gandhi A, Russell A, Dougan SK, Petersen BS, Melum E, Pertel T, Clayton KL, Raab M, Chen Q, Beauchemin N, Yazaki PJ, ... ... Petsko GA, et al. Corrigendum: CEACAM1 regulates TIM-3-mediated tolerance and exhaustion. Nature. PMID 26982724 DOI: 10.1038/Nature17421 |
0.315 |
|
| 2016 |
Deshpande AR, Wagenpfeil K, Pochapsky TC, Petsko GA, Ringe D. Metal-dependent function of a mammalian acireductone dioxygenase. Biochemistry. PMID 26858196 DOI: 10.1021/Acs.Biochem.5B01319 |
0.568 |
|
| 2015 |
Kim CH, Han BS, Moon J, Kim DJ, Shin J, Rajan S, Nguyen QT, Sohn M, Kim WG, Han M, Jeong I, Kim KS, Lee EH, Tu Y, Naffin-Olivos JL, ... ... Petsko GA, et al. Nuclear receptor Nurr1 agonists enhance its dual functions and improve behavioral deficits in an animal model of Parkinson's disease. Proceedings of the National Academy of Sciences of the United States of America. PMID 26124091 DOI: 10.1073/Pnas.1509742112 |
0.514 |
|
| 2015 |
Barmada SJ, Ju S, Arjun A, Batarse A, Archbold HC, Peisach D, Li X, Zhang Y, Tank EM, Qiu H, Huang EJ, Ringe D, Petsko GA, Finkbeiner S. Amelioration of toxicity in neuronal models of amyotrophic lateral sclerosis by hUPF1. Proceedings of the National Academy of Sciences of the United States of America. 112: 7821-6. PMID 26056265 DOI: 10.1073/Pnas.1509744112 |
0.771 |
|
| 2015 |
Berman DE, Ringe D, Petsko GA, Small SA. The use of pharmacological retromer chaperones in Alzheimer's disease and other endosomal-related disorders. Neurotherapeutics : the Journal of the American Society For Experimental Neurotherapeutics. 12: 12-8. PMID 25472693 DOI: 10.1007/S13311-014-0321-Y |
0.47 |
|
| 2015 |
Jackson KL, Dayton RD, Orchard EA, Ju S, Ringe D, Petsko GA, Maquat LE, Klein RL. Preservation of forelimb function by UPF1 gene therapy in a rat model of TDP-43-induced motor paralysis. Gene Therapy. 22: 20-8. PMID 25354681 DOI: 10.1038/Gt.2014.101 |
0.769 |
|
| 2015 |
Auclair J, Ringe D, Petsko G, Agar J. Cysteinylation of the ALS-Associated Protein SOD1 Confers Resistance to Oxidation The Faseb Journal. 29. DOI: 10.1096/Fasebj.29.1_Supplement.717.1 |
0.491 |
|
| 2015 |
Barmada SJ, Ju S, Arjun A, Batarse A, Archbold HC, Peisach D, Li X, Zhang Y, Tank EMH, Qiu H, Huang EJ, Ringe D, Petsko GA, Finkbeiner S. Amelioration of toxicity in neuronal models of amyotrophic lateral sclerosis by hUPF1 Proceedings of the National Academy of Sciences of the United States of America. 112: 7821-7826. DOI: 10.1073/pnas.1509744112 |
0.741 |
|
| 2014 |
Keedy DA, van den Bedem H, Sivak DA, Petsko GA, Ringe D, Wilson MA, Fraser JS. Crystal cryocooling distorts conformational heterogeneity in a model Michaelis complex of DHFR. Structure (London, England : 1993). 22: 899-910. PMID 24882744 DOI: 10.1016/J.Str.2014.04.016 |
0.66 |
|
| 2014 |
Naffin-Olivos JL, Georgieva M, Goldfarb N, Madan-Lala R, Dong L, Bizzell E, Valinetz E, Brandt GS, Yu S, Shabashvili DE, Ringe D, Dunn BM, Petsko GA, Rengarajan J. Mycobacterium tuberculosis Hip1 modulates macrophage responses through proteolysis of GroEL2. Plos Pathogens. 10: e1004132. PMID 24830429 DOI: 10.1371/Journal.Ppat.1004132 |
0.782 |
|
| 2014 |
Mecozzi VJ, Berman DE, Simoes S, Vetanovetz C, Awal MR, Patel VM, Schneider RT, Petsko GA, Ringe D, Small SA. Pharmacological chaperones stabilize retromer to limit APP processing. Nature Chemical Biology. 10: 443-9. PMID 24747528 DOI: 10.1038/Nchembio.1508 |
0.787 |
|
| 2014 |
Auclair JR, Salisbury JP, Johnson JL, Petsko GA, Ringe D, Bosco DA, Agar NY, Santagata S, Durham HD, Agar JN. Artifacts to avoid while taking advantage of top-down mass spectrometry based detection of protein S-thiolation. Proteomics. 14: 1152-7. PMID 24634066 DOI: 10.1002/Pmic.201300450 |
0.724 |
|
| 2014 |
Kreinbring CA, Remillard SP, Hubbard P, Brodkin HR, Leeper FJ, Hawksley D, Lai EY, Fulton C, Petsko GA, Ringe D. Structure of a eukaryotic thiaminase I. Proceedings of the National Academy of Sciences of the United States of America. 111: 137-42. PMID 24351929 DOI: 10.1073/Pnas.1315882110 |
0.813 |
|
| 2013 |
Edayathumangalam R, Wu R, Garcia R, Wang Y, Wang W, Kreinbring CA, Bach A, Liao J, Stone TA, Terwilliger TC, Hoang QQ, Belitsky BR, Petsko GA, Ringe D, Liu D. Crystal structure of Bacillus subtilis GabR, an autorepressor and transcriptional activator of gabT. Proceedings of the National Academy of Sciences of the United States of America. 110: 17820-5. PMID 24127574 DOI: 10.1073/Pnas.1315887110 |
0.79 |
|
| 2013 |
Shim JH, Greenblatt MB, Zou W, Huang Z, Wein MN, Brady N, Hu D, Charron J, Brodkin HR, Petsko GA, Zaller D, Zhai B, Gygi S, Glimcher LH, Jones DC. Schnurri-3 regulates ERK downstream of WNT signaling in osteoblasts. The Journal of Clinical Investigation. 123: 4010-22. PMID 23945236 DOI: 10.1172/Jci69443 |
0.764 |
|
| 2013 |
Auclair JR, Johnson JL, Liu Q, Salisbury JP, Rotunno MS, Petsko GA, Ringe D, Brown RH, Bosco DA, Agar JN. Post-translational modification by cysteine protects Cu/Zn-superoxide dismutase from oxidative damage. Biochemistry. 52: 6137-44. PMID 23927036 DOI: 10.1021/Bi4006122 |
0.711 |
|
| 2013 |
Auclair JR, Brodkin HR, D'Aquino JA, Petsko GA, Ringe D, Agar JN. Structural consequences of cysteinylation of Cu/Zn-superoxide dismutase Biochemistry. 52: 6145-6150. PMID 23919400 DOI: 10.1021/Bi400613H |
0.791 |
|
| 2013 |
Sigala PA, Fafarman AT, Schwans JP, Fried SD, Fenn TD, Caaveiro JM, Pybus B, Ringe D, Petsko GA, Boxer SG, Herschlag D. Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site. Proceedings of the National Academy of Sciences of the United States of America. 110: E2552-61. PMID 23798390 DOI: 10.1073/Pnas.1302191110 |
0.544 |
|
| 2013 |
Liu CF, Liu D, Momb J, Thomas PW, Lajoie A, Petsko GA, Fast W, Ringe D. A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-γ-lactonase from Bacillus thuringiensis Biochemistry. 52: 1603-1610. PMID 23387521 DOI: 10.1021/Bi400050J |
0.719 |
|
| 2013 |
Steele JW, Ju S, Lachenmayer ML, Liken J, Stock A, Kim SH, Delgado LM, Alfaro IE, Bernales S, Verdile G, Bharadwaj P, Gupta V, Barr R, Friss A, Dolios G, ... ... Petsko GA, et al. Latrepirdine stimulates autophagy and reduces accumulation of α-synuclein in cells and in mouse brain. Molecular Psychiatry. 18: 882-8. PMID 22869031 DOI: 10.1038/Mp.2012.115 |
0.774 |
|
| 2013 |
Steele JW, Lachenmayer ML, Ju S, Stock A, Liken J, Kim SH, Delgado LM, Alfaro IE, Bernales S, Verdile G, Bharadwaj P, Gupta V, Barr R, Friss A, Dolios G, ... ... Petsko GA, et al. Latrepirdine improves cognition and arrests progression of neuropathology in an Alzheimer's mouse model. Molecular Psychiatry. 18: 889-97. PMID 22850627 DOI: 10.1038/Mp.2012.106 |
0.771 |
|
| 2012 |
Ringe D, Petsko GA. Behind the movement Cell. 150: 1093-1095. PMID 22980970 DOI: 10.1016/J.Cell.2012.08.031 |
0.474 |
|
| 2012 |
Bharadwaj PR, Verdile G, Barr RK, Gupta V, Steele JW, Lachenmayer ML, Yue Z, Ehrlich ME, Petsko G, Ju S, Ringe D, Sankovich SE, Caine JM, Macreadie IG, Gandy S, et al. Latrepirdine (dimebon) enhances autophagy and reduces intracellular GFP-Aβ42 levels in yeast. Journal of Alzheimer's Disease : Jad. 32: 949-67. PMID 22903131 DOI: 10.3233/Jad-2012-120178 |
0.775 |
|
| 2012 |
Auclair JR, Somasundaran M, Green KM, Evans JE, Schiffer CA, Ringe D, Petsko GA, Agar JN. Mass spectrometry tools for analysis of intermolecular interactions. Methods in Molecular Biology (Clifton, N.J.). 896: 387-98. PMID 22821539 DOI: 10.1007/978-1-4614-3704-8_26 |
0.528 |
|
| 2012 |
Davies CW, Chaney J, Korbel G, Ringe D, Petsko GA, Ploegh H, Das C. The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE(OMe)-FMK). Bioorganic & Medicinal Chemistry Letters. 22: 3900-4. PMID 22617491 DOI: 10.1016/J.Bmcl.2012.04.124 |
0.82 |
|
| 2011 |
