G. Petsko

发表

Molecular dynamics simulations in biology

M. Karplus, G. Petsko, 1990, Nature.

Climate change and the integrity of science.

G. B. Dalrymple, W. R. Gardner, R. Rivest, 2010, Science.

Big science, little science

G. Petsko, 2009, EMBO reports.

Weakly polar interactions in proteins.

G. Petsko, S. Burley, 1988, Advances in protein chemistry.

Molecular graphics: application to the structure determination of a snake venom neurotoxin.

G. Petsko, D. Tsernoglou, J. E. McQueen, 1977, Science.

The system is broken

G. Petsko, 2006, Genome Biology.

Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins

G. Petsko, D. Ringe, C. Brenner, 1997, Nature Structural Biology.

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

G. Petsko, D. Ringe, J. Shaw, 1997, Biochemistry.

The blue marble

G. Petsko, 2011, Genome Biology.

The past is a foreign country

G. Petsko, 2010, Genome Biology.

And they said it wouldn't last...

G. Petsko, 2010, Genome Biology.

Crystallographic refinement by simulated annealing: application to crambin

M. Karplus, G. Petsko, A. Brunger, 1989 .

Temperature-dependent X-ray diffraction as a probe of protein structural dynamics

Hans Frauenfelder, Gregory A. Petsko, G. Petsko, 1979, Nature.

Fluctuations in protein structure from X-ray diffraction.

G A Petsko, G. Petsko, D. Ringe, 1984, Annual review of biophysics and bioengineering.

Evidence of the participation of remote residues in the catalytic activity of Co-type nitrile hydratase from Pseudomonas putida.

G. Petsko, M. Ondrechen, D. Ringe, 2011, Biochemistry.

Schnurri-3 regulates ERK downstream of WNT signaling in osteoblasts.

G. Petsko, S. Gygi, D. Zaller, 2013, The Journal of clinical investigation.

Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus.

G. Petsko, D. Ringe, S. Lovett, 1997, Journal of molecular biology.

Aromatic-aromatic interaction: a mechanism of protein structure stabilization.

G A Petsko, S K Burley, G. Petsko, 1985, Science.

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

G A Petsko, G. Petsko, P. Závodszky, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Purification, catalytic properties and thermostability of 3-isopropylmalate dehydrogenase from Escherichia coli.

G. Petsko, S. Lovett, G. Wallon, 1997, Biochimica et biophysica acta.

Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5Å resolution: using amino acid sequence data

G. Petsko, D. Phillips, I. Wilson, 1975, Nature.

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

G. Petsko, D. Ringe, 2003, Biophysical chemistry.

Multiple solvent crystal structures: probing binding sites, plasticity and hydration.

G. Petsko, D. Vitkup, D. Ringe, 2006, Journal of molecular biology.

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.

G. Petsko, J. Dewan, R. Tilton, 1993, Biochemistry.

Crystalline ribonuclease A loses function below the dynamical transition at 220 K

G. Petsko, D. Ringe, Ann M Stock, 1992, Nature.

The refined crystal structure of subtilisin Carlsberg at 2.5 A resolution.

G A Petsko, G. Petsko, D. Neidhart, 1988, Protein engineering.

How Enzymes Work

G. Petsko, D. Ringe, 2008, Science.

Conformational substates in a protein: structure and dynamics of metmyoglobin at 80 K.

G. Petsko, H. Frauenfelder, W. Steigemann, 1982, Proceedings of the National Academy of Sciences of the United States of America.

Guilt by association

G. Petsko, 2009, Genome Biology.

The 1.1-Å resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease

G. Petsko, D. Ringe, Y. Hod, 2003, Proceedings of the National Academy of Sciences of the United States of America.

The dark side

G. Petsko, 2000, Genome Biology.

My worries are no longer behind me

G. Petsko, 2007, Genome Biology.

Cavities in proteins: structure of a metmyoglobin-xenon complex solved to 1.9 A.

I. Kuntz, G. Petsko, R. Tilton, 1984, Biochemistry.

On the origin of enzymatic species.

G. Petsko, D. Ringe, G. L. Kenyon, 1993, Trends in biochemical sciences.

Three-dimensional structure of neurotoxin a from venom of the Philippines sea snake.

G. Petsko, D. Tsernoglou, 1977, Proceedings of the National Academy of Sciences of the United States of America.

The evolution of alpha/beta barrel enzymes.

G. Petsko, G. Farber, 1990, Trends in biochemical sciences.

An Experimental Approach to Mapping the Binding Surfaces of Crystalline Proteins

Karen N. Allen, G. Petsko, D. Ringe, 1996 .

“Sleeping Beauty”: Quiescence in Saccharomyces cerevisiae

Dagmar Ringe, Joseph V. Gray, Margaret Werner-Washburne, 2004, Microbiology and Molecular Biology Reviews.

Structure of acid beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease.

Gregory A Petsko, Dagmar Ringe, R. L. Lieberman, 2006, Nature chemical biology.

Latrepirdine improves cognition and arrests progression of neuropathology in an Alzheimer's mouse model

G. Petsko, J. Buxbaum, D. Ringe, 2013, Molecular Psychiatry.

Study of protein dynamics by X-ray diffraction.

G A Petsko, G. Petsko, D. Ringe, 1986, Methods in enzymology.

[19]Study of protein dynamics by X-ray diffraction

Dagmar Ringe, Gregory A. Petsko, G. Petsko, 1986 .

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

Gregory A Petsko, Dagmar Ringe, Chittaranjan Das, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Intrinsic motions along an enzymatic reaction trajectory

Mark A. Wilson, Martin Karplus, Gregory A. Petsko, 2007, Nature.

Economies of scale

Gregory A Petsko, G. Petsko, 2012, Genome Biology.

Effects of pH and iminosugar pharmacological chaperones on lysosomal glycosidase structure and stability.

R. L. Lieberman, G. Petsko, D. Ringe, 2009, Biochemistry.

Preservation of forelimb function by UPF1 gene therapy in a rat model of TDP-43-induced motor paralysis

G. Petsko, L. Maquat, D. Ringe, 2014, Gene Therapy.

Anatomy of a conformational change: hinged "lid" motion of the triosephosphate isomerase loop.

M Karplus, G A Petsko, M. Karplus, 1990, Science.

Chemistry and biology.

G A Petsko, G. Petsko, 2000, Proceedings of the National Academy of Sciences of the United States of America.

A transport problem?

Dagmar Ringe, Gregory A. Petsko, G. Petsko, 1990, Nature.

Targeted stabilization of Munc18‐1 function via pharmacological chaperones

G. Petsko, Jacqueline Burré, Manu Sharma, 2020, EMBO molecular medicine.

Analogous inhibitors of elastase do not always bind analogously

Dagmar Ringe, Carla Mattos, Gregory A. Petsko, 1994, Nature Structural Biology.

Structure of yeast triosephosphate isomerase at 1.9-A resolution.

F. C. Hartman, G A Petsko, G. Petsko, 1990, Biochemistry.

The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization

Mark A. Wilson, Dagmar Ringe, David W. Miller, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Estimation of uncertainties in X‐ray refinement results by use of perturbed structures

M Karplus, J Kuriyan, G A Petsko, 1987, Proteins.

Effect of anisotropy and anharmonicity on protein crystallographic refinement. An evaluation by molecular dynamics.

