P. Karplus

发表

Mobile Manipulation and Mobility as Manipulation—Design and Algorithms of RoboSimian

Brian W. Satzinger, Jason I. Reid, J. Burdick, 2015, J. Field Robotics.

Conformation dependence of backbone geometry in proteins.

Roland L. Dunbrack, P. Karplus, M. Shapovalov, 2009, Structure.

Experimentally observed conformation‐dependent geometry and hidden strain in proteins

P. Karplus, 1996, Protein science : a publication of the Protein Society.

(φ,ψ)₂ motifs: a purely conformation-based fine-grained enumeration of protein parts at the two-residue level.

P. Karplus, Weng-Keen Wong, D. Berkholz, 2012, Journal of molecular biology.

Refined structure of porcine cytosolic adenylate kinase at 2.1 A resolution.

P. Karplus, G. Schulz, D. Dreusicke, 1988, Journal of molecular biology.

Crystal structures of two mutants that have implications for the folding of bovine pancreatic ribonuclease A

H. Scheraga, P. Karplus, R. Dodge, 1998, Protein science : a publication of the Protein Society.

Nonplanar peptide bonds in proteins are common and conserved but not biased toward active sites

Roland L. Dunbrack, P. Karplus, M. Shapovalov, 2011, Proceedings of the National Academy of Sciences.

Ordered water in macromolecular structure

P. Andrew Karplus, P. Karplus, C. Faerman, 1994 .

Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin.

R F Standaert, S. Schreiber, P. Karplus, 1993, Journal of molecular biology.

Preliminary crystallographic studies of urease from jack bean and from Klebsiella aerogenes.

P. Karplus, R. Hausinger, E. Jabri, 1992, Journal of molecular biology.

The crystal structure of urease from Klebsiella aerogenes.

P. Karplus, R. Hausinger, E. Jabri, 1995, Science.

Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants.

P. Karplus, E. Jabri, P A Karplus, 1996, Biochemistry.

ATOMIC-STRUCTURE OF THE BURIED CATALYTIC POCKET OF ESCHERICHIA-COLI CHORISMATE MUTASE.

P. Karplus, B. Ganem, J. Clardy, 1995 .

Peroxiredoxin Evolution and the Regulation of Hydrogen Peroxide Signaling

P. Karplus, Z. A. Wood, L. Poole, 2003, Science.

A fresh look at the Ramachandran plot and the occurrence of standard structures in proteins

P. Karplus, S. Hollingsworth, S. A. Hollingsworth, 2010, Biomolecular concepts.

Prediction of chain flexibility in proteins

P. Karplus, G. Schulz, 1985, Naturwissenschaften.

Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS.

P. Karplus, J. Tainer, E. Getzoff, 2007, Journal of molecular biology.

Cysteine pK(a) values for the bacterial peroxiredoxin AhpC.

P. Karplus, L. Poole, K. Nelson, 2008, Biochemistry.

ChSeq: A database of chameleon sequences

Lisa N Kinch, Nick V Grishin, P Andrew Karplus, 2015, Protein science : a publication of the Protein Society.

Linking Crystallographic Model and Data Quality

P. Andrew Karplus, Kay Diederichs, K. Diederichs, 2012, Science.

Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin.

P. Karplus, Z. A. Wood, L. Poole, 2005, Biochemistry.

Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization.

P Andrew Karplus, P. Karplus, L. Poole, 2010, Journal of molecular biology.

Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling.

P. Karplus, A. Perkins, L. Poole, 2015, Trends in biochemical sciences.

Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2

P. Karplus, R. Dobson, Christoph Göbl, 2021, The Journal of biological chemistry.

Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing.

P. Karplus, G. Ferrer-Sueta, A. Denicola, 2018, Biochemistry.

Experimentally Dissecting the Origins of Peroxiredoxin Catalysis.

Andrew E. Brereton, P. Karplus, F. Salsbury, 2017, Antioxidants & redox signaling.

A primer on peroxiredoxin biochemistry.

P. Karplus, P. Karplus, 2015, Free radical biology & medicine.

Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates.

P. Karplus, L. Poole, K. Nelson, 2013, Methods in enzymology.

Peroxiredoxins in parasites.

P. Karplus, M. Gretes, L. Poole, 2012, Antioxidants & redox signaling.

Mapping the active site helix-to-strand conversion of CxxxxC peroxiredoxin Q enzymes.