Wang W, Perovic I, Chittuluru J, Kaganovich A, Nguyen LT, Liao J, Auclair JR, Johnson D, Landeru A, Simorellis AK, Ju S, Cookson MR, Asturias FJ, Agar JN, Webb BN, ... ... Petsko GA, et al. A soluble α-synuclein construct forms a dynamic tetramer. Proceedings of the National Academy of Sciences of the United States of America. 108: 17797-802. PMID 22006323 DOI: 10.1073/Pnas.1113260108 |
0.79 |
|
| 2011 |
Bosco DA, LaVoie MJ, Petsko GA, Ringe D. Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis. Cold Spring Harbor Perspectives in Biology. 3: a007500. PMID 21844169 DOI: 10.1101/Cshperspect.A007500 |
0.714 |
|
| 2011 |
Lazar LM, Fisher SZ, Moulin AG, Kovalevsky A, Novak WR, Langan P, Petsko GA, Ringe D. Time-of-flight neutron diffraction study of bovine γ-chymotrypsin at the Protein Crystallography Station. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 67: 587-90. PMID 21543868 DOI: 10.1107/S1744309111009341 |
0.793 |
|
| 2011 |
Ju S, Tardiff DF, Han H, Divya K, Zhong Q, Maquat LE, Bosco DA, Hayward LJ, Brown RH, Lindquist S, Ringe D, Petsko GA. A yeast model of FUS/TLS-dependent cytotoxicity. Plos Biology. 9: e1001052. PMID 21541368 DOI: 10.1371/Journal.Pbio.1001052 |
0.785 |
|
| 2011 |
Brodkin HR, Novak WRP, Milne AC, D'Aquino JA, Karabacak NM, Goldberg IG, Agar JN, Payne MS, Petsko GA, Ondrechen MJ, Ringe D. Evidence of the participation of remote residues in the catalytic activity of co-type nitrile hydratase from Pseudomonas putida Biochemistry. 50: 4923-4935. PMID 21473592 DOI: 10.1021/Bi101761E |
0.796 |
|
| 2010 |
Auclair JR, Boggio KJ, Petsko GA, Ringe D, Agar JN. Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis Proceedings of the National Academy of Sciences of the United States of America. 107: 21394-21399. PMID 21098299 DOI: 10.1073/Pnas.1015463107 |
0.783 |
|
| 2010 |
Lewandowski NM, Ju S, Verbitsky M, Ross B, Geddie ML, Rockenstein E, Adame A, Muhammad A, Vonsattel JP, Ringe D, Cote L, Lindquist S, Masliah E, Petsko GA, Marder K, et al. Polyamine pathway contributes to the pathogenesis of Parkinson disease. Proceedings of the National Academy of Sciences of the United States of America. 107: 16970-5. PMID 20837543 DOI: 10.1073/Pnas.1011751107 |
0.775 |
|
| 2010 |
Gleick PH, Adams RM, Amasino RM, Anders E, Anderson DJ, Anderson WW, Anselin LE, Arroyo MK, Asfaw B, Ayala FJ, Bax A, Bebbington AJ, Bell G, Bennett MV, Bennetzen JL, ... ... Petsko GA, et al. Climate change and the integrity of science. Science (New York, N.Y.). 328: 689-90. PMID 20448167 DOI: 10.1126/Science.328.5979.689 |
0.752 |
|
| 2010 |
Brandt GS, Kneen MM, Petsko GA, Ringe D, McLeish MJ. Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition Journal of the American Chemical Society. 132: 438-439. PMID 20030408 DOI: 10.1021/Ja907064W |
0.787 |
|
| 2009 |
Ringe D, Petsko GA. What are pharmacological chaperones and why are they interesting? Journal of Biology. 8. PMID 19833004 DOI: 10.1186/Jbiol186 |
0.564 |
|
| 2009 |
Petsko GA. Crystallographic cryoenzymology and the legacy of Tony Fink Current Protein and Peptide Science. 10: 416-423. PMID 19538155 DOI: 10.2174/138920309789351985 |
0.336 |
|
| 2009 |
Landon MR, Lieberman RL, Hoang QQ, Ju S, Caaveiro JM, Orwig SD, Kozakov D, Brenke R, Chuang GY, Beglov D, Vajda S, Petsko GA, Ringe D. Detection of ligand binding hot spots on protein surfaces via fragment-based methods: application to DJ-1 and glucocerebrosidase. Journal of Computer-Aided Molecular Design. 23: 491-500. PMID 19521672 DOI: 10.1007/S10822-009-9283-2 |
0.789 |
|
| 2009 |
Sigala PA, Caaveiro JM, Ringe D, Petsko GA, Herschlag D. Hydrogen bond coupling in the ketosteroid isomerase active site. Biochemistry. 48: 6932-9. PMID 19469568 DOI: 10.1021/Bi900713J |
0.535 |
|
| 2009 |
Lieberman RL, D'aquino JA, Ringe D, Petsko GA. Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability. Biochemistry. 48: 4816-27. PMID 19374450 DOI: 10.1021/Bi9002265 |
0.697 |
|
| 2009 |
Brandt GS, Kneen MM, Chakraborty S, Baykal AT, Nemeria N, Yep A, Ruby DI, Petsko GA, Kenyon GL, McLeish MJ, Jordan F, Ringe D. Snapshot of a reaction intermediate: analysis of benzoylformate decarboxylase in complex with a benzoylphosphonate inhibitor. Biochemistry. 48: 3247-57. PMID 19320438 DOI: 10.1021/Bi801950K |
0.798 |
|
| 2009 |
Novak WR, Moulin AG, Blakeley MP, Schlichting I, Petsko GA, Ringe D. A preliminary neutron diffraction study of gamma-chymotrypsin. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 65: 317-20. PMID 19255494 DOI: 10.1107/S1744309109006630 |
0.789 |
|
| 2009 |
Chakraborty S, Nemeria NS, Balakrishnan A, Brandt GS, Kneen MM, Yep A, McLeish MJ, Kenyon GL, Petsko GA, Ringe D, Jordan F. Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase. Biochemistry. 48: 981-94. PMID 19140682 DOI: 10.1021/Bi801810H |
0.796 |
|
| 2008 |
Sigala PA, Kraut DA, Caaveiro JM, Pybus B, Ruben EA, Ringe D, Petsko GA, Herschlag D. Testing geometrical discrimination within an enzyme active site: constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole. Journal of the American Chemical Society. 130: 13696-708. PMID 18808119 DOI: 10.1021/Ja803928M |
0.603 |
|
| 2008 |
Momb J, Wang C, Liu D, Thomas PW, Petsko GA, Guo H, Ringe D, Fast W. Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate modeling and active site mutations. Biochemistry. 47: 7715-25. PMID 18627130 DOI: 10.1021/Bi8003704 |
0.713 |
|
| 2008 |
Liu D, Momb J, Thomas PW, Moulin A, Petsko GA, Fast W, Ringe D. Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures. Biochemistry. 47: 7706-14. PMID 18627129 DOI: 10.1021/Bi800368Y |
0.803 |
|
| 2008 |
Ataie NJ, Hoang QQ, Zahniser MP, Tu Y, Milne A, Petsko GA, Ringe D. Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus. Biochemistry. 47: 7673-83. PMID 18576673 DOI: 10.1021/Bi702188E |
0.802 |
|
| 2008 |
Brandt GS, Nemeria N, Chakraborty S, McLeish MJ, Yep A, Kenyon GL, Petsko GA, Jordan F, Ringe D. Probing the active center of benzaldehyde lyase with substitutions and the pseudosubstrate analogue benzoylphosphonic acid methyl ester. Biochemistry. 47: 7734-43. PMID 18570438 DOI: 10.1021/Bi8004413 |
0.81 |
|
| 2008 |
Ringe D, Petsko GA. Biochemistry. How enzymes work. Science (New York, N.Y.). 320: 1428-9. PMID 18556536 DOI: 10.1126/Science.1159747 |
0.529 |
|
| 2008 |
Ringe D, Petsko GA. Jeremy R Knowles 1935–2008 Nature Chemical Biology. 4: 325-325. DOI: 10.1038/Nchembio0608-325 |
0.46 |
|
| 2008 |
Alber T, Gilbert WA, Ringe Ponzi DR, Petsko GA. The Role of Mobility in the Substrate Binding and Catalytic Machinery of Enzymes Ciba Foundation Symposium 93 - Mobility and Function in Proteins and Nucleic Acids. 4-24. DOI: 10.1002/9780470720752.ch2 |
0.562 |
|
| 2007 |
Henzler-Wildman KA, Thai V, Lei M, Ott M, Wolf-Watz M, Fenn T, Pozharski E, Wilson MA, Petsko GA, Karplus M, Hübner CG, Kern D. Intrinsic motions along an enzymatic reaction trajectory. Nature. 450: 838-44. PMID 18026086 DOI: 10.1038/Nature06410 |
0.641 |
|
| 2007 |
Liu D, Thomas PW, Momb J, Hoang QQ, Petsko GA, Ringe D, Fast W. Structure and specificity of a quorum-quenching lactonase (AiiB) from Agrobacterium tumefaciens. Biochemistry. 46: 11789-99. PMID 17900178 DOI: 10.1021/Bi7012849 |
0.814 |
|
| 2007 |
Liu D, Pozharski E, Lepore BW, Fu M, Silverman RB, Petsko GA, Ringe D. Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms". Biochemistry. 46: 10517-27. PMID 17713924 DOI: 10.1021/Bi700663N |
0.7 |
|
| 2007 |
Munih P, Moulin A, Stamper CC, Bennett B, Ringe D, Petsko GA, Holz RC. X-ray crystallographic characterization of the Co(II)-substituted Tris-bound form of the aminopeptidase from Aeromonas proteolytica. Journal of Inorganic Biochemistry. 101: 1099-107. PMID 17574677 DOI: 10.1016/J.Jinorgbio.2007.03.010 |
0.791 |
|
| 2007 |
Petsko GA. And the second shall be first Genome Biology. 8. PMID 17328789 DOI: 10.1186/Gb-2007-8-2-103 |
0.305 |
|
| 2007 |