M Karplus, J Kuriyan, G A Petsko, 1986, Journal of molecular biology.

A low‐temperature device for protein crystallography

G. Petsko, D. J. Marsh, 1973 .

Mapping protein dynamics by X-ray diffraction.

G A Petsko, G. Petsko, D. Ringe, 1985, Progress in biophysics and molecular biology.

Crystal structure at 1.8 A resolution of CDP-D-glucose 4,6-dehydratase from Yersinia pseudotuberculosis.

G. Petsko, D. Ringe, Hung‐wen Liu, 2004, Biochemistry.

What is a chaperone in the context of pharmacology?

G. Petsko, 2009 .

Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway.

M Karplus, G A Petsko, M. Karplus, 1991, Biochemistry.

TransnitrosylationfromDJ-1toPTENAttenuatesNeuronal CellDeathinParkinson'sDiseaseModels

G. Petsko, 2014 .

Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism.

G. Petsko, J. Knowles, E. Nickbarg, 1988, Biochemistry.

Crystallization of yeast triose phosphate isomerase from polyethylene glycol. Protein crystal formation following phase separation.

F. C. Hartman, G. Petsko, D. Tsernoglou, 1981, The Journal of biological chemistry.

Behind the Movement

G. Petsko, D. Ringe, 2012, Cell.

Protein misfolding and temperature up-shift cause G1 arrest via a common mechanism dependent on heat shock factor in Saccharomyces cerevisiae

Sue A. Krause, G. Petsko, J. V. Gray, 2001, Proceedings of the National Academy of Sciences of the United States of America.

On the other hand...

G. Petsko, 1992, Science.

Protein crystallography at sub-zero temperatures: lysozyme-substrate complexes in cooled mixed solvents.

G. Petsko, G. H. Hoa, P. Douzou, 1975, Journal of molecular biology.

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

M. Karplus, G. Petsko, D. Vitkup, 1997, Nature Structural Biology.

Sweden has the right idea

G. Petsko, 2006, Genome Biology.

Structural analysis of the active site of porcine pancreatic elastase based on the X-ray crystal structures of complexes with trifluoroacetyl-dipeptide-anilide inhibitors.

G A Petsko, G. Petsko, D. Ringe, 1995, Biochemistry.

The alrestatin double-decker: binding of two inhibitor molecules to human aldose reductase reveals a new specificity determinant.

G. Petsko, D. Ringe, D. Harrison, 1997, Biochemistry.

Activity of crystalline turkey egg white lysozyme

G. Petsko, J. Hajdu, P. Howell, 1992, Proteins.

Post-translational modification by cysteine protects Cu/Zn-superoxide dismutase from oxidative damage.

Qian Liu, Gregory A Petsko, Dagmar Ringe, 2013, Biochemistry.

Structural consequences of cysteinylation of Cu/Zn-superoxide dismutase.

Jared R. Auclair, Jared R Auclair, G. Petsko, 2013, Biochemistry.

Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis

Jared R. Auclair, Jared R Auclair, G. Petsko, 2010, Proceedings of the National Academy of Sciences.

A Pathfinder in High-Pressure Bioscience: In Memoriam of Gaston Hui Bon Hoa

G. Petsko, S. Sligar, J. Kornblatt, 2021, Biology.

Preliminary x-ray data for the galactose binding protein from Salmonella typhimurium.

G. Petsko, T. Alber, S. Mowbray, 1981, Journal of molecular biology.

The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica

G. Petsko, D. Ringe, W. Desmarais, 2006, JBIC Journal of Biological Inorganic Chemistry.

High-salt and low-salt models for kinked adducts of cis-diamminedichloroplatinum(II) with oligonucleotide duplexes

G. Petsko, G. Quigley, S. Lippard, 1986 .

Purification and crystallization of benzoylformate decarboxylase

G. Petsko, D. Ringe, M. Hasson, 1995, Protein science : a publication of the Protein Society.

Cholera toxin inhibits SNX27-retromer-mediated delivery of cargo proteins to the plasma membrane

G. Petsko, R. Cole, D. Berman, 2018, Journal of Cell Science.

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.

G. Petsko, D. Ringe, L. Hedstrom, 2000, Biochemistry.

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.

G. Petsko, D. Ringe, A. Milne, 2008, Biochemistry.

Structure Determination of Mycobacterium tuberculosis Serine Protease Hip1 (Rv2224c).

G. Petsko, D. Ringe, A. Milne, 2017, Biochemistry.

Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis.

G. Petsko, D. Ringe, E. Stone, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Induced pluripotent stem cells: a tool for modeling Parkinson’s disease

G. Petsko, L. Studer, A. Bose, 2022, Trends in Neurosciences.

Kinetic, spectroscopic, and X-ray crystallographic characterization of the functional E151H aminopeptidase from Aeromonas proteolytica.

G. Petsko, D. Ringe, R. Holz, 2005, Biochemistry.

The Coming Epidemic of Neurologic Disorders: What Science Is – and Should Be – Doing About It

G. Petsko, 2012, Daedalus.

AAVrh.10-Mediated APOE2 Central Nervous System Gene Therapy for APOE4-Associated Alzheimer's Disease.

G. Petsko, S. Paul, D. Ballon, 2018, Human gene therapy. Clinical development.

A new alpha-synuclein missense variant (Thr72Met) in two Turkish families with Parkinson’s disease

G. Petsko, M. Emre, H. Hanagasi, 2021, Parkinsonism & related disorders.

Targeting α -synuclein for treating Parkinson’s disease: mechanistic and therapeutic considerations

Miquel, G. Petsko, E. Bézard, 2017 .

X-ray crystallographic studies of the alanine-specific racemase from Bacillus stearothermophilus. Overproduction, crystallization, and preliminary characterization.

G. Petsko, C. Walsh, M. Distefano, 1987, The Journal of biological chemistry.

High resolution X-ray and NMR structural study of human T-cell immunoglobulin and mucin domain containing protein-3

G. Petsko, G. Wagner, V. Kuchroo, 2018, Scientific Reports.

The iron content of iron superoxide dismutase: determination by anomalous scattering

G. Petsko, D. Ringe, K. Suzuki, 1983, Proceedings of the Royal Society of London. Series B. Biological Sciences.

Crystallization of the Fab fragment of a monoclonal anti-digoxin antibody and its complex with digoxin.

G. Petsko, J. Novotný, E. Haber, 1983, Journal of molecular biology.

Nuclear receptor Nurr1 agonists enhance its dual functions and improve behavioral deficits in an animal model of Parkinson’s disease

G. Petsko, D. Ringe, Joon Shin, 2015, Proceedings of the National Academy of Sciences.

Juntendo Medical Journal

G. Petsko, F. Yamakura, Masao Tsukada, 2015 .

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

G. Petsko, D. Ringe, T. Fenn, 2003, Acta crystallographica. Section D, Biological crystallography.

From Sequence to Consequence: Structural Biology and Rational Drug Design in the Age of Genomics

G. Petsko, D. Ringe, 2003 .

Mandelate racemase and class-related enzymes

G. Petsko, G. L. Kenyon, J. Gerlt, 1992 .

1-Butaneboronic acid binding to Aeromonas proteolytica aminopeptidase: a case of arrested development.