P Andrew Karplus, P. Karplus, A. Perkins, 2012, Biochemistry.

Conformational studies of the robust 2-Cys peroxiredoxin Salmonella typhimurium AhpC by solution phase hydrogen/deuterium (H/D) exchange monitored by electrospray ionization mass spectrometry.

P. Karplus, C. Maier, L. Poole, 2011, International journal of mass spectrometry.

Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds.

P. Karplus, D. Horita, L. Poole, 2009, Biochemistry.

Dimers to doughnuts: redox-sensitive oligomerization of 2-cysteine peroxiredoxins.

P. Karplus, Z. A. Wood, L. Poole, 2002, Biochemistry.

Tuning of Peroxiredoxin Catalysis for Various Physiological Roles

P. Karplus, A. Perkins, L. Poole, 2014, Biochemistry.

Evolutionary origin of a secondary structure: π-helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality.

P Andrew Karplus, P. Karplus, D. Arp, 2010, Journal of molecular biology.

Peroxiredoxins as molecular triage agents, sacrificing themselves to enhance cell survival during a peroxide attack.

P. Karplus, L. Poole, 2012, Molecular cell.

Better models by discarding data?

K. Diederichs, P. Karplus, 2013, Acta crystallographica. Section D, Biological crystallography.

A Novel Mechanism of Chemoprotection by Sulforaphane

P. Karplus, F. Chung, R. Dashwood, 2004, Cancer Research.

Inhibition of Histone Deacetylase A Novel Mechanism of Chemoprotection by Sulforaphane : Updated

P. Karplus, F. Chung, R. Dashwood, 2004 .

The crystal structure of urease from Klebsiella aerogenes.

Robert P. Hausinger, Evelyn Jabri, P. Karplus, 1995, Science.

Iron-containing urease in a pathogenic bacterium

E. L. Carter, P. Karplus, R. Hausinger, 2011, Proceedings of the National Academy of Sciences.

Inhibition of human glutathione reductase by the nitrosourea drugs 1,3-bis(2-chloroethyl)-1-nitrosourea and 1-(2-chloroethyl)-3-(2-hydroxyethyl)-1-nitrosourea. A crystallographic analysis.

P. Karplus, G. Schulz, R. Schirmer, 1988, European Journal of Biochemistry.

Structure of the Cdt1 C‐terminal domain: Conservation of the winged helix fold in replication licensing factors

P. Karplus, P. Güntert, Yunje Cho, 2009, Protein science : a publication of the Protein Society.

The mitotic kinesin-14 KlpA contains a context-dependent directionality switch

P. Karplus, X. Xiang, Weihong Qiu, 2016, Nature Communications.

The mitotic kinesin-14 KlpA contains a context-dependent directionality switch

P. Karplus, X. Xiang, Weihong Qiu, 2016, bioRxiv.

The Flavin Environment in Old Yellow Enzyme

P. Karplus, K. Fox, 1999, The Journal of Biological Chemistry.

Overcoming near-cognate suppression in a Release Factor 1-deficient host with an improved nitro-tyrosine tRNA synthetase.

P. Karplus, R. Mehl, P. Hosseinzadeh, 2020, Journal of molecular biology.

On the reliability of peptide nonplanarity seen in ultra‐high resolution crystal structures

Andrew E. Brereton, P. Karplus, Andrew E. Brereton, 2016, Protein science : a publication of the Protein Society.

Distal Phalanx Intermediate Phalanx Proximal Phalanx Haptic Classification and Faulty Sensor Compensation for a Robotic Hand

H. Stuart, P. Karplus, Habiya Beg, 2012 .

Structure and role for active site lid of lactate monooxygenase from Mycobacterium smegmatis

P. Karplus, K. M. Kean, K. Kean, 2018, Protein science : a publication of the Protein Society.

Structure of a Sedoheptulose 7-Phosphate Cyclase: ValA from Streptomyces hygroscopicus

P. Karplus, T. Mahmud, Shumpei Asamizu, 2014, Biochemistry.

The tumor suppressor merlin controls growth in its open state, and phosphorylation converts it to a less-active more-closed state.

P. Karplus, A. Bretscher, I. Sher, 2012, Developmental cell.

Structural, thermodynamic, and kinetic effects of a phosphomimetic mutation in dynein light chain LC8.

