| Year |
Citation |
Score |
| 2023 |
Debrine AM, Karplus PA, Rockey DD. A structural foundation for studying chlamydial polymorphic membrane proteins. Microbiology Spectrum. e0324223. PMID 37882824 DOI: 10.1128/spectrum.03242-23 |
0.31 |
|
| 2022 |
Gottfried-Lee I, Perona JJ, Karplus PA, Mehl RA, Cooley RB. Structures of Pyrrolysine tRNA-Synthetases Support the Need for De Novo Selections When Altering the Substrate Specificity. Acs Chemical Biology. PMID 36395426 DOI: 10.1021/acschembio.2c00640 |
0.355 |
|
| 2019 |
Aloi S, Davies CG, Karplus PA, Wilbanks SM, Jameson GNL. Substrate Specificity in Thiol Dioxygenases. Biochemistry. 58: 2398-2407. PMID 31045343 DOI: 10.1021/acs.biochem.9b00079 |
0.332 |
|
| 2019 |
Kean KM, Karplus PA. Structure and role for active site lid of lactate monooxygenase from Mycobacterium smegmatis. Protein Science : a Publication of the Protein Society. 28: 135-149. PMID 30207005 DOI: 10.1002/pro.3506 |
0.311 |
|
| 2017 |
Nelson KJ, Perkins A, Van Swearingen AE, Hartman S, Brereton AE, Parsonage D, Salsbury FR, Karplus PA, Poole LB. Experimentally Dissecting the Origins of Peroxiredoxin Catalysis. Antioxidants & Redox Signaling. PMID 28375740 DOI: 10.1089/Ars.2016.6922 |
0.774 |
|
| 2017 |
Osborn AR, Kean KM, Alseud KM, Almabruk KH, Asamizu S, Lee JA, Karplus PA, Mahmud T. Evolution and Distribution of C7-Cyclitol Synthases in Prokaryotes and Eukaryotes. Acs Chemical Biology. PMID 28182402 DOI: 10.1021/Acschembio.7B00066 |
0.306 |
|
| 2016 |
Perkins A, Parsonage D, Nelson KJ, Ogba OM, Cheong PH, Poole LB, Karplus PA. Peroxiredoxin Catalysis at Atomic Resolution. Structure (London, England : 1993). PMID 27594682 DOI: 10.1016/J.Str.2016.07.012 |
0.778 |
|
| 2016 |
Driggers CM, Kean KM, Hirschberger LL, Cooley RB, Stipanuk MH, Karplus PA. Structure-based insights into the role of the Cys-Tyr crosslink and inhibitor-recognition by Mammalian Cysteine Dioxygenase. Journal of Molecular Biology. PMID 27477048 DOI: 10.1016/J.Jmb.2016.07.012 |
0.353 |
|
| 2016 |
Hollingsworth SA, Lewis MC, Karplus PA. Beyond basins: φ,ψ preferences of a residue depend heavily on the φ,ψ values of its neighbors. Protein Science : a Publication of the Protein Society. PMID 27342939 DOI: 10.1002/pro.2973 |
0.362 |
|
| 2016 |
Brereton AE, Karplus PA. On the reliability of peptide non-planarity seen in ultra-high resolution crystal structures. Protein Science : a Publication of the Protein Society. PMID 26779991 DOI: 10.1002/pro.2883 |
0.313 |
|
| 2015 |
Buchko GW, Perkins A, Parsonage D, Poole LB, Karplus PA. Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics. Biomolecular Nmr Assignments. PMID 26438558 DOI: 10.1007/S12104-015-9637-8 |
0.733 |
|
| 2015 |
Perkins A, Nelson KJ, Parsonage D, Poole LB, Karplus PA. Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling. Trends in Biochemical Sciences. 40: 435-45. PMID 26067716 DOI: 10.1016/J.Tibs.2015.05.001 |
0.77 |
|
| 2015 |
Li W, Kinch LN, Karplus PA, Grishin NV. ChSeq: A database of chameleon sequences. Protein Science : a Publication of the Protein Society. 24: 1075-86. PMID 25970262 DOI: 10.1002/Pro.2689 |
0.304 |
|
| 2015 |
Elkhal CK, Kean KM, Parsonage D, Maenpuen S, Chaiyen P, Claiborne A, Karplus PA. Structure and proposed mechanism of L-α-glycerophosphate oxidase from Mycoplasma pneumoniae. The Febs Journal. 282: 3030-42. PMID 25688572 DOI: 10.1111/Febs.13233 |