G. Petsko, D. Ringe, R. Holz, 1999, Biochemistry.

Progress and Problems in the Study of Protein Dynamics by X-Ray Diffraction

G. Petsko, 1987 .

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

G. Petsko, D. Ringe, E. Pozharski, 2007, Biochemistry.

D-CYCLOSERINE INACTIVATION OF D-AMINO ACID AMINOTRANSFERASE LEADS TO A STABLE NONCOVALENT PROTEIN COMPLEX WITH AN AROMATIC CYCLOSERINE-PLP DERIVATIVE

G. Petsko, D. Ringe, D. Peisach, 1998 .

Preparation of isomorphous heavy-atom derivatives.

G. Petsko, 1985, Methods in enzymology.

Latrepirdine (dimebon) enhances autophagy and reduces intracellular GFP-Aβ42 levels in yeast.

G. Petsko, D. Ringe, R. Martins, 2012, Journal of Alzheimer's disease : JAD.

Spectroscopic and X-ray crystallographic characterization of bestatin bound to the aminopeptidase from Aeromonas (Vibrio) proteolytica.

G. Petsko, D. Ringe, R. Holz, 2004, Biochemistry.

[12] Flow cell construction and use

G. Petsko, 1985 .

Laser‐Raman spectroscopy of biomolecules 16‐temperature dependence of the conformation of crystalline ribonuclease a from x‐ray diffraction and Raman spectroscopy

G. Petsko, T. J. Thamann, R. Lord, 1982 .

Retromer Combinatorials for Gene-Therapy Across a Spectrum of Neurological Diseases

G. Petsko, S. Small, Yasir H. Qureshi, 2020, bioRxiv.

Inactivation and destruction of conserved Trp159 of Fe-superoxide dismutase from Porphyromonas gingivalis by hydrogen peroxide.

G. Petsko, D. Ringe, K. Nakayama, 1998, European journal of biochemistry.

X-ray Laue diffraction from crystals of xylose isomerase.

G. Petsko, J. Hajdu, S. Almo, 1988, Proceedings of the National Academy of Sciences of the United States of America.

The introduction of specific sites for heavy metal binding in a crystalline protein.

G. Petsko, S. Mowbray, 1983, The Journal of biological chemistry.

Ribonuclease structure and catalysis: crystal structure of sulfate-free native ribonuclease A at 1.5-A resolution.

G. Petsko, R. Campbell, 1987, Biochemistry.

Mandelate Racemase: Structure-Function Studies of a Pseudosymmetric Enzyme

G. Petsko, G. L. Kenyon, J. Gerlt, 1995 .

High-Salt and Low-Salt Models for Kinked Adducts of cis-Diamminedichloroplatinum(II) with Oligonucleotide Duplexes.

G. Petsko, G. Quigley, S. Lippard, 1986 .

Laser Raman spectroscopy of biomolecules: Structural studies of ragweed allergen Ra5

G. Petsko, B. Seaton, R. Lord, 1985 .

Probing the catalytic mechanism of yeast triose phosphate isomerase by site-specific mutagenesis.

G. Petsko, R. C. Davenport, D. Frankel, 1984, Biochemical Society transactions.

Mobilitv and J function in proteins and nucleicacids

G. Petsko, F. Richards, J. Whelan, 2013 .

David Phillips and the origin of structural enzymology.

G. Petsko, L. Johnson, 1999, Trends in biochemical sciences.

Structure-Function Relationships in Mandelate Racemase and Muconate Lactonizing Enzyme

G. Petsko, G. L. Kenyon, J. Gerlt, 1990 .

Crystallographic studies of chicken triose phosphate isomerase.

G. Petsko, D. Phillips, D. Banner, 1972, Cold Spring Harbor symposia on quantitative biology.

The structure of subtilopeptidase A. I. X-ray crystallographic data.

G. Petsko, D. Tsernoglou, 1976, Journal of molecular biology.

The little Big Bang

G. Petsko, 1994, Nature.

Preliminary x-ray data on crystals of mandelate racemase.

G. Petsko, G. L. Kenyon, J. Gerlt, 1988, The Journal of biological chemistry.

Engineering and design.

Gregory A. Petsko, Stephen G. Sligar, G. Petsko, 1995, Current opinion in structural biology.

Electrostatic interactions in aromatic oligopeptides contribute to protein stability

Stephen K. Burley, Gregory A. Petsko, G. Petsko, 1989 .

Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis

Steven C. Almo, Ilme Schlichting, Alfred Wittinghofer, 1990, Nature.

Quantum enzymology: Tunnel vision

Dagmar Ringe, Gregory A. Petsko, G. Petsko, 1999, Nature.

Solvent mobility and the protein 'glass' transition

Dagmar Ringe, Dennis Vitkup, Martin Karplus, 2000, Nature Structural Biology.

Crystal structure of Bacillus subtilis GabR, an autorepressor and transcriptional activator of gabT

Wei Wang, Thomas C. Terwilliger, Dagmar Ringe, 2013, Proceedings of the National Academy of Sciences.

The oxidation state of DJ-1 regulates its chaperone activity toward α-synuclein

Mark A. Wilson, Wenbo Zhou, Gregory A. Petsko, 2006 .

On the limitations of the Laue method when applied to crystals of macromolecules

Steven C. Almo, Soichi Wakatsuki, Gregory A. Petsko, 1992 .

X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis.

Dagmar Ringe, Gregory A. Petsko, Karen N. Allen, 1994, Biochemistry.

Biology's structurally sound foundations

Gregory A. Petsko, G. Petsko, 1999, Nature.

Molecular metamorphosis

Dagmar Ringe, Gregory A. Petsko, G. Petsko, 1991, Nature.

The structural enzymology of proton-transfer reactions

John Alan Gerlt, Dagmar Ringe, Martin Karplus, 1993 .

Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous

Gregory A. Petsko, G. Petsko, G. L. Kenyon, 1990, Nature.

Current Protocols in Bioinformatics: Preface

Lincoln Stein, Gary D. Stormo, Andreas D. Baxevanis, 2010 .

Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate Modeling and Active Site Mutations†

Hua Guo, Dagmar Ringe, Gregory A. Petsko, 2008, Biochemistry.

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

G. Petsko, D. Ringe, W. Fast, 2007, Biochemistry.

The evolution of a/ barrel enzymes

Gregory A. Petsko, Gregory K. Farber, G. Petsko, 1990 .

Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis. 1. Product-Bound Structures†‡

Dagmar Ringe, Gregory A. Petsko, Walter Fast, 2008, Biochemistry.

Art is long and time is fleeting: the current problems and future prospects for time-resolved enzyme crystallography

Gregory A. Petsko, G. Petsko, 1992, Philosophical Transactions of the Royal Society of London. Series A: Physical and Engineering Sciences.

Observation of the light-triggered binding of pyrone to chymotrypsin by Laue x-ray crystallography.

G. Petsko, B. Stoddard, D. Ringe, 1991, Proceedings of the National Academy of Sciences of the United States of America.

CEACAM1 regulates TIM-3-mediated tolerance and exhaustion

Hidde L. Ploegh, Andre Franke, Yasuyuki Kondo, 2014, Nature.

Corrigendum: CEACAM1 regulates TIM-3-mediated tolerance and exhaustion

G. Petsko, M. Ostrowski, H. Ploegh, 2016, Nature.

About the Validation of Homology Models: A Case Study on Factor D, a Serine Protease in the Human Complement System

Dagmar Ringe, Gregory A. Petsko, Thomas Thüne, 1996, German Conference on Bioinformatics.