P. Karplus, E. Barbar, G. Benison, 2009, Biochemistry.

Crystal Structure of the Antioxidant Enzyme Glutathione Reductase Inactivated by Peroxynitrite*

P. Karplus, R. Schirmer, K. Becker, 2002, The Journal of Biological Chemistry.

Structural Basis of Improved Second-Generation 3-Nitro-tyrosine tRNA Synthetases

P. Karplus, C. Driggers, R. Mehl, 2014, Biochemistry.

Native proteins trap high-energy transit conformations

Andrew E. Brereton, P. Karplus, 2015, Science Advances.

The Arg-Gly-Asp-containing, solvent-exposed loop of Ptr ToxA is required for internalization.

P. Karplus, L. Ciuffetti, V. Manning, 2008, Molecular plant-microbe interactions : MPMI.

Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain.

P. Karplus, A. Bretscher, R. Fehon, 2007, Journal of molecular biology.

Gleaning Unexpected Fruits from Hard‐Won Synthetases: Probing Principles of Permissivity in Non‐canonical Amino Acid–tRNA Synthetases

P. Karplus, R. Mehl, R. Cooley, 2014, Chembiochem : a European journal of chemical biology.

A putative Fe2+-bound persulfenate intermediate in cysteine dioxygenase.

D. J. Schuller, P. Karplus, J. Dominy, 2008, Biochemistry.

Mammalian Cysteine Dioxygenase

P. Karplus, C. Driggers, M. Stipanuk, 2015 .

Structures of Arg‐ and Gln‐type bacterial cysteine dioxygenase homologs

P. Karplus, C. Driggers, S. Hartman, 2015, Protein science : a publication of the Protein Society.

Characterization of the Mononickel Metallocenter in H134A Mutant Urease*

P. Karplus, R. Hausinger, M. Pearson, 1996, The Journal of Biological Chemistry.

The Role of Glutamine 114 in Old Yellow Enzyme*

P. Karplus, V. Massey, B. J. Brown, 2002, The Journal of Biological Chemistry.

Low-resolution structure of recombinant human granulocyte-macrophage colony stimulating factor.

K. Diederichs, P. Karplus, T. Boone, 1991, Journal of molecular biology.

Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex

R F Standaert, P. Karplus, J. Clardy, 1991, Science.

Kinetic mechanism of l–α–glycerophosphate oxidase from Mycoplasma pneumoniae

P. Karplus, S. Maenpuen, P. Chaiyen, 2015, The FEBS journal.

AN ABSTRACT OF THE THESIS OF Justin T. Biel for the degree of Honors Baccalaureate of Science in Biochemistry and Biophysics presented on July 16 th , 2013. Title: Peptide Non-planarity Regained.

P. Karplus, J. Biel, Andrew Karplus, 2013 .

Crystallization and preliminary crystallographic analysis of the soluble alpha-glycerophosphate oxidase from Streptococcus sp.

P. Karplus, C. Finnerty, A. Claiborne, 2002, Acta crystallographica. Section D, Biological crystallography.

Biochemical and crystallographic characterization of ferredoxin-NADP(+) reductase from nonphotosynthetic tissues.

P. Karplus, C. Finnerty, A. Negri, 2001, Biochemistry.

Synthesis and characterization of photolabile o-nitrobenzyl derivatives of urea.

P. Karplus, E. Jabri, G. P. Hess, 2002, The Journal of organic chemistry.

Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution.

P. Karplus, T. Tsukihara, H. Sakai, 2006, Biochemistry.

Structure of the active FERM domain of Ezrin

P. Karplus, A. Bretscher, N. Nassar, 2003 .

Structure of the Active N-terminal Domain of Ezrin

P. Karplus, A. Bretscher, N. Nassar, 2003, The Journal of Biological Chemistry.

Involvement of serine 96 in the catalytic mechanism of ferredoxin-NADP+ reductase: structure--function relationship as studied by site-directed mutagenesis and X-ray crystallography.

P. Karplus, G. Zanetti, M. Vanoni, 1995, Biochemistry.

Structure‐function relations for old yellow enzyme

P. Karplus, V. Massey, K. Fox, 1995, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Beyond basins: φ,ψ preferences of a residue depend heavily on the φ,ψ values of its neighbors

P. Karplus, S. Hollingsworth, Matthew C Lewis, 2016, Protein science : a publication of the Protein Society.

HUMAN GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR

K. Diederichs, P. Karplus, T. Boone, 1996 .

Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris.