Lieberman RL, Wustman BA, Huertas P, Powe AC, Pine CW, Khanna R, Schlossmacher MG, Ringe D, Petsko GA. Structure of acid beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease. Nature Chemical Biology. 3: 101-7. PMID 17187079 DOI: 10.1038/Nchembio850 |
0.727 |
|
| 2006 |
Petsko GA. An introduction to modeling structure from sequence. Current Protocols in Bioinformatics / Editoral Board, Andreas D. Baxevanis ... [Et Al.]. Unit 5.1. PMID 18428765 DOI: 10.1002/0471250953.Bi0501S15 |
0.317 |
|
| 2006 |
Ding X, 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. 34: 410-23. PMID 17083959 DOI: 10.1016/J.Bioorg.2006.10.002 |
0.602 |
|
| 2006 |
Kraut DA, Sigala PA, Pybus B, Liu CW, Ringe D, Petsko GA, Herschlag D. Testing electrostatic complementarity in enzyme catalysis: hydrogen bonding in the ketosteroid isomerase oxyanion hole. Plos Biology. 4: e99. PMID 16602823 DOI: 10.1371/Journal.Pbio.0040099 |
0.557 |
|
| 2006 |
Desmarais W, Bienvenue DL, Bzymek KP, Petsko GA, Ringe D, Holz RC. The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 398-408. PMID 16596389 DOI: 10.1007/S00775-006-0093-X |
0.566 |
|
| 2006 |
Das C, Hoang QQ, Kreinbring CA, Luchansky SJ, Meray RK, Ray SS, Lansbury PT, Ringe D, Petsko GA. 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. 103: 4675-80. PMID 16537382 DOI: 10.1073/Pnas.0510403103 |
0.784 |
|
| 2006 |
Mattos C, Bellamacina CR, Peisach E, Pereira A, Vitkup D, Petsko GA, Ringe D. Multiple solvent crystal structures: probing binding sites, plasticity and hydration. Journal of Molecular Biology. 357: 1471-82. PMID 16488429 DOI: 10.1016/J.Jmb.2006.01.039 |
0.801 |
|
| 2005 |
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. 353: 678-91. PMID 16181642 DOI: 10.1016/J.Jmb.2005.08.033 |
0.607 |
|
| 2005 |
Bzymek KP, Moulin A, Swierczek SI, Ringe D, Petsko GA, Bennett B, Holz RC. Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase from Aeromonas proteolytica. Biochemistry. 44: 12030-40. PMID 16142900 DOI: 10.1021/Bi0505823 |
0.812 |
|
| 2005 |
Liu D, Lepore BW, Petsko GA, Thomas PW, Stone EM, Fast W, Ringe D. Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis. Proceedings of the National Academy of Sciences of the United States of America. 102: 11882-7. PMID 16087890 DOI: 10.1073/Pnas.0505255102 |
0.7 |
|
| 2005 |
Pozharski E, Moulin A, Hewagama A, Shanafelt AB, Petsko GA, Ringe D. Diversity in hapten recognition: structural study of an anti-cocaine antibody M82G2. Journal of Molecular Biology. 349: 570-82. PMID 15885702 DOI: 10.1016/J.Jmb.2005.03.080 |
0.776 |
|
| 2004 |
Yang J, Wang Y, Woolridge EM, Arora V, Petsko GA, Kozarich JW, Ringe D. 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. 43: 10424-34. PMID 15301541 DOI: 10.1021/Bi036205C |
0.61 |
|
| 2004 |
Stamper CC, Bienvenue DL, Bennett B, Ringe D, Petsko GA, Holz RC. Spectroscopic and X-ray crystallographic characterization of bestatin bound to the aminopeptidase from Aeromonas (Vibrio) proteolytica. Biochemistry. 43: 9620-8. PMID 15274616 DOI: 10.1021/Bi049126P |
0.59 |
|
| 2004 |
Gray JV, Petsko GA, Johnston GC, Ringe D, Singer RA, Werner-Washburne M. "Sleeping beauty": quiescence in Saccharomyces cerevisiae. Microbiology and Molecular Biology Reviews : Mmbr. 68: 187-206. PMID 15187181 DOI: 10.1128/Mmbr.68.2.187-206.2004 |
0.499 |
|
| 2004 |
Canet-Avilés RM, Wilson MA, Miller DW, Ahmad R, McLendon C, Bandyopadhyay S, Baptista MJ, Ringe D, Petsko GA, Cookson MR. The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization. Proceedings of the National Academy of Sciences of the United States of America. 101: 9103-8. PMID 15181200 DOI: 10.1073/Pnas.0402959101 |
0.512 |
|
| 2004 |
Fenn TD, Ringe D, Petsko GA. Xylose isomerase in substrate and inhibitor michaelis states: atomic resolution studies of a metal-mediated hydride shift. Biochemistry. 43: 6464-74. PMID 15157080 DOI: 10.2210/Pdb1S5N/Pdb |
0.585 |
|
| 2004 |
Vogan EM, Bellamacina C, He X, Liu HW, Ringe D, Petsko GA. Crystal structure at 1.8 A resolution of CDP-D-glucose 4,6-dehydratase from Yersinia pseudotuberculosis. Biochemistry. 43: 3057-67. PMID 15023057 DOI: 10.1021/Bi035547F |
0.57 |
|
| 2004 |
Pozharski E, Wilson MA, Hewagama A, Shanafelt AB, Petsko G, Ringe D. Anchoring a cationic ligand: the structure of the Fab fragment of the anti-morphine antibody 9B1 and its complex with morphine. Journal of Molecular Biology. 337: 691-7. PMID 15019787 DOI: 10.1016/J.Jmb.2003.12.084 |
0.547 |
|
| 2004 |
Holyoak T, Kettner CA, Petsko GA, Fuller RS, Ringe D. Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases. Biochemistry. 43: 2412-21. PMID 14992578 DOI: 10.1021/Bi035849H |
0.814 |
|
| 2004 |
Wilson MA, St Amour CV, Collins JL, Ringe D, Petsko GA. The 1.8-A resolution crystal structure of YDR533Cp from Saccharomyces cerevisiae: a member of the DJ-1/ThiJ/PfpI superfamily. Proceedings of the National Academy of Sciences of the United States of America. 101: 1531-6. PMID 14745011 DOI: 10.1073/Pnas.0308089100 |
0.588 |
|
| 2003 |
Holyoak T, Fenn TD, Wilson MA, Moulin AG, Ringe D, Petsko GA. Malonate: a versatile cryoprotectant and stabilizing solution for salt-grown macromolecular crystals. Acta Crystallographica. Section D, Biological Crystallography. 59: 2356-8. PMID 14646118 DOI: 10.1107/S0907444903021784 |
0.782 |
|
| 2003 |
Ringe D, Petsko GA. The 'glass transition' in protein dynamics: what it is, why it occurs, and how to exploit it. Biophysical Chemistry. 105: 667-80. PMID 14499926 DOI: 10.1016/S0301-4622(03)00096-6 |
0.534 |
|
| 2003 |
Wilson MA, Collins JL, Hod Y, Ringe D, Petsko GA. The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease. Proceedings of the National Academy of Sciences of the United States of America. 100: 9256-61. PMID 12855764 DOI: 10.1073/Pnas.1133288100 |
0.605 |
|
| 2003 |
Holyoak T, Wilson MA, Fenn TD, Kettner CA, Petsko GA, Fuller RS, Ringe D. 2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor. Biochemistry. 42: 6709-18. PMID 12779325 DOI: 10.1021/Bi034434T |
0.813 |
|
| 2003 |
Beebe JA, Arabshahi A, Clifton JG, Ringe D, Petsko GA, Frey PA. Galactose mutarotase: pH dependence of enzymatic mutarotation. Biochemistry. 42: 4414-20. PMID 12693937 DOI: 10.1021/Bi020639A |
0.515 |
|
| 2003 |
Gan L, Seyedsayamdost MR, Shuto S, Matsuda A, Petsko GA, Hedstrom L. The immunosuppressive agent mizoribine monophosphate forms a transition state analogue complex with inosine monophosphate dehydrogenase. Biochemistry. 42: 857-63. PMID 12549902 DOI: 10.1021/Bi0271401 |
0.379 |
|
| 2003 |
Fenn TD, Ringe D, Petsko GA. POVScript+: A program for model and data visualization using persistence of vision ray-tracing Journal of Applied Crystallography. 36: 944-947. DOI: 10.1107/S0021889803006721 |
0.509 |
|
| 2002 |
Kenyon GL, DeMarini DM, Fuchs E, Galas DJ, Kirsch JF, Leyh TS, Moos WH, Petsko GA, Ringe D, Rubin GM, Sheahan LC. Defining the mandate of proteomics in the post-genomics era: workshop report. Molecular & Cellular Proteomics : McP. 1: 763-80. PMID 12438560 |
0.449 |
|
| 2002 |
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. 41: 13309-17. PMID 12403633 DOI: 10.1021/Bi0203785 |
0.407 |
|
| 2002 |
Desmarais WT, Bienvenue DL, Bzymek KP, Holz RC, Petsko GA, Ringe D. The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition. Structure (London, England : 1993). 10: 1063-72. PMID 12176384 DOI: 10.1016/S0969-2126(02)00810-9 |
0.593 |
|
| 2002 |
Petsko GA. The father of us all. Genome Biology. 3: COMMENT1004. PMID 11897016 DOI: 10.1186/Gb-2002-3-3-Comment1004 |
0.359 |
|
| 2002 |
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. 41: 2621-9. PMID 11851409 DOI: 10.1021/Bi015844P |
0.771 |
|
| 2002 |
Vitkup D, Ringe D, Karplus M, Petsko GA. Why protein R-factors are so large: a self-consistent analysis. Proteins. 46: 345-54. PMID 11835510 DOI: 10.1002/Prot.10035 |
0.745 |
|