Fishing in Src-infested waters

Gregory A. Petsko, G. Petsko, 1992, Nature.

Why protein R‐factors are so large: A self‐consistent analysis

Gregory A Petsko, Dagmar Ringe, Dennis Vitkup, 2002, Proteins.

Anchoring a cationic ligand: the structure of the Fab fragment of the anti-morphine antibody 9B1 and its complex with morphine.

Edwin Pozharski, Dagmar Ringe, G. Petsko, 2004, Journal of molecular biology.

Artifacts to avoid while taking advantage of top‐down mass spectrometry based detection of protein S‐thiolation

Sandro Santagata, Dagmar Ringe, Jared R. Auclair, 2014, Proteomics.

A soluble α-synuclein construct forms a dynamic tetramer

Wei Wang, Gregory A Petsko, Dagmar Ringe, 2011, Proceedings of the National Academy of Sciences.

Crystal cryocooling distorts conformational heterogeneity in a model Michaelis complex of DHFR.

David A Sivak, Henry van den Bedem, David A. Sivak, 2014, Structure.

Testing Electrostatic Complementarity in Enzyme Catalysis: Hydrogen Bonding in the Ketosteroid Isomerase Oxyanion Hole

Daniel Herschlag, Gregory A Petsko, Dagmar Ringe, 2006, PLoS biology.

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

Gregory A Petsko, Dagmar Ringe, G. Petsko, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Photolysis and deacylation of inhibited chymotrypsin.

G. Petsko, B. Stoddard, D. Ringe, 1990, Biochemistry.

Endosomal recycling reconciles the Alzheimer’s disease paradox

G. Petsko, S. Small, 2020, Science Translational Medicine.

The catalytic pathway of cytochrome p450cam at atomic resolution.

J Berendzen, R M Sweet, D. E. Benson, 2000, Science.

A lily worth gilding

G. Petsko, Laurie H Glimcher, 2021, Cell.

Elucidating the causes of neurodegeneration

G. Petsko, S. Small, 2022, Science.

Identification of RIOK2 as a master regulator of human blood cell development

G. Petsko, L. Glimcher, Steve Carr, 2021, Nature Immunology.

Transformation

G. Petsko, 2006, Genome Biology.

Homologuephobia

G. Petsko, 2001, Genome Biology.

Winter, plague and pestilence

G. Petsko, 2001, Genome Biology.

The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein.

G. Petsko, Min Zhu, A. Fink, 2006, Journal of molecular biology.

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

G. Petsko, D. Ringe, J. Kozarich, 2004, Biochemistry.

Many happy returns

G. Petsko, 2009, Genome Biology.

Structural analysis of human CEACAM1 oligomerization

G. Petsko, N. Beauchemin, R. Blumberg, 2022, Communications Biology.

The right to be wrong

G. Petsko, 2008, Genome Biology.

Heavy metal revival

G. Petsko, 1995, Nature.

Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase.

G. Petsko, D. Ringe, G. L. Kenyon, 2009, Biochemistry.

Retromer in Alzheimer disease, Parkinson disease and other neurological disorders

G. Petsko, S. Small, 2015, Nature Reviews Neuroscience.

Effects of D-serine on bacterial D-amino acid transaminase: accumulation of an intermediate and inactivation of the enzyme.

G. Petsko, B. Stoddard, D. Ringe, 1989, Biochemistry.

Preliminary X-ray data for a D-amino acid amino-transferase from a novel thermophilic Bacillus.

G. Petsko, B. Stoddard, D. Ringe, 1987, Journal of molecular biology.

Proton magnetic resonance studies of ``polywater-water'' mixtures

G. Petsko, 1971 .

New high pH crystal forms of ribonucleases A and S.

G. Petsko, D. Tsernoglou, P. Martin, 1976, Journal of molecular biology.

Site‐directed Mutagenesis Applied to Glucose Isomerase from Streptomyces violaceoniger and Streptomyces olivochromogenes

G. Petsko, A. Glasfeld, G. Tiraby, 1990, Annals of the New York Academy of Sciences.

Chemically stable fluorescent proteins for advanced microscopy

G. Petsko, L. Looger, Ce-Feng Liu, 2022, Nature Methods.

Instructions for repair

G. Petsko, 2006, Genome Biology.

The Use of Pharmacological Retromer Chaperones in Alzheimer’s Disease and other Endosomal-related Disorders

G. Petsko, D. Ringe, D. Berman, 2014, Neurotherapeutics.

Transformation

G. Petsko, 2006, Genome Biology.

Left-handed comments.

G. Petsko, 1992, Science.

Let's get our priorities straight

G. Petsko, 2006, Genome Biology.

The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate.

G L Kenyon, G A Petsko, G. Petsko, 1994, Biochemistry.

Structure and activity of two photoreversible cinnamates bound to chymotrypsin.

G A Petsko, G. Petsko, B. Stoddard, 1990, Biochemistry.

An idea whose time has gone

Gregory A Petsko, G. Petsko, 2007, Genome Biology.

Endosomal Traffic Jams Represent a Pathogenic Hub and Therapeutic Target in Alzheimer’s Disease

G. Petsko, R. Mayeux, S. Small, 2017, Trends in Neurosciences.

The crystal structure of a post‐synaptic neurotoxin from sea snake at 2.2 Å resolution

G. Petsko, D. Tsernoglou, 1976, FEBS letters.

Structure and function of snake venom curarimimetic neurotoxins.

D Tsernoglou, G A Petsko, G. Petsko, 1981, Molecular pharmacology.

Count me out

G. Petsko, 2000, Genome Biology.

The walking dead

Gregory A Petsko, G. Petsko, 2011, Genome Biology.

Xylose isomerase in substrate and inhibitor michaelis States: atomic resolution studies of a metal-mediated hydride shift(,).

G. Petsko, D. Ringe, T. Fenn, 2004 .

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.

Karen N. Allen, G A Petsko, G. Petsko, 1995, Biochemistry.

X-ray crystallographic structures of D-xylose isomerase-substrate complexes position the substrate and provide evidence for metal movement during catalysis.

Karen N. Allen, G A Petsko, G. Petsko, 1994, Biochemistry.

Parkinson’s Disease and Melanoma: Co-Occurrence and Mechanisms

G. Petsko, D. Eliezer, A. Bose, 2018, Journal of Parkinson's disease.

An anion binding site in human aldose reductase: mechanistic implications for the binding of citrate, cacodylate, and glucose 6-phosphate.

G. Petsko, D. Ringe, D. Harrison, 1994, Biochemistry.

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.

G. Petsko, D. Ringe, D. Harrison, 1994, Biochemistry.

Crystallographic studies of the mechanism of xylose isomerase.

G A Petsko, G. Petsko, D. Ringe, 1989, Biochemistry.

Dimerization energetics of benzene and aromatic amino acid side chains

Stephen K. Burley, Gregory A. Petsko, G. Petsko, 1986 .

Structural Studies of a Cinchona Alkaloid Catalyst

G. Petsko, D. Ringe, S. Travis, 2013 .

The 2.1-A resolution structure of iron superoxide dismutase from Pseudomonas ovalis.

Barry L. Stoddard, Dagmar Ringe, Gregory A. Petsko, 1990, Biochemistry.

Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis.