P. Karplus, X. Lei, Z. A. Wood, 2000, Archives of biochemistry and biophysics.

Ensemblator v3: Robust atom‐level comparative analyses and classification of protein structure ensembles

Andrew E. Brereton, P. Karplus, Andrew E. Brereton, 2018, Protein science : a publication of the Protein Society.

Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease.

P. Karplus, R. Hausinger, M. Pearson, 1997, Biochemistry.

Hydrophobicity regained: Hydrophobicity regained

P. Andrew Karplus, P. Karplus, 1997 .

Hydrophobicity regained.

P. Karplus, P A Karplus, 1997, Protein science : a publication of the Protein Society.

On the Active Site of Old Yellow Enzyme

P. Karplus, Z. Deng, V. Massey, 1998, The Journal of Biological Chemistry.

Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins.

P. Karplus, K. Fox, 1994, Structure.

Refined structure of glutathione reductase at 1.54 A resolution.

P. Karplus, G. Schulz, P A Karplus, 1987, Journal of molecular biology.

Kukoamine A and other hydrophobic acylpolyamines: potent and selective inhibitors of Crithidia fasciculata trypanothione reductase.

P. Karplus, B. Ganem, S. Savvides, 1995, The Biochemical journal.

De novo synthesis of a sunscreen compound in vertebrates

Robert L. Tanguay, P. Karplus, Garrett Holzwarth, 2015, eLife.

Oxidized and synchrotron cleaved structures of the disulfide redox center in the N‐terminal domain of Salmonella typhimurium AhpF

Blaine R. Roberts, P. Karplus, Z. A. Wood, 2005, Protein science : a publication of the Protein Society.

Protein sulfenic acids in redox signaling.

P. Karplus, L. Poole, A. Claiborne, 2004, Annual review of pharmacology and toxicology.

Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family.

P. Karplus, P A Karplus, J R Herriott, 1991, Science.

Probing the Roles of Active Site Residues in D-Xylose Isomerase (*)

H. L. Carrell, P. Karplus, C. Batt, 1995, The Journal of Biological Chemistry.

Perturbing the metal site in D-xylose isomerase. Effect of mutations of His-220 on enzyme stability.

H. L. Carrell, P. Karplus, C. Batt, 1994, The Journal of biological chemistry.

Catalytic cycle of human glutathione reductase near 1 A resolution.

P Andrew Karplus, Donald S Berkholz, P. Karplus, 2008, Journal of molecular biology.

Crystal structure of Escherichia coli SsuE: defining a general catalytic cycle for FMN reductases of the flavodoxin-like superfamily.

P. Karplus, C. Driggers, H. Ellis, 2014, Biochemistry.

Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase.

P. Karplus, G. Schulz, E. Pai, 1988, Biochemistry.

Improved R-factors for diffraction data analysis in macromolecular crystallography

P. Andrew Karplus, Kay Diederichs, K. Diederichs, 1997, Nature Structural Biology.

Novel fold and putative receptor binding site of granulocyte-macrophage colony-stimulating factor.

K. Diederichs, P. Karplus, T. Boone, 1991, Science.

Molecular Dynamics Studies of the Hydration of α,α-Trehalose

P. Karplus, J. Brady, Qiang Liu, 1997 .

Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution.

P. Karplus, G. Schulz, P A Karplus, 1994, Journal of molecular biology.

Refined crystal structure of spinach ferredoxin reductase at 1.7 A resolution: oxidized, reduced and 2'-phospho-5'-AMP bound states.

P. Karplus, P A Karplus, C M Bruns, 1995, Journal of molecular biology.

High‐resolution studies of hydride transfer in the ferredoxin:NADP+ reductase superfamily

P. Karplus, G. Zanetti, A. Hall, 2017, The FEBS journal.

Competition between C-terminal Tyrosine and Nicotinamide Modulates Pyridine Nucleotide Affinity and Specificity in Plant Ferredoxin-NADP+ Reductase*

P. Karplus, A. Arakaki, E. Ceccarelli, 2000, The Journal of Biological Chemistry.

A productive NADP+ binding mode of ferredoxin–NADP + reductase revealed by protein engineering and crystallographic studies

P. Karplus, A. Arakaki, E. Ceccarelli, 1999, Nature Structural Biology.

Probing the Function of the Invariant Glutamyl Residue 312 in Spinach Ferredoxin-NADP+ Reductase*