| 2002 |
Vogan EM, Bellamacina CR, He X, Foxman BM, Ringe D, Liu HW, Petsko GA. Purification, crystallization and molecular symmetry of CDP-D-glucose 4,6-dehydratase from Yersinia pseudotuberculosis. Acta Crystallographica. Section D, Biological Crystallography. 58: 370-3. PMID 11807280 DOI: 10.1107/S0907444901021473 |
0.547 |
|
| 2001 |
Hadfield A, Shammas C, Kryger G, Ringe D, Petsko GA, Ouyang J, Viola RE. Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase. Biochemistry. 40: 14475-83. PMID 11724560 DOI: 10.1021/Bi015713O |
0.612 |
|
| 2001 |
Stamper C, Bennett B, Edwards T, Holz RC, Ringe D, Petsko G. Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis. Biochemistry. 40: 7035-46. PMID 11401547 DOI: 10.1021/Bi0100891 |
0.577 |
|
| 2001 |
Petsko GA. Structural basis of thermostability in hyperthermophilic proteins, or "there's more than one way to skin a cat". Methods in Enzymology. 334: 469-78. PMID 11398484 DOI: 10.1016/S0076-6879(01)34486-5 |
0.307 |
|
| 2000 |
Petsko GA. The grail problem. Genome Biology. 1: COMMENT002. PMID 11104515 DOI: 10.1186/Gb-2000-1-1-Comment002 |
0.362 |
|
| 2000 |
Heymont J, Berenfeld L, Collins J, Kaganovich A, Maynes B, Moulin A, Ratskovskaya I, Poon PP, Johnston GC, Kamenetsky M, DeSilva J, Sun H, Petsko GA, Engebrecht J. 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. 97: 12672-7. PMID 11070083 DOI: 10.1073/Pnas.97.23.12672 |
0.776 |
|
| 2000 |
McMillan FM, Cahoon M, White A, Hedstrom L, Petsko GA, Ringe D. 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. 39: 4533-42. PMID 10758003 DOI: 10.1021/Bi992645L |
0.611 |
|
| 2000 |
Jeffery 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. 13: 105-12. PMID 10708649 DOI: 10.1093/Protein/13.2.105 |
0.756 |
|
| 2000 |
Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sligar SG. The catalytic pathway of cytochrome p450cam at atomic resolution. Science (New York, N.Y.). 287: 1615-22. PMID 10698731 DOI: 10.1126/Science.287.5458.1615 |
0.759 |
|
| 2000 |
Petsko GA. Enzyme evolution. Design by necessity. Nature. 403: 606-7. PMID 10688181 DOI: 10.1038/35001176 |
0.33 |
|
| 2000 |
Petsko GA, Ringe D. Observation of unstable species in enzyme-catalyzed transformations using protein crystallography. Current Opinion in Chemical Biology. 4: 89-94. PMID 10679381 DOI: 10.1016/S1367-5931(99)00057-5 |
0.577 |
|
| 2000 |
Jeffery CJ, Bahnson BJ, Chien W, Ringe D, Petsko GA. Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator. Biochemistry. 39: 955-64. PMID 10653639 DOI: 10.1021/Bi991604M |
0.826 |
|
| 2000 |
Vitkup D, Ringe D, Petsko GA, Karplus M. Solvent mobility and the protein 'glass' transition. Nature Structural Biology. 7: 34-8. PMID 10625424 DOI: 10.1038/71231 |
0.752 |
|
| 2000 |
Jeffery CJ, Gloss LM, Petsko GA, Ringe D. The Role of Residues Outside the Active Site in Catalysis: Structural Basis for Function of C191 Mutants of E. Coli Aspartate Aminotransferase Protein Engineering. 13: 105. DOI: 10.2210/Pdb1Qir/Pdb |
0.731 |
|
| 1999 |
De Paola CC, Bennett B, Holz RC, Ringe D, Petsko GA. 1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development. Biochemistry. 38: 9048-53. PMID 10413478 DOI: 10.1021/Bi9900572 |
0.603 |
|
| 1999 |
Johnson LN, Petsko GA. David Phillips and the origin of structural enzymology Trends in Biochemical Sciences. 24: 287-289. PMID 10390620 DOI: 10.1016/S0968-0004(99)01423-1 |
0.518 |
|
| 1999 |
Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R. Structure of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis. Journal of Molecular Biology. 289: 991-1002. PMID 10369777 DOI: 10.1006/Jmbi.1999.2828 |
0.598 |
|
| 1999 |
Ringe D, Petsko GA. Quantum enzymology. Tunnel vision. Nature. 399: 417-8. PMID 10365952 DOI: 10.1038/20819 |
0.527 |
|
| 1999 |
Johnson LN, Petsko GA. David Phillips (1924-99) Nature. 399: 26. PMID 10331385 DOI: 10.1038/19878 |
0.527 |
|
| 1999 |
Zhang Z, Komives EA, Sugio S, Blacklow SC, Narayana N, Xuong NH, Stock AM, Petsko GA, Ringe D. The role of water in the catalytic efficiency of triosephosphate isomerase. Biochemistry. 38: 4389-97. PMID 10194358 DOI: 10.1021/Bi9826759 |
0.718 |
|
| 1999 |
Morollo AA, Petsko GA, Ringe D. Structure of a Michaelis complex analogue: propionate binds in the substrate carboxylate site of alanine racemase. Biochemistry. 38: 3293-301. PMID 10079072 DOI: 10.1021/Bi9822729 |
0.618 |
|
| 1999 |
Wieczorek SJ, Kalivoda KA, Clifton JG, Ringe D, Petsko GA, Gerlt JA. Evolution of enzymatic activities in the enolase superfamily: Identification of a 'new' general acid catalyst in the active site of D- galactonate dehydratase from Escherichia coli Journal of the American Chemical Society. 121: 4540-4541. DOI: 10.1021/Ja990500W |
0.518 |
|
| 1998 |
Jeffery CJ, Barry T, Doonan S, Petsko GA, Ringe D. Crystallization and preliminary X-ray diffraction analysis of aspartate aminotransferase from Saccharomyces cerevisiae. Acta Crystallographica. Section D, Biological Crystallography. 54: 659-61. PMID 9761867 DOI: 10.1107/S0907444997016235 |
0.723 |
|
| 1998 |
Sugio S, Kashima A, Kishimoto K, Peisach D, Petsko GA, Ringe D, Yoshimura T, Esaki N. Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination. Protein Engineering. 11: 613-9. PMID 9749913 DOI: 10.1093/Protein/11.8.613 |
0.612 |
|
| 1998 |
Hasson MS, Schlichting I, Moulai J, Taylor K, Barrett W, Kenyon GL, Babbitt PC, Gerlt JA, Petsko GA, Ringe D. 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. 95: 10396-401. PMID 9724714 DOI: 10.1073/Pnas.95.18.10396 |
0.788 |
|
| 1998 |
Hasson MS, Muscate A, McLeish MJ, Polovnikova LS, Gerlt JA, Kenyon GL, Petsko GA, Ringe D. The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes. Biochemistry. 37: 9918-30. PMID 9665697 DOI: 10.1021/Bi973047E |
0.626 |
|
| 1998 |
Jeffery CJ, Barry T, Doonan S, Petsko GA, Ringe D. Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase. Protein Science : a Publication of the Protein Society. 7: 1380-7. PMID 9655342 DOI: 10.1002/Pro.5560070614 |
0.77 |
|
| 1998 |
Závodszky P, Kardos J, Svingor Á, 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. 95: 7406-7411. PMID 9636162 DOI: 10.1073/Pnas.95.13.7406 |
0.334 |
|
| 1998 |
Yamakura F, Rardin RL, Petsko GA, Ringe D, Hiraoka BY, Nakayama K, Fujimura T, Taka H, Murayama K. Inactivation and destruction of conserved Trp159 of Fe-superoxide dismutase from Porphyromonas gingivalis by hydrogen peroxide. European Journal of Biochemistry / Febs. 253: 49-56. PMID 9578460 DOI: 10.1046/J.1432-1327.1998.2530049.X |
0.724 |
|
| 1998 |
Van Ophem PW, Erickson SD, Martinez Del Pozo A, Haller I, Chait BT, Yoshimura T, Soda K, Ringe D, Petsko G, Manning JM. Substrate inhibition of D-amino acid transaminase and protection by salts and by reduced nicotinamide adenine dinucleotide: Isolation and initial characterization of a pyridoxo intermediate related to inactivation Biochemistry. 37: 2879-2888. PMID 9485439 DOI: 10.1021/bi972842p |
0.467 |
|
| 1997 |
Hasson MS, Schlichting I, McGowen MM, Woolridge EM, Kozarich JW, Petsko GA, Ringe D. Characterization of two crystal forms of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida. Acta Crystallographica. Section D, Biological Crystallography. 53: 352-3. PMID 15299946 DOI: 10.1107/S0907444996015648 |
0.644 |
|
| 1997 |
Harrison DH, Bohren KM, Petsko GA, Ringe D, Gabbay KH. The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant. Biochemistry. 36: 16134-40. PMID 9405046 DOI: 10.1021/Bi9717136 |
0.691 |
|
| 1997 |
Wallon G, Lovett ST, Magyar C, Svingor A, Szilagyi A, Zàvodszky P, Ringe D, Petsko GA. Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. I5 suggest reasons for thermal instability. Protein Engineering. 10: 665-72. PMID 9278279 DOI: 10.1093/Protein/10.6.665 |
0.574 |
|
| 1997 |