G. Petsko, D. Ringe, D Ringe, 2001, Biochemistry.

Testing geometrical discrimination within an enzyme active site: constrained hydrogen bonding in the ketosteroid isomerase oxyanion hole.

Daniel Herschlag, Gregory A Petsko, Jose M M Caaveiro, 2008, Journal of the American Chemical Society.

POVScript+: a program for model and data visualization using persistence of vision ray-tracing

Dagmar Ringe, Gregory A. Petsko, Timothy D. Fenn, 2003 .

Grain of truth

Gregory A Petsko, G. Petsko, 2002, Genome Biology.

Amino‐aromatic interactions in proteins

G A Petsko, S K Burley, G. Petsko, 1986, FEBS letters.

Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase.

G. Petsko, D. Ringe, A. Danishefsky, 1991, Biochemistry.

The ubiquitous cofactor NADH protects against substrate‐induced inhibition of a pyridoxal enzyme

G. Petsko, D. Ringe, K. Soda, 1996, Protein science : a publication of the Protein Society.

Hydrogen bond coupling in the ketosteroid isomerase active site.

G. Petsko, D. Ringe, D. Herschlag, 2009, Biochemistry.

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

G. Petsko, J. Clifton, D. Ringe, 1999 .

Transnitrosylation from DJ-1 to PTEN Attenuates Neuronal Cell Death in Parkinson's Disease Models

G. Petsko, R. Liddington, S. Lipton, 2014, The Journal of Neuroscience.

Isotopic exchange plus substrate and inhibition kinetics of D-xylose isomerase do not support a proton-transfer mechanism.

Karen N. Allen, G. Petsko, D. Ringe, 1994, Biochemistry.

The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes.

G. Petsko, D. Ringe, M. Hasson, 1998, Biochemistry.

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.

Karen N. Allen, G. Petsko, D. Ringe, 1994, Biochemistry.

The 3.0 A crystal structure of xylose isomerase from Streptomyces olivochromogenes.

G. Petsko, D. Ringe, G. Farber, 1987, Protein engineering.

Xylose isomerase in substrate and inhibitor michaelis states: atomic resolution studies of a metal-mediated hydride shift.

G. Petsko, D. Ringe, T. Fenn, 2004, Biochemistry.

Probing the active center of benzaldehyde lyase with substitutions and the pseudosubstrate analogue benzoylphosphonic acid methyl ester.

G. Petsko, D. Ringe, G. L. Kenyon, 2008, Biochemistry.

Refined crystal structure of the triphosphate conformation of H‐ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis.

W. Kabsch, G. Petsko, E. Pai, 1990, The EMBO journal.

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

G L Kenyon, G A Petsko, G. Petsko, 1995, Biochemistry.

Control of oligomeric enzyme thermostability by protein engineering.

G. Petsko, A. Klibanov, J. Casal, 1987, Proceedings of the National Academy of Sciences of the United States of America.

X-ray cryoenzymology.

G. Petsko, A. Fink, 1981, Advances in enzymology and related areas of molecular biology.

Crystal Structures of Cystathionine β-Synthase from Saccharomyces cerevisiae: One Enzymatic Step at a Time.

Christopher D. McCune, G. Petsko, D. Ringe, 2018, Biochemistry.

Proteins at work: "stop-action" pictures at subzero temperatures.

G. Petsko, P. Douzou, 1984, Advances in protein chemistry.

Proton Magnetic Resonance Spectrum of Polywater

G. Petsko, 1970, Science.

Snapshot of a reaction intermediate: analysis of benzoylformate decarboxylase in complex with a benzoylphosphonate inhibitor.

G. Petsko, D. Ringe, G. L. Kenyon, 2009, Biochemistry.

Protein sequencing by computer graphics.

D Tsernoglou, G A Petsko, A T Tu, 1977, Biochimica et biophysica acta.

Life is a Ponzi scheme

G. Petsko, 2009, Genome Biology.

Personalized iPSC-Derived Dopamine Progenitor Cells for Parkinson's Disease.

G. Petsko, Quanzheng Li, B. Cohen, 2020, The New England journal of medicine.

Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition.

G. Petsko, D. Ringe, M. Kneen, 2010, Journal of the American Chemical Society.

Latrepirdine stimulates autophagy and reduces accumulation of α-synuclein in cells and in mouse brain

G. Petsko, D. Ringe, R. Martins, 2012, Molecular Psychiatry.

Structure determination of turkey egg-white lysozyme using Laue diffraction data.

G A Petsko, G. Petsko, J. Hajdu, 1992, Acta crystallographica. Section B, Structural science.

Crystal structure of the DNA binding domain of the transcription factor T-bet suggests simultaneous recognition of distant genome sites

G. Petsko, D. Ringe, J. Dekker, 2016, Proceedings of the National Academy of Sciences.

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

G. Petsko, V. Anderson, B. Bahnson, 2002, Biochemistry.

Misfolded Proteins Are Competent to Mediate a Subset of the Responses to Heat Shock in Saccharomyces cerevisiae * 210

G. Petsko, D. Botstein, C. Kao, 2002, The Journal of Biological Chemistry.

Amelioration of toxicity in neuronal models of amyotrophic lateral sclerosis by hUPF1

G. Petsko, D. Ringe, S. Finkbeiner, 2015, Proceedings of the National Academy of Sciences.

Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis.

G. Petsko, D. Ringe, D. A. Bosco, 2011, Cold Spring Harbor perspectives in biology.

A Yeast Model of FUS/TLS-Dependent Cytotoxicity

Daniel F Tardiff, G. Petsko, Robert H. Brown, 2011, PLoS biology.

Werner-washburne " Sleeping Beauty " : Quiescence in Saccharomyces Cerevisiae †

G. C. Johnston, G. Petsko, D. Ringe, 2022 .

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

Gregory A Petsko, Dagmar Ringe, G. Petsko, 2005, Journal of molecular biology.

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.

G. C. Johnston, G. Petsko, Hong Sun, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Too big to succeed?

Gregory A Petsko, G. Petsko, 2009, Genome Biology.

Active site analysis of the potential antimicrobial target aspartate semialdehyde dehydrogenase.

G. Petsko, D. Ringe, J. Ouyang, 2001, Biochemistry.

Retromer in Alzheimer disease, Parkinson disease and other neurological disorders

G. Petsko, S. Small, 2015, Nature Reviews Neuroscience.

Before you call the midwife

G. Petsko, Laurie H. Glimcher, 2022, Cell.

mGreenLantern: a bright monomeric fluorescent protein with rapid expression and cell filling properties for neuronal imaging

Mitchell H. Murdock, G. Petsko, H. Morishita, 2020, Proceedings of the National Academy of Sciences.

A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-γ-lactonase from Bacillus thuringiensis.

G. Petsko, D. Ringe, Ce-Feng Liu, 2013, Biochemistry.

Targeting α-synuclein for treatment of Parkinson's disease: mechanistic and therapeutic considerations

G. Petsko, E. Bézard, M. Vila, 2015, The Lancet Neurology.

Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution.

G. Petsko, J. Knowles, D. Ringe, 1994, Biochemistry.

Composition analysis of α-helices in thermophilic organisms

G. Petsko, G. Warren, 1995 .

Detection of ligand binding hot spots on protein surfaces via fragment-based methods: application to DJ-1 and glucocerebrosidase

Dima Kozakov, Ryan Brenke, Dmitri Beglov, 2009, J. Comput. Aided Mol. Des..