P. Karplus, G. Zanetti, Z. Deng, 1998, The Journal of Biological Chemistry.

Spinach Ferredoxin-NADP+ Reductase: Structure-Function Relationship as Studied by Site-Directed Mutagenesis

P. Karplus, G. Zanetti, F. Sternieri, 1995 .

Structure-function relations for ferredoxin reductase

P. Karplus, C. M. Bruns, 1994, Journal of bioenergetics and biomembranes.

Structural prototypes for an extended family of flavoprotein reductases: Comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin

P. Karplus, C. C. Correll, M. Ludwig, 1993, Protein science : a publication of the Protein Society.

Typical 2‐Cys peroxiredoxins – structures, mechanisms and functions

P. Karplus, L. Poole, A. Hall, 2009, The FEBS journal.

Evolution and Distribution of C7-Cyclitol Synthases in Prokaryotes and Eukaryotes.

P. Karplus, T. Mahmud, Shumpei Asamizu, 2017, ACS chemical biology.

Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose.

M. Himmel, P. Karplus, W. Adney, 1996, Biochemistry.

Structure and mechanism of endo/exocellulase E4 from Thermomonospora fusca

P. Karplus, D. Irwin, D. Wilson, 1997, Nature Structural Biology.

P Andrew Karplus, George F Rohrmann, P. Karplus, 2001, BMC Evolutionary Biology.

Self-masking in an Intact ERM-merlin Protein: An Active Role for the Central α-Helical Domain

P. Karplus, A. Bretscher, R. Fehon, 2007 .

Structure of the ERM Protein Moesin Reveals the FERM Domain Fold Masked by an Extended Actin Binding Tail Domain

P. Karplus, A. Bretscher, M. Pearson, 2000, Cell.

Amino acid sequence of spinach ferredoxin:NADP+ oxidoreductase.

P. Karplus, K. Walsh, J. Herriott, 1984, Biochemistry.

The interplay of ligand binding and quaternary structure in the diverse interactions of dynein light chain LC8.

P. Karplus, E. Barbar, G. Benison, 2008, Journal of molecular biology.

Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: implications for flavin-linked sulfur trafficking.

P. Karplus, C. Furdui, D. Parsonage, 2009, Biochemistry.

Hematopoietic growth factors: understanding functional diversity in structural terms.

P. Karplus, K. Kaushansky, 1993, Blood.

Refined crystal structure and mutagenesis of human granulocyte‐macrophage colony‐stimulating factor

K. Diederichs, P. Karplus, T. Boone, 1996, Proteins.

Structure-based Insights into the Catalytic Power and Conformational Dexterity of Peroxiredoxins

P Andrew Karplus, P. Karplus, L. Poole, 2022 .

Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics

P. Karplus, G. W. Buchko, A. Perkins, 2016, Biomolecular NMR assignments.

A forward-looking suggestion for resolving the stereochemical restraints debate: ideal geometry functions.

Roland L Dunbrack, Roland L. Dunbrack, P Andrew Karplus, 2008, Acta crystallographica. Section D, Biological crystallography.

Structure and dynamics of LC8 complexes with KXTQT-motif peptides: swallow and dynein intermediate chain compete for a common site.

P. Karplus, E. Barbar, G. Benison, 2007, Journal of molecular biology.

Characterization of Sulfoxygenation and Structural Implications of Human Flavin-Containing Monooxygenase Isoform 2 (FMO2.1) Variants S195L and N413K

David E. Williams, P. Karplus, A. Benninghoff, 2009, Drug Metabolism and Disposition.

Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity.

P. Karplus, A. Claiborne, T. Mallett, 2008, Biochemistry.

Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin

P. Karplus, L. Poole, D. Parsonage, 2008, Proceedings of the National Academy of Sciences.

A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution.

P. Karplus, G. Schulz, E. Pai, 1989, European journal of biochemistry.

Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers

P. Karplus, R. Schirmer, K. Becker, 1998, Nature Structural Biology.

AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low Mr thioredoxin reductase.

P. Karplus, Z. A. Wood, L. Poole, 2000, European journal of biochemistry.

Assessing and maximizing data quality in macromolecular crystallography.

Kay Diederichs, P Andrew Karplus, K. Diederichs, 2015, Current opinion in structural biology.