0.345 |
|
| 2015 |
Parsonage D, Nelson KJ, Ferrer-Sueta G, Alley S, Karplus PA, Furdui CM, Poole LB. Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC. Biochemistry. 54: 1567-75. PMID 25633283 DOI: 10.1021/Bi501515W |
0.303 |
|
| 2015 |
Zafred D, Steiner B, Teufelberger AR, Hromic A, Karplus PA, Schofield CJ, Wallner S, Macheroux P. Rationally engineered flavin-dependent oxidase reveals steric control of dioxygen reduction. The Febs Journal. PMID 25619330 DOI: 10.1111/Febs.13212 |
0.337 |
|
| 2015 |
Driggers CM, Hartman SJ, Karplus PA. Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs. Protein Science : a Publication of the Protein Society. 24: 154-61. PMID 25307852 DOI: 10.1002/pro.2587 |
0.361 |
|
| 2014 |
Perkins A, Poole LB, Karplus PA. Tuning of peroxiredoxin catalysis for various physiological roles. Biochemistry. 53: 7693-705. PMID 25403613 DOI: 10.1021/Bi5013222 |
0.764 |
|
| 2014 |
Moriarty NW, Tronrud DE, Adams PD, Karplus PA. Conformation-dependent backbone geometry restraints set a new standard for protein crystallographic refinement. The Febs Journal. 281: 4061-71. PMID 24890778 DOI: 10.1111/febs.12860 |
0.362 |
|
| 2014 |
Kean KM, Codding SJ, Asamizu S, Mahmud T, Karplus PA. Structure of a sedoheptulose 7-phosphate cyclase: ValA from streptomyces hygroscopicus Biochemistry. 53: 4250-4260. PMID 24832673 DOI: 10.1021/Bi5003508 |
0.395 |
|
| 2014 |
Driggers CM, Dayal PV, Ellis HR, Karplus PA. Crystal structure of Escherichia coli SsuE: defining a general catalytic cycle for FMN reductases of the flavodoxin-like superfamily. Biochemistry. 53: 3509-19. PMID 24816272 DOI: 10.1021/bi500314f |
0.381 |
|
| 2014 |
Perkins A, Poole LB, Karplus PA. Tuning of peroxiredoxin catalysis for various physiological roles Biochemistry. 53: 7693-7705. DOI: 10.1021/bi5013222 |
0.714 |
|
| 2014 |
Kean KM, Codding SJ, Asamizu S, Mahmud T, Karplus PA. Correction to Structure of a Sedoheptulose 7-Phosphate Cyclase: ValA from Streptomyces hygroscopicus Biochemistry. 53: 4316-4316. DOI: 10.1021/Bi5007496 |
0.329 |
|
| 2013 |
Perkins A, Nelson KJ, Williams JR, Parsonage D, Poole LB, Karplus PA. The sensitive balance between the fully folded and locally unfolded conformations of a model peroxiredoxin. Biochemistry. 52: 8708-21. PMID 24175952 DOI: 10.1021/Bi4011573 |
0.797 |
|
| 2013 |
Gretes MC, Karplus PA. 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. Protein Science : a Publication of the Protein Society. 22: 1445-52. PMID 23934758 DOI: 10.1002/pro.2328 |
0.37 |
|
| 2013 |
Driggers CM, Cooley RB, Sankaran B, Hirschberger LL, Stipanuk MH, Karplus PA. Cysteine dioxygenase structures from pH4 to 9: consistent cys-persulfenate formation at intermediate pH and a Cys-bound enzyme at higher pH. Journal of Molecular Biology. 425: 3121-36. PMID 23747973 DOI: 10.1016/J.Jmb.2013.05.028 |
0.305 |
|
| 2012 |
Perkins A, Gretes MC, Nelson KJ, Poole LB, Karplus PA. Mapping the active site helix-to-strand conversion of CxxxxC peroxiredoxin Q enzymes. Biochemistry. 51: 7638-50. PMID 22928725 DOI: 10.1021/Bi301017S |
0.806 |
|
| 2012 |
Berkholz DS, Driggers CM, Shapovalov MV, Dunbrack RL, Karplus PA. Nonplanar peptide bonds in proteins are common and conserved but not biased toward active sites. Proceedings of the National Academy of Sciences of the United States of America. 109: 449-53. PMID 22198840 DOI: 10.1073/Pnas.1107115108 |