Catalytic ability and stability of two recombinant mutants of D‐amino acid transaminase involved in coenzyme binding

G. Petsko, D. Ringe, D. Peisach, 1995, Protein science : a publication of the Protein Society.

Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity.

G. Petsko, D. Ringe, K. Soda, 1995, Biochemistry.

Structure of iron superoxide dismutase from Pseudomonas ovalis at 2.9-A resolution.

G. Petsko, D. Ringe, K. Suzuki, 1983, Proceedings of the National Academy of Sciences of the United States of America.

Reducing C-terminal truncation mitigates synucleinopathy and neurodegeneration in a transgenic model of multiple system atrophy

G. Petsko, E. Bézard, D. Ringe, 2016, Proceedings of the National Academy of Sciences.

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

G A Petsko, G. Petsko, D. Ringe, 1999, Journal of molecular biology.

25-Hydroxycholesterol amplifies microglial IL-1β production in an apoE isoform-dependent manner

G. Petsko, D. Holtzman, S. Paul, 2020, Journal of Neuroinflammation.

Thermal expansion of a protein.

I. Kuntz, M. Karplus, G. Petsko, 1987, Biochemistry.

Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.

G. Petsko, D. Ringe, D. Peisach, 1998, Protein engineering.

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.

G. Petsko, B. Chait, D. Ringe, 1998, Biochemistry.

The co-crystal structure of ubiquitin carboxy-terminal hydrolase L1 (UCHL1) with a tripeptide fluoromethyl ketone (Z-VAE(OMe)-FMK).

G. Petsko, D. Ringe, H. Ploegh, 2012, Bioorganic & medicinal chemistry letters.

Déjá vu all over again

G. Petsko, 1991, Nature.

Structure of oxidized flavodoxin from Anacystis nidulans.

D Tsernoglou, G A Petsko, G. Petsko, 1983, Journal of molecular biology.

X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 A resolution.

M Karplus, J Kuriyan, G A Petsko, 1986, Journal of molecular biology.

The 1.20 A resolution crystal structure of the aminopeptidase from Aeromonas proteolytica complexed with tris: a tale of buffer inhibition.

G. Petsko, D. Ringe, W. Desmarais, 2002, Structure.

PLP and GABA trigger GabR-mediated transcription regulation in Bacillus subtilis via external aldimine formation

G. Petsko, D. Ringe, R. Wu, 2017, Proceedings of the National Academy of Sciences.

The neuronal retromer can regulate both neuronal and microglial phenotypes of Alzheimer’s disease

G. Petsko, D. Berman, S. Small, 2022, Cell reports.

Pharmacological chaperones stabilize retromer to limit APP processing.

G. Petsko, D. Ringe, D. Berman, 2014, Nature chemical biology.

Acquired resistance to IDH inhibition through trans or cis dimer-interface mutations

Steven K. Albanese, Ariën S. Rustenburg, G. Petsko, 2018, Nature.

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

G. Petsko, D. Ringe, E. Pozharski, 2005, Journal of molecular biology.

Acquired resistance to IDH inhibition through trans or cis dimer-interface mutations

Bo Wang, John D. Chodera, Steven K. Albanese, 2018, Nature.

Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability.

David W. Miller, G. Petsko, M. Cookson, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Atomic coordinates for triose phosphate isomerase from chicken muscle.

D W Banner, G A Petsko, G. Petsko, 1976, Biochemical and biophysical research communications.

Polyamine pathway contributes to the pathogenesis of Parkinson disease

G. Petsko, D. Ringe, K. Marder, 2010, Proceedings of the National Academy of Sciences.

The role of water in the catalytic efficiency of triosephosphate isomerase.

G A Petsko, G. Petsko, N. Xuong, 1999, Biochemistry.

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

G. Petsko, N. Xuong, D. Ringe, 1996, Biochemistry.

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.

G. Petsko, D. Ringe, E. Komives, 1995, Biochemistry.

Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95.

G. Petsko, J. Knowles, E. Komives, 1991, Biochemistry.

Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.

G A Petsko, G. Petsko, E Lolis, 1990, Biochemistry.

Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic base glutamic acid 165 is changed to aspartic acid.

G. Petsko, E. Komives, D. Joseph-McCarthy, 1994, Biochemistry.

PGE1 and PGA1 bind to Nurr1 and activate its transcriptional function

G. Petsko, K. Lim, H. Park, 2020, Nature Chemical Biology.

RETROMER REPLETION WITH AAV9-VPS35 RESTORES ENDOSOMAL FUNCTION IN THE MOUSE HIPPOCAMPUS

G. Petsko, D. Berman, S. Small, 2019, Alzheimer's & Dementia.

Stabilizing the Retromer Complex in a Human Stem Cell Model of Alzheimer’s Disease Reduces TAU Phosphorylation Independently of Amyloid Precursor Protein

G. Petsko, L. Goldstein, S. Small, 2018, Stem cell reports.

Going to the dogs

Gregory A Petsko, G. Petsko, 2008, Genome Biology.

Strange days

G. Petsko, 2007, Genome Biology.

When failure should be the option

Gregory A Petsko, G. Petsko, 2010, BMC Biology.

Studies of calmodulin structure: laser raman spectroscopy of biomolecules.

G. Petsko, B. Seaton, J. Head, 1983, Biochemistry.

A Topographic View of Supercooled Liquids and Glass Formation

B. F. Rasmussen, H. Frauenfelder, E. Mayer, 2005 .

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

P C Babbitt, G L Kenyon, G A Petsko, 1998, Proceedings of the National Academy of Sciences of the United States of America.

War and peace

Gregory A Petsko, G. Petsko, 2003, Genome Biology.

Subunit interface of triosephosphate isomerase: site-directed mutagenesis and characterization of the altered enzyme.

G A Petsko, G. Petsko, A. Klibanov, 1987, Biochemistry.

Solution of a Protein Crystal Structure with a Model Obtained from NMR Interproton Distance Restraints

M. Karplus, G. Petsko, A. Gronenborn, 1987, Science.

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.

G. Petsko, G. L. Kenyon, J. Gerlt, 1991, Biochemistry.

Crystal structure of elastase–substrate complex at −55 °C

G. Petsko, D. Tsernoglou, T. Alber, 1976, Nature.

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

G. Petsko, 2001, Methods in enzymology.

Crystal structure of rabbit phosphoglucose isomerase, a glycolytic enzyme that moonlights as neuroleukin, autocrine motility factor, and differentiation mediator.

G. Petsko, D. Ringe, C. Jeffery, 2000, Biochemistry.

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

G. Petsko, D. Ringe, C. Jeffery, 2000, Protein engineering.

Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317.

G. Petsko, J. Clifton, G. L. Kenyon, 1995, Biochemistry.

Protein crystallography at sub-zero temperatures: cryo-protective mother liquors for protein crystals.

G A Petsko, G. Petsko, 1975, Journal of molecular biology.

Brain-wide analysis of the supraspinal connectome reveals anatomical correlates to functional recovery after spinal injury

G. Petsko, Vatsal Mehra, Zimei Wang, 2022, eLife.

26-10 Fab-digoxin complex: affinity and specificity due to surface complementarity.

R L Campbell, G A Petsko, G. Petsko, 1993, Proceedings of the National Academy of Sciences of the United States of America.

The usual suspects

Gregory A Petsko, G. Petsko, 2003, Genome Biology.