Roles of the Catalytic Domain and Two Cellulose Binding Domains of Thermomonospora fusca E4 in Cellulose Hydrolysis

Shenmin Zhang, P. Karplus, D. Irwin, 1998, Journal of bacteriology.

Identification and Characterization of Bacterial Cysteine Dioxygenases: a New Route of Cysteine Degradation for Eubacteria

P. Karplus, J. Dominy, M. Stipanuk, 2006, Journal of bacteriology.

Structural survey of the peroxiredoxins.

P Andrew Karplus, P. Karplus, A. Hall, 2007, Sub-cellular biochemistry.

Sulfenic Acids and Peroxiredoxins in Oxidant Defense and Signaling

P. Karplus, L. Poole, K. Nelson, 2013 .

On the occurrence of linear groups in proteins

P Andrew Karplus, Donald S Berkholz, P. Karplus, 2009, Protein science : a publication of the Protein Society.

The insect immune protein scolexin is a novel serine proteinase homolog

P. Karplus, C. Finnerty, R. Granados, 2008, Protein science : a publication of the Protein Society.

Structure of Ptr ToxA: An RGD-Containing Host-Selective Toxin from Pyrenophora tritici-repentisw⃞

P. Karplus, L. Ciuffetti, V. Manning, 2005, The Plant Cell Online.

Crystal Structure of Mammalian Cysteine Dioxygenase

P. Karplus, Qun Liu, Q. Hao, 2006, Journal of Biological Chemistry.

Native state fluctuations in a peroxiredoxin active site match motions needed for catalysis.

P. Karplus, L. Poole, P. Reardon, 2021, Structure.

Cysteine-based Redox Switches in Enzymes

P. Karplus, L. Poole, Chananat Klomsiri, 2022 .

Charge is the major discriminating factor for glutathione reductase versus trypanothione reductase inhibitors.

P. Karplus, B. Ganem, S. Savvides, 1996, Bioorganic & medicinal chemistry.

Using a conformation-dependent stereochemical library improves crystallographic refinement of proteins.

Dale E Tronrud, P Andrew Karplus, Donald S Berkholz, 2010, Acta crystallographica. Section D, Biological crystallography.

Backbone makes a significant contribution to the electrostatics of α/β‐barrel proteins

P. Karplus, D. Ripoll, C. Faerman, 1997, Protein science : a publication of the Protein Society.

Structural changes common to catalysis in the Tpx peroxiredoxin subfamily.

P. Karplus, B. Sankaran, L. Poole, 2009, Journal of molecular biology.

Trypanocidal bisbenzylisoquinoline alkaloids are inhibitors of trypanothione reductase.

A. Rojas de Arias, P. Karplus, C. Faerman, 1998, Journal of enzyme inhibition.

Structural comparisons among the short-chain helical cytokines.

A Wlodawer, A M Gronenborn, G M Clore, 1994, Structure.

Isolation of Legume Glycosyltransferases and Active Site Mapping of the Phaseolus lunatus Zeatin O-glucosyltransferase ZOG1

P. Karplus, X. Shan, Ruth C. Martin, 2008, Journal of Plant Growth Regulation.

Insulin antagonism: a novel role for human serum transferrin.

P. Karplus, C. Faerman, S. Bazaes, 1998, Hormone and metabolic research = Hormon- und Stoffwechselforschung = Hormones et metabolisme.

Cysteine dioxygenase structures from pH4 to 9: consistent cys-persulfenate formation at intermediate pH and a Cys-bound enzyme at higher pH.

P. Karplus, B. Sankaran, C. Driggers, 2013, Journal of molecular biology.

A new default restraint library for the protein backbone in Phenix: a conformation-dependent geometry goes mainstream

Dale E Tronrud, Paul D Adams, Nigel W Moriarty, 2016, Acta crystallographica. Section D, Structural biology.

The Crystal Structure of Dynein Intermediate Chain-Light Chain Roadblock Complex Gives New Insights into Dynein Assembly*

P. Karplus, E. Barbar, Yujuan Song, 2010, The Journal of Biological Chemistry.

Multivalency in the Assembly of Intrinsically Disordered Dynein Intermediate Chain*

Elisar Barbar, P Andrew Karplus, Justin Hall, 2009, The Journal of Biological Chemistry.

Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots

P. Andrew Karplus, Tom Boone, P. Karplus, 2000, Nature Structural Biology.

The sensitive balance between the fully folded and locally unfolded conformations of a model peroxiredoxin.