Brenner C, Garrison P, Gilmour J, Peisach D, Ringe D, Petsko GA, Lowenstein JM. Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins. Nature Structural Biology. 4: 231-8. PMID 9164465 DOI: 10.1038/Nsb0397-231 |
0.683 |
|
| 1997 |
Vitkup D, Petsko GA, Karplus M. A comparison between molecular dynamics and X-ray results for dissociated CO in myoglobin. Nature Structural Biology. 4: 202-8. PMID 9164461 DOI: 10.1038/Nsb0397-202 |
0.7 |
|
| 1997 |
Wallon G, Kryger G, Lovett ST, Oshima T, Ringe D, Petsko GA. Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus. Journal of Molecular Biology. 266: 1016-31. PMID 9086278 DOI: 10.1006/Jmbi.1996.0797 |
0.613 |
|
| 1997 |
Shaw JP, Petsko GA, Ringe D. Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution. Biochemistry. 36: 1329-42. PMID 9063881 DOI: 10.1021/Bi961856C |
0.552 |
|
| 1997 |
Wallon G, Yamamoto K, Kirino H, Yamagishi A, Lovett ST, Petsko GA, Oshima T. Purification, catalytic properties and thermostability of 3-isopropylmalate dehydrogenase from Escherichia coli. Biochimica Et Biophysica Acta. 1337: 105-12. PMID 9003442 DOI: 10.1016/S0167-4838(96)00157-4 |
0.322 |
|
| 1996 |
Jones WM, van Ophem PW, Pospischil MA, Ringe D, Petsko G, Soda K, Manning JM. The ubiquitous cofactor NADH protects against substrate-induced inhibition of a pyridoxal enzyme. Protein Science : a Publication of the Protein Society. 5: 2545-51. PMID 8976563 DOI: 10.1002/Pro.5560051217 |
0.559 |
|
| 1996 |
Komives EA, Lougheed JC, Zhang Z, Sugio S, Narayana N, Xuong NH, Petsko GA, Ringe D. The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase. Biochemistry. 35: 15474-84. PMID 8952501 DOI: 10.1021/Bi961556V |
0.567 |
|
| 1996 |
Petsko GA. Not just your average structures. Nature Structural Biology. 3: 565-6. PMID 8673594 DOI: 10.1038/Nsb0796-565 |
0.332 |
|
| 1996 |
Martinez Del Pozo A, Van Ophem PW, Ringe D, Petsko G, Soda K, Manning JM. Interaction of pyridoxal 5′-phosphate with tryptophan-139 at the subunit interface of dimeric D-amino acid transaminase Biochemistry. 35: 2112-2116. PMID 8652553 DOI: 10.1021/Bi9522211 |
0.581 |
|
| 1996 |
Schafer SL, Barrett WC, Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL. Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant. Biochemistry. 35: 5662-9. PMID 8639525 DOI: 10.1021/Bi960174M |
0.308 |
|
| 1996 |
Schlichting I, Berendzen J, Chu K, Stock AM, Davies M, Mueller EJ, Sligar S, Sweet RM, Ringe D, Petsko GA. Intermediates in the reaction pathway of cytochrome P450cam Acta Crystallographica Section a Foundations of Crystallography. 52: C49-C49. DOI: 10.1107/S0108767396097085 |
0.716 |
|
| 1996 |
Allen KN, Bellamacina CR, Ding X, Jeffery CJ, Mattos C, Petsko GA, Ringe D. An Experimental Approach to Mapping the Binding Surfaces of Crystalline Proteins† The Journal of Physical Chemistry. 100: 2605-2611. DOI: 10.1021/Jp952516O |
0.796 |
|
| 1995 |
Joseph-McCarthy D, Petsko GA, Karplus M. Use of a minimum perturbation approach to predict TIM mutant structures. Protein Engineering. 8: 1103-15. PMID 8819976 DOI: 10.1093/Protein/8.11.1103 |
0.507 |
|
| 1995 |
Warren GL, Petsko GA. Composition analysis of alpha-helices in thermophilic organisms. Protein Engineering. 8: 905-13. PMID 8746728 DOI: 10.1093/Protein/8.9.905 |
0.305 |
|
| 1995 |
Van Ophem PW, Pospischil MA, Ringe D, Peisach D, Petsko G, Soda K, Manning JM. Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding Protein Science. 4: 2578-2586. PMID 8580849 DOI: 10.1002/Pro.5560041215 |
0.576 |
|
| 1995 |
Bohren KM, Wermuth B, Harrison D, Ringe D, Petsko GA, Gabbay KH. Expression, crystallization and preliminary crystallographic analysis of human carbonyl reductase. Journal of Molecular Biology. 244: 659-64. PMID 7990149 DOI: 10.1006/Jmbi.1994.1762 |
0.71 |
|
| 1995 |
Mitra B, Kallarakal AT, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL. Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317. Biochemistry. 34: 2777-87. PMID 7893689 DOI: 10.1021/Bi00009A006 |
0.356 |
|
| 1995 |
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. 34: 3742-3749. PMID 7893671 DOI: 10.1021/Bi00011A032 |
0.773 |
|
| 1995 |
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. 34: 3193-3203. PMID 7880814 DOI: 10.1021/Bi00010A008 |
0.727 |
|
| 1995 |
Babbitt PC, Mrachko GT, Hasson MS, Huisman GW, Kolter R, Ringe D, Petsko GA, Kenyon GL, Gerlt JA. A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids. Science (New York, N.Y.). 267: 1159-61. PMID 7855594 DOI: 10.1126/Science.7855594 |
0.712 |
|
| 1995 |
Hasson MS, Muscate A, Henehan GT, Guidinger PF, Petsko GA, Ringe D, Kenyon GL. Purification and crystallization of benzoylformate decarboxylase. Protein Science : a Publication of the Protein Society. 4: 955-9. PMID 7663351 DOI: 10.1002/Pro.5560040515 |
0.582 |
|
| 1995 |
Sugio S, Petsko GA, Manning JM, Soda K, Ringe D. Crystal structure of a D-amino acid aminotransferase: How the protein controls stereoselectivity Biochemistry. 34: 9661-9669. PMID 7626635 DOI: 10.1021/Bi00030A002 |
0.574 |
|
| 1995 |
Peisach E, Casebier D, Gallion SL, Furth P, Petsko GA, Hogan JC, Ringe D. Interaction of a peptidomimetic aminimide inhibitor with elastase. Science (New York, N.Y.). 269: 66-9. PMID 7604279 DOI: 10.1126/Science.7604279 |
0.55 |
|
| 1995 |
Kryger G, Wallon G, Lovett ST, Ringe D, Petsko GA. Revision of the amino-acid sequence of 3-isopropylmalate dehydrogenase from Salmonella typhimurium by means of X-ray crystallography. Gene. 164: 85-7. PMID 7590327 DOI: 10.1016/0378-1119(95)00494-Q |
0.526 |
|
| 1995 |
Komives EA, Lougheed JC, Liu K, Sugio S, Zhang Z, Petsko GA, Ringe D. 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. 34: 13612-21. PMID 7577950 DOI: 10.1021/Bi00041A041 |
0.584 |
|
| 1995 |
Schiering N, Tao X, Zeng H, Murphy JR, Petsko GA, Ringe D. Structures of the apo- 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. 92: 9843-50. PMID 7568230 DOI: 10.1073/Pnas.92.21.9843 |
0.568 |
|
| 1995 |
Kenyon GL, Gerlt JA, Petsko GA, Kozarich JW. Mandelate Racemase: Structure-Function Studies of a Pseudosymmetric Enzyme Accounts of Chemical Research. 28: 178-186. DOI: 10.1021/Ar00052A003 |
0.351 |
|
| 1994 |
Allen KN, Lavie A, Farber GK, Glasfeld A, Petsko GA, Ringe D. Isotopic exchange plus substrate and inhibition kinetics of D-xylose isomerase do not support a proton-transfer mechanism Biochemistry. 33: 1481-1487. PMID 8312268 DOI: 10.1021/Bi00172A026 |
0.748 |
|
| 1994 |
Mattos C, Petsko GA, Karplus M. Analysis of two-residue turns in proteins Journal of Molecular Biology. 238: 733-747. PMID 8182746 DOI: 10.1006/Jmbi.1994.1332 |
0.666 |
|
| 1994 |
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. 33: 5469-5480. PMID 8180169 DOI: 10.2210/Pdb1Xyb/Pdb |
0.76 |
|
| 1994 |
Zhang Z, Sugio S, Komives EA, Liu KD, Knowles JR, Petsko GA, Ringe D. Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution. Biochemistry. 33: 2830-7. PMID 8130195 DOI: 10.1021/Bi00176A012 |
0.615 |
|
| 1994 |
Joseph-McCarthy 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. 33: 2815-23. PMID 8130194 DOI: 10.1021/Bi00176A010 |
0.658 |
|
| 1994 |
Bohren KM, Grimshaw CE, Lai CJ, Harrison DH, Ringe D, Petsko GA, Gabbay KH. 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. 33: 2021-32. PMID 8117659 DOI: 10.1021/Bi00174A007 |
0.712 |
|
| 1994 |
Harrison DH, Bohren KM, Ringe D, Petsko GA, Gabbay KH. An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate. Biochemistry. 33: 2011-20. PMID 8117658 DOI: 10.1021/Bi00174A006 |
0.714 |
|
| 1994 |
Ding X, Rasmussen BF, Petsko GA, Ringe D. Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastase. Biochemistry. 33: 9285-93. PMID 8049229 DOI: 10.2210/Pdb1Esb/Pdb |
0.597 |
|
| 1994 |
Schiering N, Tao X, Murphy JR, Petsko GA, Ringe D. Crystallization and preliminary X-ray studies of the diphtheria Tox repressor from Corynebacterium diphtheriae. Journal of Molecular Biology. 244: 654-6. PMID 7990147 DOI: 10.1006/Jmbi.1994.1760 |