Molecular mechanics modeling of oligonucleotide adducts of the antitumor drug cis‐diamminedichloroplatinum(II)

G. Petsko, G. Quigley, S. Lippard, 1987, Biopolymers.

Molecular mechanics calculations on cis ([Pt(NH3)2{d(GpG)}] adducts in two oligonucleotide duplexes

G. Petsko, G. Quigley, S. Lippard, 1985 .

Design by necessity

G. Petsko, 2001, Genome Biology.

Enzyme evolution: Design by necessity

G. Petsko, 2000, Nature.

Three-dimensional structure of murine anti-p-azophenylarsonate Fab 36-71. 2. Structural basis of hapten binding and idiotypy.

G. Petsko, M. N. Margolies, R. Strong, 1991, Biochemistry.

The x-ray structure of the periplasmic galactose binding protein from Salmonella typhimurium at 3.0-A resolution.

G. Petsko, S. Mowbray, 1983, The Journal of biological chemistry.

On the three-dimensional structure and catalytic mechanism of triose phosphate isomerase.

D W Banner, G A Petsko, G. Petsko, 1981, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis.

G. Petsko, D. Ringe, J. Stock, 1994, Biochemistry.

The life aquatic

G. Petsko, 2005, Genome Biology.

Structure of a eukaryotic thiaminase I

G. Petsko, D. Ringe, D. Hawksley, 2013, Proceedings of the National Academy of Sciences.

Direct structural observation of an acyl-enzyme intermediate in the hydrolysis of an ester substrate by elastase.

G A Petsko, G. Petsko, D. Ringe, 1994, Biochemistry.

Protein crosslinking as a therapeutic strategy for SOD1-related ALS

Jared R. Auclair, Joseph P. Salisbury, G. Petsko, 2021, bioRxiv.

Structure and mechanism of benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633, a member of the Class 3 aldehyde dehydrogenase superfamily

G. Petsko, D. Ringe, M. Kneen, 2017, Protein engineering, design & selection : PEDS.

Reaction of myoglobin with phenylhydrazine: a molecular doorstop.

D. E. Kerr, G. Petsko, D. Ringe, 1984, Biochemistry.

Computer simulation and analysis of the reaction pathway of triosephosphate isomerase.

M Karplus, G A Petsko, M. Karplus, 1991, Biochemistry.

On the protein crystal chemistry of chloroplatinite ions: general principles and interactions with triose phosphate isomerase.

G. Petsko, D. Phillips, I. Wilson, 1978, Journal of molecular biology.

Time-of-flight neutron diffraction study of bovine γ-chymotrypsin at the Protein Crystallography Station.

G. Petsko, D. Ringe, P. Langan, 2011, Acta crystallographica. Section F, Structural biology and crystallization communications.

Structural dynamics of liganded myoglobin.

H Frauenfelder, G A Petsko, G. Petsko, 1980, Biophysical journal.

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

G A Petsko, G. Petsko, D. Ringe, 1999, Biochemistry.

Cloning, sequencing, and expression in Escherichia coli of the gene encoding a 45-kilodalton protein, elongation factor Tu, from Chlamydia trachomatis serovar F

G. Petsko, Y. Shi, Y. Zhang, 1994, Journal of bacteriology.

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

G. Petsko, S. Shuto, A. Matsuda, 2003, Biochemistry.

Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site

G. Petsko, D. Ringe, D. Herschlag, 2013, Proceedings of the National Academy of Sciences.

Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium

G. Petsko, V. Kuchroo, E. Sundberg, 2021, Communications Biology.

Structural basis of the dynamic human CEACAM1 monomer-dimer equilibrium

G. Petsko, G. Wagner, V. Kuchroo, 2020, bioRxiv.

The father of us all

G. Petsko, 2002, Genome Biology.

When bubbles burst

G. Petsko, 2008, Genome Biology.

No stone unturned

Gregory A Petsko, G. Petsko, 2010, Genome Biology.

Goodbye, Columbus

G. Petsko, 2012, Genome Biology.

Defining the mandate of proteomics in the post-genomics era: workshop report.

Gerald M Rubin, Gregory A Petsko, Dagmar Ringe, 2002, Molecular & cellular proteomics : MCP.

Apocalypse now?

G. Petsko, 2012, Genome Biology.

Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase

G. Petsko, D. Ringe, C. Jeffery, 1998, Protein science : a publication of the Protein Society.

A Christmas Carol

Gregory A Petsko, G. Petsko, 2001, Genome Biology.

A structure of sperm whale myoglobin at a nitrogen gas pressure of 145 atmospheres.

G. Petsko, R. F. Tilton, 1988, Biochemistry.

Characterization of crystals of xylose isomerase from Streptomyces violaceoniger.

G. Petsko, D. Ringe, A. Glasfeld, 1988, Journal of Biological Chemistry.

The highs and lows of scientific conferences

Gregory A. Petsko, G. Petsko, 2006, Nature Reviews Molecular Cell Biology.

Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae.

G. Petsko, D. Ringe, J. Murphy, 1995, Proceedings of the National Academy of Sciences of the United States of America.

Crystallization and preliminary X-ray studies of the diphtheria Tox repressor from Corynebacterium diphtheriae.

G. Petsko, D. Ringe, J. Murphy, 1994, Journal of Molecular Biology.

Tsunami

G. Petsko, 2005, Genome Biology.

Analyzing Molecular Interactions

G. Petsko, J. Yates, 2003, Current protocols in bioinformatics.

Caspase-1 causes truncation and aggregation of the Parkinson’s disease-associated protein α-synuclein

David W. Miller, G. Petsko, M. Cookson, 2016, Proceedings of the National Academy of Sciences.

Banana republic

G. Petsko, 2002, Genome Biology.

Do the math

Gregory A Petsko, G. Petsko, 2006, Genome Biology.

Transition-state analogues in protein crystallography: probes of the structural source of enzyme catalysis.

G. Petsko, E. Lolis, 1990, Annual review of biochemistry.

Interaction of a peptidomimetic aminimide inhibitor with elastase.

G A Petsko, G. Petsko, D. Ringe, 1995, Science.

Preserving some sanity

G. Petsko, 2011, Genome Biology.

The next epidemic

G. Petsko, 2006, Genome Biology.

Mycobacterium tuberculosis Hip1 Modulates Macrophage Responses through Proteolysis of GroEL2

G. Petsko, D. Ringe, J. Rengarajan, 2014, PLoS pathogens.

Mycobacterium tuberculosis Hip 1 Modulates Macrophage Responses through Proteolysis of GroEL 2

G. Petsko, D. Ringe, J. Rengarajan, 2022 .

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.

G. Petsko, M. N. Margolies, R. Strong, 1991, Biochemistry.

Q&A: What are pharmacological chaperones and why are they interesting?

G. Petsko, D. Ringe, 2009, Journal of biology.

The Use of Pharmacological Retromer Chaperones in Alzheimer’s Disease and other Endosomal-related Disorders

G. Petsko, D. Ringe, D. Berman, 2014, Neurotherapeutics.

Dimerization of the Alzheimer’s disease pathogenic receptor SORLA regulates its association with retromer

G. Petsko, S. Small, E. Fazeli, 2023, Proceedings of the National Academy of Sciences of the United States of America.

Corrections - Cavities in Proteins: Structure of a Metmyoglobin-Xenon Complex Solved to 1.9

I. Kuntz, G. Petsko, R. F. Tilton, 1985 .

Apocalypse now?