P. Karplus, A. Perkins, L. Poole, 2013, Biochemistry.

In-house sulfur SAD phasing: a case study of the effects of data quality and resolution cutoffs.

P. Karplus, G. Sarma, 2006, Acta crystallographica. Section D, Biological crystallography.

Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics

P. Karplus, G. W. Buchko, A. Perkins, 2015, Biomolecular NMR Assignments.

Consensus preferred hydration sites in six FKBP12‐drug complexes

P. Karplus, C. Faerman, P A Karplus, 1995, Proteins.

Site-specific dual encoding and labeling of proteins via genetic code expansion.

P. Karplus, R. Mehl, Riley M. Bednar, 2023, Cell chemical biology.

Structure-Based Insights into the Role of the Cys-Tyr Crosslink and Inhibitor Recognition by Mammalian Cysteine Dioxygenase.

P. Karplus, C. Driggers, M. Stipanuk, 2016, Journal of molecular biology.

Immobilization of Proteins with Controlled Load and Orientation.

P. Karplus, R. Mehl, J. Baio, 2019, ACS applied materials & interfaces.

Data Processing: How Good Are My Data Really ?

K. Diederichs, P. Karplus, 2013 .

C-Terminal truncation of rabbit flavin-containing monooxygenase isoform 2 enhances solubility.

David E. Williams, P. Karplus, C. Pereira, 2006, Archives of biochemistry and biophysics.

Rationally engineered flavin‐dependent oxidase reveals steric control of dioxygen reduction

P. Karplus, C. Schofield, P. Macheroux, 2015, The FEBS journal.

The sedoheptulose 7-phosphate cyclases and their emerging roles in biology and ecology.

P. Karplus, T. Mahmud, K. M. Kean, 2017, Natural product reports.

Structure and proposed mechanism of l‐α‐glycerophosphate oxidase from Mycoplasma pneumoniae

P. Karplus, S. Maenpuen, P. Chaiyen, 2015, The FEBS journal.

Crystal structure of the catalytic domain of a thermophilic endocellulase.

P. Karplus, D. Wilson, M. Spezio, 1993, Biochemistry.

Autonomous Synthesis of Functional, Permanently Phosphorylated Proteins for Defining the Interactome of Monomeric 14-3-3ζ

P. Karplus, R. Mehl, N. Sluchanko, 2023, ACS central science.

PermaPhosSer: autonomous synthesis of functional, permanently phosphorylated proteins

P. Karplus, R. Mehl, J. Beckman, 2021, bioRxiv : the preprint server for biology.

Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots.

P. Karplus, S. Savvides, T. Boone, 2000 .

Structure of alpha-glycerophosphate oxidase from Streptococcus sp.: a template for the mitochondrial alpha-glycerophosphate dehydrogenase.

P. Karplus, D. Parsonage, A. Claiborne, 2008, Biochemistry.

Glutathione reductase of the malarial parasite Plasmodium falciparum: crystal structure and inhibitor development.

P. Karplus, R. Schirmer, K. Becker, 2003, Journal of molecular biology.

Structural Aspects of Plant Ferredoxin : NADP+ Oxidoreductases

P. Karplus, H. R. Faber, P. Karplus, 2004, Photosynthesis Research.

Kinetics and Crystallographic Analysis of Human Glutathione Reductase in Complex with a Xanthene Inhibitor (*)

P. Karplus, S. Savvides, 1996, The Journal of Biological Chemistry.

Kinetic and structural characterization of urease active site variants.

P. Karplus, R. Hausinger, M. Pearson, 2000, Biochemistry.

Characterization of metal-substituted Klebsiella aerogenes urease

P. Karplus, R. Hausinger, M. Pearson, 1999, JBIC Journal of Biological Inorganic Chemistry.

Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand.

P. Karplus, R. Hausinger, M. Pearson, 1998, Biochemistry.

Peroxiredoxin Catalysis at Atomic Resolution.

P. Karplus, A. Perkins, L. Poole, 2016, Structure.

Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC.

P. Karplus, G. Ferrer-Sueta, C. Furdui, 2015, Biochemistry.

Crystal structure of a novel Plasmodium falciparum 1-Cys peroxiredoxin.

P. Karplus, C. Nickel, S. Rahlfs, 2005, Journal of molecular biology.

The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain

P. Karplus, A. Bretscher, C. Finnerty, 2004, Journal of Cell Science.

Substrate Specificity in Thiol Dioxygenases.