0.564 |
|
| 1994 |
Joseph-McCarthy 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. 33: 2824-9. PMID 7907502 DOI: 10.1021/Bi00176A011 |
0.419 |
|
| 1994 |
Allen KN, Lavie A, Glasfeld A, Tanada TN, Gerrity DP, Carlson SC, Farber GK, Petsko GA, Ringe D. 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. 33: 1488-1494. PMID 7906142 DOI: 10.1021/Bi00172A027 |
0.767 |
|
| 1994 |
Mattos C, Rasmussen B, Ding X, Petsko GA, Ringe D. Analogous inhibitors of elastase do not always bind analogously Nature Structural Biology. 1: 55-58. PMID 7656008 DOI: 10.1038/Nsb0194-55 |
0.717 |
|
| 1993 |
Stock AM, Martinez-Hackert E, Rasmussen BF, West AH, Stock JB, Ringe D, Petsko GA. Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis. Biochemistry. 32: 13375-80. PMID 8257674 DOI: 10.1021/Bi00212A001 |
0.773 |
|
| 1993 |
Petsko GA, Kenyon GL, Gerlt JA, Ringe D, Kozarich JW. On the origin of enzymatic species. Trends in Biochemical Sciences. 18: 372-6. PMID 8256284 DOI: 10.1016/0968-0004(93)90091-Z |
0.568 |
|
| 1993 |
Mitra B, Gerlt JA, Babbitt PC, Koo CW, Kenyon GL, Joseph D, Petsko GA. A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida. Biochemistry. 32: 12959-67. PMID 8241149 DOI: 10.1021/Bi00211A003 |
0.581 |
|
| 1993 |
Jeffrey PD, Strong RK, Sieker LC, Chang CY, Campbell RL, Petsko GA, Haber E, Margolies MN, Sheriff S. 26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity. Proceedings of the National Academy of Sciences of the United States of America. 90: 10310-4. PMID 8234291 DOI: 10.1073/Pnas.90.21.10310 |
0.659 |
|
| 1993 |
Petsko G, Ringe D, Allen K, Lavie A, Gerhart-Mueller E, Clifton J, Hasson M, Fujita S, Sugio S, Xhang X, Davenport R, Lolis E, Neidhart D, Kenyon G, Gerlt J, et al. The structural enzymology of proton-transfer reactions Protein Engineering, Design and Selection. 6: 37. DOI: 10.1093/Protein/6.Supplement.37-A |
0.798 |
|
| 1992 |
Howell PL, Warren C, Amatayakul-Chantler S, Petsko GA, Hajdu J. Activity of crystalline turkey egg white lysozyme. Proteins. 12: 91-9. PMID 1553384 DOI: 10.1002/Prot.340120111 |
0.549 |
|
| 1992 |
Tilton RF, Dewan JC, Petsko GA. Effects of temperature on protein structure and dynamics: X-ray crystallographic studies of the protein ribonuclease-A at nine different temperatures from 98 to 320 K Biochemistry. 31: 2469-2481. PMID 1547232 DOI: 10.1021/Bi00124A006 |
0.306 |
|
| 1992 |
Howell PL, Almo SC, Parsons MR, Hajdu J, Petsko GA. Structure determination of turkey egg-white lysozyme using Laue diffraction data. Acta Crystallographica. Section B, Structural Science. 48: 200-7. PMID 1515108 DOI: 10.1107/S0108768191012466 |
0.672 |
|
| 1992 |
Rasmussen BF, Stock AM, Ringe D, Petsko GA. Crystalline ribonuclease A loses function below the dynamical transition at 220 K. Nature. 357: 423-4. PMID 1463484 DOI: 10.1038/357423A0 |
0.685 |
|
| 1992 |
Kryger G, Petsko GA, Ouyang J, Viola RE. Crystallization and preliminary crystallographic analysis of aspartate-beta-semialdehyde dehydrogenase from Escherichia coli. Journal of Molecular Biology. 228: 300-1. PMID 1360028 DOI: 10.1016/0022-2836(92)90508-H |
0.329 |
|
| 1992 |
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 A. 340: 323-334. DOI: 10.1098/Rsta.1992.0070 |
0.326 |
|
| 1992 |
Gerlt JA, Kenyon GL, Kozarich JW, Neidhart DJ, Petsko GA, Powers VM. Mandelate racemase and class-related enzymes Current Opinion in Structural Biology. 2: 736-742. DOI: 10.1016/0959-440X(92)90209-P |
0.336 |
|
| 1991 |
Petsko GA. Enzyme evolution. Déjà vu all over again. Nature. 352: 104-5. PMID 2067568 DOI: 10.1038/352104A0 |
0.304 |
|
| 1991 |
Stoddard BL, Koenigs P, Porter N, Petratos K, Petsko GA, Ringe D. 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. 88: 5503-5507. PMID 2062832 DOI: 10.1073/Pnas.88.13.5503 |
0.606 |
|
| 1991 |
Bash PA, Field MJ, Davenport RC, Petsko GA, Ringe D, Karplus M. Computer simulation and analysis of the reaction pathway of triosephosphate isomerase. Biochemistry. 30: 5826-32. PMID 2043624 DOI: 10.1021/Bi00238A003 |
0.616 |
|
| 1991 |
Davenport RC, Bash PA, Seaton BA, Karplus M, Petsko GA, Ringe D. Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway. Biochemistry. 30: 5821-6. PMID 2043623 DOI: 10.1021/Bi00238A002 |
0.779 |
|
| 1991 |
Strong RK, Petsko GA, Sharon J, Margolies MN. Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 2. Structural basis of hapten binding and idiotypy Biochemistry. 30: 3749-3757. PMID 2015230 DOI: 10.1021/Bi00229A023 |
0.559 |
|
| 1991 |
Strong RK, Campbell R, Rose DR, Petsko GA, Sharon J, Margolies MN. Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 1. X-ray crystallography, site-directed mutagenesis, and modeling of the complex with hapten Biochemistry. 30: 3739-3748. PMID 2015229 DOI: 10.1021/Bi00229A022 |
0.59 |
|
| 1991 |
Komives EA, Chang LC, Lolis E, Tilton RF, Petsko GA, Knowles JR. Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95. Biochemistry. 30: 3011-9. PMID 2007138 DOI: 10.1021/Bi00226A005 |
0.631 |
|
| 1991 |
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. 30: 1980-5. PMID 1993208 DOI: 10.1021/Bi00221A035 |
0.609 |
|
| 1991 |
Ringe D, Petsko GA. Viral proteases. Molecular metamorphosis. Nature. 354: 22-3. PMID 1944564 DOI: 10.1038/354022d0 |
0.421 |
|
| 1991 |
Neidhart DJ, Howell PL, Petsko GA, Powers VM, Li RS, Kenyon GL, Gerlt JA. 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. 30: 9264-73. PMID 1892834 DOI: 10.1021/Bi00102A019 |
0.525 |
|
| 1991 |
Stoddard BL, Strong RK, Farber GK, Arrott A, Petsko GA. Design of apparatus and experiments to determine the effect of microgravity on the crystallization of biological macromolecules using the MIR spacestation Journal of Crystal Growth. 110: 312-316. DOI: 10.1016/0022-0248(91)90900-P |
0.527 |
|
| 1990 |
Petsko GA, Rees AR. Second structure determinations. Protein Engineering. 3: 67. PMID 2594725 DOI: 10.1093/Protein/3.2.67 |
0.307 |
|
| 1990 |
Joseph D, Petsko GA, Karplus M. Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop. Science (New York, N.Y.). 249: 1425-8. PMID 2402636 DOI: 10.1126/Science.2402636 |
0.516 |
|
| 1990 |
Ringe D, Petsko GA. Cystic fibrosis. A transport problem? Nature. 346: 312-3. PMID 2374603 DOI: 10.1038/346312A0 |
0.45 |
|
| 1990 |
Stoddard BL, Bruhnke J, Porter N, Ringe D, Petsko GA. Structure and activity of two photoreversible cinnamates bound to chymotrypsin Biochemistry. 29: 4871-4879. PMID 2364065 DOI: 10.1021/Bi00472A017 |
0.598 |
|
| 1990 |
Rose DR, Strong RK, Margolies MN, Gefter ML, Petsko GA. Crystal structure of the antigen-binding fragment of the murine anti-arsonate monoclonal antibody 36-71 at 2.9-Å resolution Proceedings of the National Academy of Sciences of the United States of America. 87: 338-342. PMID 2296590 DOI: 10.1073/Pnas.87.1.338 |
0.582 |
|
| 1990 |
Stoddard BL, Lynne Howell P, Ringe D, Petsko GA. The 2.1-Å resolution structure of iron superoxide dismutase from Pseudomonas ovalis Biochemistry®. 29: 8885-8893. PMID 2271564 DOI: 10.1021/Bi00490A002 |
0.566 |
|
| 1990 |
Stoddard BL, Bruhnke J, Koenigs P, Porter N, Ringe D, Petsko GA. Photolysis and deacylation of inhibited chymotrypsin Biochemistry. 29: 8042-8051. PMID 2261462 DOI: 10.1021/Bi00487A008 |
0.581 |
|
| 1990 |
Neidhart DJ, Kenyon GL, Gerlt JA, Petsko GA. Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous. Nature. 347: 692-4. PMID 2215699 DOI: 10.1038/347692A0 |
0.381 |
|
| 1990 |
Karplus M, Petsko GA. Molecular dynamics simulations in biology. Nature. 347: 631-9. PMID 2215695 DOI: 10.1038/347631A0 |
0.484 |
|
| 1990 |
Farber GK, Petsko GA. The evolution of alpha/beta barrel enzymes. Trends in Biochemical Sciences. 15: 228-34. PMID 2200166 DOI: 10.1016/0968-0004(90)90035-A |
0.304 |
|
| 1990 |