G. Petsko, 2019, Genome Biology.

Analysis of two-residue turns in proteins.

M Karplus, G A Petsko, M. Karplus, 1994, Journal of molecular biology.

Design of apparatus and experiments to determine the effect of microgravity on the crystallization of biological macromolecules using the MIR spacestation

G. Petsko, B. Stoddard, A. Arrott, 1991 .

A preliminary neutron diffraction study of gamma-chymotrypsin.

G. Petsko, D. Ringe, I. Schlichting, 2009, Acta crystallographica. Section F, Structural biology and crystallization communications.

Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. I5 suggest reasons for thermal instability.

G A Petsko, G. Petsko, A. Szilágyi, 1997, Protein engineering.

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

G. Petsko, D. Ringe, 2000, Current opinion in chemical biology.

ENDOSOMAL TRAFFIC JAMS REPRESENT A PATHOGENIC HUB AND THERAPEUTIC TARGET IN ALZHEIMER’S DISEASE

G. Petsko, S. Small, Yasir H. Qureshi, 2019, Alzheimer's & Dementia.

Live and let diet

Gregory A Petsko, G. Petsko, 2003, Genome Biology.

A drop in the bucket

G. Petsko, 2004, Genome Biology.

Color blind

G. Petsko, 2004, Genome Biology.

Dominoes

Gregory A Petsko, G. Petsko, 2011, Genome Biology.

Do the math

G. Petsko, 2006, Genome Biology.

Brain-wide quantification of the supraspinal connectome

G. Petsko, Vatsal Mehra, Zimei Wang, 2021, bioRxiv.

Purification, crystallization and molecular symmetry of CDP-D-glucose 4,6-dehydratase from Yersinia pseudotuberculosis.

G. Petsko, D. Ringe, Hung‐wen Liu, 2002, Acta crystallographica. Section D, Biological crystallography.

Galactose mutarotase: pH dependence of enzymatic mutarotation.

G. Petsko, P. Frey, J. Clifton, 2003, Biochemistry.

Protein engineering of yeast triose phosphate isomerase

G. Petsko, A. Klibanov, J. Casal, 1987 .

An introduction to modeling structure from sequence.

Gregory A Petsko, G. Petsko, 2006, Current protocols in bioinformatics.

Cystic fibrosis. A transport problem?

G. Petsko, D. Ringe, 1990, Nature.

Crystal Structure of Green Fluorescent Protein Clover and Design of Clover-Based Redox Sensors.

G. Petsko, Ce-Feng Liu, B. C. Campbell, 2018, Structure.

Crystal structure of the K12M/G15A triosephosphate isomerase double mutant and electrostatic analysis of the active site.

G. Petsko, E. Komives, D. Joseph-McCarthy, 1994, Biochemistry.

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

G. Petsko, D. Ringe, T. Holyoak, 2004, Biochemistry.

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

G. Petsko, D. Ringe, R. Holz, 2007, Journal of inorganic biochemistry.

Immediate release of crystallographic data: a proposal.

A Wlodawer, D Davies, G Petsko, 1998, Science.

Endosomal Traffic Jams Represent a Pathogenic Hub and Therapeutic Target in Alzheimer’s Disease

G. Petsko, R. Mayeux, S. Small, 2017, Trends in Neurosciences.

The Parkinson's disease protein DJ-1 is neuroprotective due to cysteine-sulfinic acid-driven mitochondrial localization

David W. Miller, G. Petsko, Sourav Bandyopadhyay, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Reducing C-terminal truncation mitigates synucleinopathy and neurodegeneration in a transgenic model of multiple system atrophy

G. Petsko, E. Bézard, D. Ringe, 2016, Proceedings of the National Academy of Sciences.

Crystal structure of Bacillus subtilis GabR, an autorepressor and transcriptional activator of gabT

Todd A. Stone, G. Petsko, D. Ringe, 2013, Proceedings of the National Academy of Sciences.

And the second shall be first

Gregory A Petsko, G. Petsko, 2007, Genome Biology.

POVScript+: a program for model and data visualization using persistence of vision ray-tracing

G. Petsko, D. Ringe, T. Fenn, 2003 .

Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?

G. Petsko, D. Ringe, T. Alber, 1987, Cold Spring Harbor symposia on quantitative biology.

Chemistry and biology.

G. Petsko, 2000, Proceedings of the National Academy of Sciences of the United States of America.

A seat at the table

Gregory A Petsko, G. Petsko, 2008, Genome Biology.

2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor.

Gregory A Petsko, Dagmar Ringe, G. Petsko, 2003, Biochemistry.

How Enzymes Work

G. Petsko, D. Ringe, 2008, Science.

25‐Hydroxycholesterol amplifies microglial IL‐1beta production in an APOE isoform‐dependent manner

G. Petsko, D. Holtzman, Michael Lewis, 2020, Alzheimer's & Dementia.

Metal-Dependent Function of a Mammalian Acireductone Dioxygenase.

G. Petsko, D. Ringe, T. Pochapsky, 2016, Biochemistry.

Q&A: What are pharmacological chaperones and why are they interesting?

G. Petsko, Dagmar Ringe, 2009, Journal of biology.

7 – A Consumer’s Guide to Protein Crystallography

G. Petsko, D. Ringe, 1996 .

The system is broken

G. Petsko, 2006, Genome Biology.

Analyzing Molecular Interactions

G. Petsko, 2003, Current Protocols in Bioinformatics.

Dynamic Processes in Proteins by X-Ray Diffraction

G. Petsko, J. Hajdu, B. Stoddard, 1990 .

Preliminary X-ray data for the ribose binding protein from Salmonella typhimurium.

G. Petsko, S. Mowbray, 1982, Journal of molecular biology.

Spectroscopic and X-ray Crystallographic Characterization of Spectroscopic and X-ray Crystallographic Characterization of Bestatin Bound to the Aminopeptidase from Bestatin Bound to the Aminopeptidase from Aeromonas (Vibrio) proteolytica

G. Petsko, D. Ringe, R. Holz, 2022 .

The structure of iron superoxide dismutase from Pseudomonas ovalis complexed with the inhibitor azide.

G A Petsko, G. Petsko, B. Stoddard, 1990, Protein engineering.

Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site

G. Petsko, D. Ringe, D. Herschlag, 2013, Proceedings of the National Academy of Sciences.

Dual chemistry catalyzed by human acireductone dioxygenase

G. Petsko, D. Ringe, T. Pochapsky, 2017, Protein engineering, design & selection : PEDS.

Evaluating protein cross-linking as a therapeutic strategy to stabilize SOD1 variants in a mouse model of familial ALS

Jared R. Auclair, Joseph P. Salisbury, G. Petsko, 2024, PLoS biology.

Mass spectrometry tools for analysis of intermolecular interactions.

Jared R. Auclair, G. Petsko, D. Ringe, 2012, Methods in molecular biology.

Going to the dogs

G. Petsko, 2008, Genome Biology.

The Rosetta Stone

G. Petsko, 2001, Genome Biology.

A Christmas Carol

G. Petsko, 2001, Genome Biology.

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

G. Petsko, L. Hedstrom, Lu Gan, 2002, Biochemistry.

Big science, little science

G. Petsko, 2009, EMBO reports.