0.8 |
|
| 2012 |
Hollingsworth SA, Lewis MC, Berkholz DS, Wong WK, Karplus PA. (φ,ψ)₂ motifs: a purely conformation-based fine-grained enumeration of protein parts at the two-residue level. Journal of Molecular Biology. 416: 78-93. PMID 22198294 DOI: 10.1016/J.Jmb.2011.12.022 |
0.803 |
|
| 2011 |
Cooley RB, Arp DJ, Karplus PA. Symerythrin structures at atomic resolution and the origins of rubrerythrins and the ferritin-like superfamily. Journal of Molecular Biology. 413: 177-94. PMID 21872605 DOI: 10.1016/J.Jmb.2011.08.019 |
0.38 |
|
| 2011 |
Nirudodhi S, Parsonage D, Karplus PA, Poole LB, Maier CS. 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. International Journal of Mass Spectrometry. 302: 93-100. PMID 21516234 DOI: 10.1016/J.Ijms.2010.08.018 |
0.323 |
|
| 2011 |
Hall A, Nelson K, Poole LB, Karplus PA. Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins. Antioxidants & Redox Signaling. 15: 795-815. PMID 20969484 DOI: 10.1089/Ars.2010.3624 |
0.364 |
|
| 2011 |
Stipanuk MH, Simmons CR, Karplus PA, Dominy JE. Thiol dioxygenases: unique families of cupin proteins. Amino Acids. 41: 91-102. PMID 20195658 DOI: 10.1007/S00726-010-0518-2 |
0.369 |
|
| 2010 |
Hollingsworth SA, Karplus PA. A fresh look at the Ramachandran plot and the occurrence of standard structures in proteins. Biomolecular Concepts. 1: 271-283. PMID 21436958 DOI: 10.1515/BMC.2010.022 |
0.335 |
|
| 2010 |
Cooley RB, Arp DJ, Karplus PA. Evolutionary origin of a secondary structure: π-helices as cryptic but widespread insertional variations of α-helices that enhance protein functionality. Journal of Molecular Biology. 404: 232-46. PMID 20888342 DOI: 10.1016/J.Jmb.2010.09.034 |
0.321 |
|
| 2010 |
Hall A, Parsonage D, Poole LB, Karplus PA. Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization. Journal of Molecular Biology. 402: 194-209. PMID 20643143 DOI: 10.1016/J.Jmb.2010.07.022 |
0.313 |
|
| 2010 |
Tronrud DE, Berkholz DS, Karplus PA. Using a conformation-dependent stereochemical library improves crystallographic refinement of proteins. Acta Crystallographica. Section D, Biological Crystallography. 66: 834-42. PMID 20606264 DOI: 10.1107/S0907444910019207 |
0.799 |
|
| 2010 |
Berkholz DS, Krenesky PB, Davidson JR, Karplus PA. Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry. Nucleic Acids Research. 38: D320-5. PMID 19906726 DOI: 10.1093/Nar/Gkp1013 |
0.794 |
|
| 2009 |
Berkholz DS, Shapovalov MV, Dunbrack RL, Karplus PA. Conformation dependence of backbone geometry in proteins. Structure (London, England : 1993). 17: 1316-25. PMID 19836332 DOI: 10.1016/J.Str.2009.08.012 |
0.804 |
|
| 2009 |
Wallen JR, Mallett TC, Boles W, Parsonage D, Furdui CM, Karplus PA, Claiborne A. Crystal structure and catalytic properties of Bacillus anthracis CoADR-RHD: implications for flavin-linked sulfur trafficking. Biochemistry. 48: 9650-67. PMID 19725515 DOI: 10.1021/Bi900887K |
0.406 |
|
| 2009 |
Khayrutdinov BI, Bae WJ, Yun YM, Lee JH, Tsuyama T, Kim JJ, Hwang E, Ryu KS, Cheong HK, Cheong C, Ko JS, Enomoto T, Karplus PA, Güntert P, Tada S, et al. Structure of the Cdt1 C-terminal domain: conservation of the winged helix fold in replication licensing factors. Protein Science : a Publication of the Protein Society. 18: 2252-64. PMID 19722278 DOI: 10.1002/Pro.236 |