P. Karplus, C. G. Davies, G. Jameson, 2019, Biochemistry.

A conformation-dependent stereochemical library improves crystallographic refinement even at atomic resolution.

Dale E Tronrud, P Andrew Karplus, P. Karplus, 2011, Acta crystallographica. Section D, Biological crystallography.

Creating a Selective Nanobody Against 3-Nitrotyrosine Containing Proteins

P. Karplus, R. Mehl, D. Mourich, 2022, Frontiers in Chemistry.

NMR structure of the HIV-1 reverse transcriptase thumb subdomain

Andrew E. Brereton, P. Karplus, A. Gronenborn, 2016, Journal of biomolecular NMR.

Automated NMR resonance assignments and structure determination using a minimal set of 4D spectra

P. Andrew Karplus, Andrew E. Brereton, Nikolaos G. Sgourakis, 2018, Nature Communications.

Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry

Peter B. Krenesky, P. Karplus, D. Berkholz, 2009, Nucleic Acids Res..

Generating Efficient Methanomethylophilus alvus Pyrrolysyl-tRNA Synthetases for Structurally Diverse Non-Canonical Amino Acids.

P. Karplus, J. Perona, R. Mehl, 2022, ACS chemical biology.

The tumor suppressor merlin controls growth in its open state and is converted by phosphorylation to a less-active more- closed state

P. Karplus, A. Bretscher, I. Sher, 2013 .

70 Years of Crystalline Urease: What Have We Learned?

P. Karplus, R. Hausinger, M. Pearson, 1997 .

Thiol dioxygenases: unique families of cupin proteins

P. Karplus, J. Dominy, M. Stipanuk, 2011, Amino Acids.

REFINED STRUCTURE OF GLUTATHIONE REDUCTASE AT 1.54 ANGSTROMS RESOLUTION

P. Karplus, G. Schulz, 1988 .

STRUCTURE/FUNCTION OF SPINACH FERREDOXIN:NADP+ OXIDOREDUCTASE

P. Karplus, 1991 .

Structural insights into a thermostable variant of human carbonic anhydrase II

P. Karplus, Joseph J. Porter, R. Mehl, 2018, Protein science : a publication of the Protein Society.

Conformation‐dependent backbone geometry restraints set a new standard for protein crystallographic refinement

P. Karplus, P. Adams, D. Tronrud, 2014, The FEBS journal.

Crystallization of Old Yellow Enzyme illustrates an effective strategy for increasing protein crystal size.

P. Karplus, K. Fox, 1993, Journal of Molecular Biology.

Nanobody assemblies with fully flexible topology enabled by genetically encoded tetrazine amino acids

P. Karplus, R. Mehl, S. Jana, 2022, Science advances.

Typical 2‐Cys peroxiredoxins – structures, mechanisms and functions

P. Karplus, L. Poole, A. Hall, 2009, The FEBS journal.

A structural foundation for studying chlamydial polymorphic membrane proteins

P. Karplus, D. Rockey, Abigail M. Debrine, 2023, Microbiology spectrum.

Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: implications for flavin-linked sulfur trafficking.

P. Karplus, C. Furdui, D. Parsonage, 2009, Biochemistry.

Observed octameric assembly of a Plasmodium yoelii peroxiredoxin can be explained by the replacement of native “ball‐and‐socket” interacting residues by an affinity tag

P. Karplus, M. Gretes, 2013, Protein Science.

Native state fluctuations in a peroxiredoxin active site match motions needed for catalysis.

P. Karplus, L. Poole, P. Reardon, 2021, Structure.

Cysteine-based redox switches in enzymes.

P. Karplus, L. Poole, Chananat Klomsiri, 2011, Antioxidants & redox signaling.

Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity.

P. Karplus, A. Claiborne, C. Paige, 2008, Biochemistry.

Structures of Methanomethylophilus alvus Pyrrolysine tRNA-Synthetases Support the Need for De Novo Selections When Altering the Substrate Specificity.

P. Karplus, J. Perona, R. Mehl, 2022, ACS chemical biology.

Overexpression of Crithidia fasciculata trypanothione reductase and crystallization using a novel geometry.

R. Puchalski, P. Karplus, S. Savvides, 1995, Acta crystallographica. Section D, Biological crystallography.