Lolis E, Petsko GA. Transition-state analogues in protein crystallography: probes of the structural source of enzyme catalysis. Annual Review of Biochemistry. 59: 597-630. PMID 2197984 DOI: 10.1146/Annurev.Bi.59.070190.003121 |
0.61 |
|
| 1990 |
Schlichting I, Almo SC, Rapp G, Wilson K, Petratos K, Lentfer A, Wittinghofer A, Kabsch W, Pai EF, Petsko GA, Goody RS. Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis Nature. 345: 309-315. PMID 2111463 DOI: 10.1038/345309A0 |
0.662 |
|
| 1990 |
Neidhart DC, Howell PL, Petsko GA, Gerlt JA, Kozarich JW, Powers VM, Kenyon GL. Restructuring catalysis in the mandelate pathway. Biochemical Society Symposium. 57: 135-41. PMID 2099737 |
0.47 |
|
| 1990 |
Stoddard BL, Ringe D, Petsko GA. The structure of iron superoxide dismutase from Pseudomonas ovalis complexed with the inhibitor azide Protein Engineering, Design and Selection. 4: 113-119. PMID 2075185 DOI: 10.1093/Protein/4.2.113 |
0.567 |
|
| 1990 |
Manning JM, Martinez del Pozo A, Ueno H, Tanizawa K, Nishimura K, Soda K, Ringe D, Stoddard B, Petsko G. Bacterial D-amino acid transaminase. Stereospecificity of reaction pathway, spectral effects, and inactivation generated by D-serine Annals of the New York Academy of Sciences. 585: 516-518. DOI: 10.1111/J.1749-6632.1990.Tb28092.X |
0.497 |
|
| 1990 |
Pai EF, Krengel U, Petsko GA, Goody RS, Kabsch W, Wittinghofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. The Embo Journal. 9: 2351-2359. DOI: 10.1002/J.1460-2075.1990.Tb07409.X |
0.387 |
|
| 1989 |
Martinez Del Pozo A, Pospischil MA, Ueno H, Manning JM, Tanizawa K, Nishimura K, Soda K, Ringe D, Stoddard B, Petsko GA. Effects of D-Serine on Bacterial D-Amino Acid Transaminase: Accumulation of an Intermediate and Inactivation of the Enzyme Biochemistry. 28: 8798-8803. PMID 2513882 DOI: 10.1021/Bi00448A018 |
0.52 |
|
| 1989 |
Farber GK, Glasfeld A, Tiraby G, Ringe D, Petsko GA. Crystallographic studies of the mechanism of xylose isomerase Biochemistry. 28: 7289-7297. PMID 2510821 DOI: 10.1021/Bi00444A022 |
0.606 |
|
| 1989 |
Brünger AT, Karplus M, Petsko GA. Crystallographic refinement by simulated annealing: application to crambin Acta Crystallographica Section a Foundations of Crystallography. 45: 50-61. DOI: 10.1107/S0108767388009195 |
0.447 |
|
| 1988 |
Farber GK, Machin P, Almo SC, Petsko GA, Hajdu J. X-ray Laue diffraction from crystals of xylose isomerase Proceedings of the National Academy of Sciences of the United States of America. 85: 112-115. PMID 3422408 DOI: 10.1073/Pnas.85.1.112 |
0.533 |
|
| 1988 |
Tilton RF, Petsko GA. A structure of sperm whale myoglobin at a nitrogen gas pressure of 145 atmospheres Biochemistry. 27: 6574-6582. PMID 3219355 DOI: 10.1021/Bi00417A057 |
0.312 |
|
| 1988 |
Neidhart DJ, Petsko GA. The refined crystal structure of subtilisin Carlsberg at 2.5 A resolution. Protein Engineering. 2: 271-6. PMID 3150541 DOI: 10.1093/Protein/2.4.271 |
0.434 |
|
| 1988 |
Burley SK, Petsko GA. Weakly polar interactions in proteins. Advances in Protein Chemistry. 39: 125-89. PMID 3072867 DOI: 10.1016/S0065-3233(08)60376-9 |
0.62 |
|
| 1988 |
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. 27: 5948-60. PMID 2847777 DOI: 10.1021/Bi00416A019 |
0.366 |
|
| 1987 |
Brünger AT, Campbell RL, Clore GM, Gronenborn AM, Karplus M, Petsko GA, Teeter MM. Solution of a protein crystal structure with a model obtained from NMR interproton distance restraints. Science (New York, N.Y.). 235: 1049-53. PMID 17782253 DOI: 10.1126/Science.235.4792.1049 |
0.723 |
|
| 1987 |
Frauenfelder H, Hartmann H, Karplus M, Kuntz ID, Kuriyan J, Parak F, Petsko GA, Ringe D, Tilton RF, Connolly ML. Thermal expansion of a protein. Biochemistry. 26: 254-61. PMID 3828301 DOI: 10.1021/Bi00375A035 |
0.695 |
|
| 1987 |
Kozelka J, Archer S, Petsko GA, Lippard SJ, Quigley GJ. Molecular mechanics modeling of oligonucleotide adducts of the antitumor drug cis-diamminedichloroplatinum(II). Biopolymers. 26: 1245-71. PMID 3663859 DOI: 10.1002/Bip.360260804 |
0.425 |
|
| 1987 |
Stoddard B, Howell L, Asano S, Soda K, Tanizawa K, Ringe D, Petsko GA. Preliminary X-ray data for a D-amino acid amino-transferase from a novel thermophilic Bacillus. Journal of Molecular Biology. 196: 441-2. PMID 3656456 DOI: 10.1016/0022-2836(87)90705-4 |
0.547 |
|
| 1987 |
Casal JI, Ahern TJ, Davenport RC, Petsko GA, Klibanov AM. Subunit interface of triosephosphate isomerase: site-directed mutagenesis and characterization of the altered enzyme. Biochemistry. 26: 1258-64. PMID 3552044 DOI: 10.1021/Bi00379A009 |
0.369 |
|
| 1987 |
Ahern TJ, Casal JI, Petsko GA, Klibanov AM. Control of oligomeric enzyme thermostability by protein engineering. Proceedings of the National Academy of Sciences of the United States of America. 84: 675-9. PMID 3543933 DOI: 10.1073/Pnas.84.3.675 |
0.348 |
|
| 1987 |
Farber GK, Petsko GA, Ringe D. The 3.0 A crystal structure of xylose isomerase from Streptomyces olivochromogenes. Protein Engineering. 1: 459-66. PMID 3508293 DOI: 10.1093/Protein/1.6.459 |
0.569 |
|
| 1987 |
Kuriyan J, Karplus M, Petsko GA. Estimation of uncertainties in X-ray refinement results by use of perturbed structures. Proteins. 2: 1-12. PMID 3447165 DOI: 10.1002/Prot.340020102 |
0.603 |
|
| 1987 |
Campbell RL, Petsko GA. Ribonuclease structure and catalysis: crystal structure of sulfate-free native ribonuclease A at 1.5-A resolution. Biochemistry. 26: 8579-84. PMID 3442678 DOI: 10.1021/Bi00400A013 |
0.613 |
|
| 1987 |
Alber TC, Davenport RC, Giammona DA, Lolis E, Petsko GA, Ringe D. 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. 52: 603-13. PMID 3331346 DOI: 10.1101/Sqb.1987.052.01.069 |
0.753 |
|
| 1987 |
BURLEY SK, PETSKO GA. ChemInform Abstract: Dimerization Energetics of Benzene and Aromatic Amino Acid Side Chains. Cheminform. 18. DOI: 10.1002/chin.198717064 |
0.549 |
|
| 1986 |
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. 192: 133-54. PMID 3820301 DOI: 10.1016/0022-2836(86)90470-5 |
0.619 |
|
| 1986 |
Kuriyan J, Petsko GA, Levy RM, Karplus M. Effect of anisotropy and anharmonicity on protein crystallographic refinement. An evaluation by molecular dynamics. Journal of Molecular Biology. 190: 227-54. PMID 3795269 DOI: 10.1016/0022-2836(86)90295-0 |
0.608 |
|
| 1986 |
Ringe D, Petsko GA. Study of protein dynamics by X-ray diffraction. Methods in Enzymology. 131: 389-433. PMID 3773767 DOI: 10.1016/0076-6879(86)31050-4 |
0.562 |
|
| 1986 |
Burley SK, Petsko GA. Amino-aromatic interactions in proteins. Febs Letters. 203: 139-43. PMID 3089835 DOI: 10.1016/0014-5793(86)80730-X |
0.633 |
|
| 1986 |
Burley SK, Petsko GA. Dimerization energetics of benzene and aromatic amino acid side chains Journal of the American Chemical Society. 108: 7995-8001. DOI: 10.1021/Ja00285A019 |
0.623 |
|
| 1986 |
Kozelka J, Petsko GA, Quigley GJ, Lippard SJ. High-salt and low-salt models for kinked adducts of cis-diamminedichloroplatinum(II) with oligonucleotide duplexes Inorganic Chemistry. 25: 1075-1077. DOI: 10.1002/Chin.198633280 |
0.369 |
|
| 1985 |
Burley SK, Petsko GA. Aromatic-aromatic interaction: a mechanism of protein structure stabilization. Science (New York, N.Y.). 229: 23-8. PMID 3892686 DOI: 10.1126/Science.3892686 |
0.623 |
|
| 1985 |
Ringe D, Petsko GA. Mapping protein dynamics by X-ray diffraction. Progress in Biophysics and Molecular Biology. 45: 197-235. PMID 3892584 DOI: 10.1016/0079-6107(85)90002-1 |
0.514 |
|
| 1985 |
Kozelka J, Petsko GA, Lippard SJ, Quigley GJ. Molecular mechanics calculations on cis-[Pt(NH3)2{d(GpG)}] adducts in two oligonucleotide duplexes Journal of the American Chemical Society. 107: 4079-4081. DOI: 10.1021/Ja00299A055 |
0.369 |
|
| 1985 |
Tilton, Jr. R, Kuntz, Jr. I, Petsko G. Corrections - Cavities in Proteins: Structure of a Metmyoglobin-Xenon Complex Solved to 1.9 Å Biochemistry. 24: 7853-7853. DOI: 10.1021/Bi00347A601 |
0.318 |
|
| 1985 |
Lord RC, Petsko GA, Seaton BA, Goodfriend L. Laser Raman spectroscopy of biomolecules: Structural studies of ragweed allergen Ra5 Spectrochimica Acta Part a: Molecular Spectroscopy. 41: 199-203. DOI: 10.1016/0584-8539(85)80097-0 |
0.614 |
|
| 1985 |
KOZELKA J, PETSKO GA, LIPPARD SJ, QUIGLEY G. ChemInform Abstract: MOLECULAR MECHANICS CALCULATIONS ON CIS-(PT(NH3)2(D(GPG))) ADDUCTS IN TWO OLIGONUCLEOTIDE DUPLEXES Chemischer Informationsdienst. 16. DOI: 10.1002/Chin.198543063 |
0.371 |
|
| 1984 |
Ringe D, Petsko GA, Kerr DE, Ortiz de Montellano PR. Reaction of myoglobin with phenylhydrazine: a molecular doorstop. Biochemistry. 23: 2-4. PMID 6691963 DOI: 10.1021/Bi00296A001 |
0.53 |
|
| 1984 |
Tilton RF, Kuntz ID, Petsko GA. Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9 Å Biochemistry. 23: 2849-2857. PMID 6466620 DOI: 10.1021/Bi00308A002 |
0.387 |
|
| 1984 |
Petsko GA, Davenport RC, Frankel D, RaiBhandary UL. Probing the catalytic mechanism of yeast triose phosphate isomerase by site-specific mutagenesis. Biochemical Society Transactions. 12: 229-32. PMID 6373437 DOI: 10.1042/Bst0120229 |
0.408 |
|
| 1984 |
Petsko GA, Ringe D. Fluctuations in protein structure from X-ray diffraction. Annual Review of Biophysics and Bioengineering. 13: 331-71. PMID 6331286 DOI: 10.1146/annurev.bb.13.060184.001555 |
0.489 |
|
| 1984 |
Seaton BA, Campbell RL, Petsko GA, Rose DR, Edelstein I, Marcus F. Preliminary X-ray crystallographic studies of pig kidney fructose-1,6-bisphosphatase. The Journal of Biological Chemistry. 259: 8915-6. PMID 6086617 |
0.618 |
|
| 1984 |
Burley SK, Petsko GA, Ringe D. Effects of X-irradiation of single crystals of ribonuclease A Acta Crystallographica Section a Foundations of Crystallography. 40: C41-C41. DOI: 10.1107/S0108767384098548 |
0.693 |
|
| 1984 |
Douzou P, Petsko GA. Proteins at Work: “Stop-Action” Pictures at Subzero Temperatures Advances in Protein Chemistry. 36: 245-361. DOI: 10.1016/S0065-3233(08)60299-5 |
0.406 |
|
| 1983 |
Rose DR, Seaton BA, Petsko GA, Novotný J, Margolies MN, Locke E, Haber E. Crystallization of the Fab fragment of a monoclonal anti-digoxin antibody and its complex with digoxin. Journal of Molecular Biology. 165: 203-6. PMID 6842605 DOI: 10.1016/S0022-2836(83)80252-6 |
0.637 |
|
| 1983 |
Ringe D, Petsko GA, Yamakura F, Suzuki K, Ohmori D. Structure of iron superoxide dismutase from Pseudomonas ovalis at 2.9-A resolution. Proceedings of the National Academy of Sciences of the United States of America. 80: 3879-83. PMID 6575382 DOI: 10.1073/Pnas.80.13.3879 |
0.558 |
|
| 1983 |
Smith WW, Pattridge KA, Ludwig ML, Petsko GA, Tsernoglou D, Tanaka M, Yasunobu KT. Structure of oxidized flavodoxin from Anacystis nidulans. Journal of Molecular Biology. 165: 737-53. PMID 6406674 DOI: 10.1016/S0022-2836(83)80277-0 |
0.371 |
|
| 1983 |
Mowbray SL, Petsko GA. The x-ray structure of the periplasmic galactose binding protein from Salmonella typhimurium at 3.0-A resolution. The Journal of Biological Chemistry. 258: 7991-7. PMID 6345536 DOI: 10.2210/Pdb1Gbp/Pdb |
0.64 |
|
| 1983 |
Seaton BA, Head JF, Lord RC, Petsko GA. Studies of calmodulin structure: laser raman spectroscopy of biomolecules. Biochemistry. 22: 973-8. PMID 6301532 DOI: 10.1021/Bi00273A041 |
0.63 |
|
| 1983 |
Ringe D, Petsko GA, Yamakura F, Suzuki K, Ohmori D. The iron content of iron superoxide dismutase: determination by anomalous scattering. Proceedings of the Royal Society of London. Series B, Biological Sciences. 218: 119-26. PMID 6135208 DOI: 10.1098/Rspb.1983.0030 |
0.531 |
|
| 1982 |
Pinn E, Pähler A, Saenger W, Petsko GA, Green NM. Crystallization and preliminary X-ray investigation of avidin European Journal of Biochemistry. 123: 545-546. PMID 7075599 DOI: 10.1111/J.1432-1033.1982.Tb06566.X |
0.302 |
|
| 1982 |
Mowbray SL, Petsko GA. Preliminary X-ray data for the ribose binding protein from Salmonella typhimurium. Journal of Molecular Biology. 160: 545-7. PMID 6759659 DOI: 10.1016/0022-2836(82)90313-8 |
0.618 |
|
| 1982 |
Gilbert WA, Lord RC, Petsko GA, Thamann TJ. Laser-Raman spectroscopy of biomolecules 16-temperature dependence of the conformation of crystalline ribonuclease a from x-ray diffraction and Raman spectroscopy Journal of Raman Spectroscopy. 12: 173-179. DOI: 10.1002/Jrs.1250120217 |
0.713 |
|
| 1981 |
Alber T, Fahnestock M, Mowbray SL, Petsko GA. Preliminary x-ray data for the galactose binding protein from Salmonella typhimurium. Journal of Molecular Biology. 147: 471-4. PMID 7031261 DOI: 10.1016/0022-2836(81)90497-6 |
0.724 |
|
| 1981 |
Alber T, Banner DW, Bloomer AC, Petsko GA, Phillips D, Rivers PS, Wilson IA. On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 293: 159-171. PMID 6115415 DOI: 10.1098/Rstb.1981.0069 |
0.798 |
|
| 1981 |
Tsernoglou D, Petsko GA, Hudson RA. Structure and Function of Snake Venom Curarimimetic Neurotoxins Molecular Pharmacology. 14: 710-716. DOI: 10.2210/Pdb1Nxb/Pdb |
0.32 |
|
| 1980 |
Frauenfelder H, Petsko GA. Structural dynamics of liganded myoglobin. Biophysical Journal. 32: 465-83. PMID 7248456 DOI: 10.1016/S0006-3495(80)84984-8 |
0.349 |
|
| 1979 |
Frauenfelder H, Petsko GA, Tsernoglou D. Temperature-dependent X-ray diffraction as a probe of protein structural dynamics. Nature. 280: 558-63. PMID 460437 DOI: 10.1038/280558A0 |
0.323 |
|
| 1978 |
Petsko GA, Phillips DC, Williams RJ, Wilson IA. On the protein crystal chemistry of chloroplatinite ions: general principles and interactions with triose phosphate isomerase. Journal of Molecular Biology. 120: 345-59. PMID 650685 DOI: 10.1016/0022-2836(78)90423-0 |
0.701 |
|
| 1977 |
Tsernoglou D, Petsko GA. Three-dimensional structure of neurotoxin a from venom of the Philippines sea snake. Proceedings of the National Academy of Sciences of the United States of America. 74: 971-4. PMID 265589 DOI: 10.1073/Pnas.74.3.971 |
0.35 |
|
| 1976 |
Banner DW, Bloomer Ac, Petsko GA, Phillips DC, Wilson IA. Atomic coordinates for triose phosphate isomerase from chicken muscle. Biochemical and Biophysical Research Communications. 72: 146-55. PMID 985462 DOI: 10.1016/0006-291X(76)90972-4 |
0.662 |
|
| 1976 |
Petsko GA, Tsernoglou D. The structure of subtilopeptidase A. I. X-ray crystallographic data. Journal of Molecular Biology. 106: 453-6. PMID 978729 DOI: 10.1016/0022-2836(76)90096-6 |
0.355 |
|
| 1976 |
Tsernoglou D, Petsko GA. The crystal structure of a post-synaptic neurotoxin from sea snake at A resolution. Febs Letters. 68: 1-4. PMID 964372 DOI: 10.1016/0014-5793(76)80390-0 |
0.335 |
|
| 1976 |
Alber T, Petsko GA, Tsernoglou D. Crystal structure of elastase-substrate complex at -55 °C Nature. 263: 297-300. PMID 958484 DOI: 10.1038/263297A0 |
0.638 |
|
| 1975 |
Banner DW, Bloomer AC, Petsko GA, Phillips DC, Pogson CI, Wilson IA, Corran PH, Furth AJ, Milman JD, Offord RE, Priddle JD, Waley SG. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data. Nature. 255: 609-14. PMID 1134550 DOI: 10.1038/255609A0 |
0.672 |
|
| 1975 |
Petsko GA. Protein crystallography at sub-zero temperatures: cryo-protective mother liquors for protein crystals. Journal of Molecular Biology. 96: 381-92. PMID 240944 DOI: 10.1016/0022-2836(75)90167-9 |
0.323 |
|
| 1975 |
Douzou P, Hoa GH, Petsko GA. Protein crystallography at sub-zero temperatures: lysozyme-substrate complexes in cooled mixed solvents. Journal of Molecular Biology. 96: 367-80. PMID 240943 DOI: 10.1016/0022-2836(75)90166-7 |
0.361 |
|
| 1972 |
Banner DW, Bloomer AC, Petsko GA, Phillips DC, Pogson CI. Crystallographic studies of chicken triose phosphate isomerase. Cold Spring Harbor Symposia On Quantitative Biology. 36: 151-5. PMID 4508133 DOI: 10.1101/Sqb.1972.036.01.021 |
0.646 |
|
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