0.334 |
|
| 2009 |
Hollingsworth SA, Berkholz DS, Karplus PA. On the occurrence of linear groups in proteins. Protein Science : a Publication of the Protein Society. 18: 1321-5. PMID 19472372 DOI: 10.1002/Pro.133 |
0.785 |
|
| 2009 |
Hall A, Parsonage D, Horita D, Karplus PA, Poole LB, Barbar E. Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds. Biochemistry. 48: 5984-93. PMID 19459661 DOI: 10.1021/Bi900270W |
0.327 |
|
| 2008 |
Berkholz DS, Faber HR, Savvides SN, Karplus PA. Catalytic cycle of human glutathione reductase near 1 A resolution. Journal of Molecular Biology. 382: 371-84. PMID 18638483 DOI: 10.1016/J.Jmb.2008.06.083 |
0.808 |
|
| 2008 |
Wallen JR, Paige C, Mallett TC, Karplus PA, Claiborne A. Pyridine nucleotide complexes with Bacillus anthracis coenzyme A-disulfide reductase: a structural analysis of dual NAD(P)H specificity. Biochemistry. 47: 5182-93. PMID 18399646 DOI: 10.1021/Bi8002204 |
0.337 |
|
| 2008 |
Karplus PA, Shapovalov MV, Dunbrack RL, Berkholz DS. A forward-looking suggestion for resolving the stereochemical restraints debate: ideal geometry functions. Acta Crystallographica. Section D, Biological Crystallography. 64: 335-6. PMID 18323629 DOI: 10.1107/S0907444908002333 |
0.779 |
|
| 2008 |
Colussi T, Parsonage D, Boles W, Matsuoka T, Mallett TC, Karplus PA, Claiborne A. Structure of alpha-glycerophosphate oxidase from Streptococcus sp.: a template for the mitochondrial alpha-glycerophosphate dehydrogenase. Biochemistry. 47: 965-77. PMID 18154320 DOI: 10.1021/Bi701685U |
0.354 |
|
| 2007 |
Karplus PA, Hall A. Structural survey of the peroxiredoxins. Sub-Cellular Biochemistry. 44: 41-60. PMID 18084889 |
0.35 |
|
| 2007 |
Li Q, Nance MR, Kulikauskas R, Nyberg K, Fehon R, Karplus PA, Bretscher A, Tesmer JJ. Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain. Journal of Molecular Biology. 365: 1446-59. PMID 17134719 DOI: 10.1016/J.Jmb.2006.10.075 |
0.602 |
|
| 2006 |
Mallett TC, Wallen JR, Karplus PA, Sakai H, Tsukihara T, Claiborne A. Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 A resolution. Biochemistry. 45: 11278-89. PMID 16981688 DOI: 10.1021/Bi061139A |
0.408 |
|
| 2006 |
Dominy JE, Simmons CR, Karplus PA, Gehring AM, Stipanuk MH. Identification and characterization of bacterial cysteine dioxygenases: a new route of cysteine degradation for eubacteria. Journal of Bacteriology. 188: 5561-9. PMID 16855246 DOI: 10.1128/Jb.00291-06 |
0.324 |
|
| 2006 |
Krueger SK, Siddens LK, Henderson MC, VanDyke JE, Karplus PA, Pereira CB, Williams DE. C-Terminal truncation of rabbit flavin-containing monooxygenase isoform 2 enhances solubility. Archives of Biochemistry and Biophysics. 450: 149-56. PMID 16620765 DOI: 10.1016/J.Abb.2006.03.012 |
0.33 |
|
| 2006 |
Simmons CR, Liu Q, Huang Q, Hao Q, Begley TP, Karplus PA, Stipanuk MH. Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear iron center for cysteine thiol oxidation. The Journal of Biological Chemistry. 281: 18723-33. PMID 16611640 DOI: 10.1074/Jbc.M601555200 |
0.341 |
|
| 2005 |
Sarma GN, Manning VA, Ciuffetti LM, Karplus PA. Structure of Ptr ToxA: an RGD-containing host-selective toxin from Pyrenophora tritici-repentis. The Plant Cell. 17: 3190-202. PMID 16214901 DOI: 10.1105/Tpc.105.034918 |
0.341 |
|
| 2005 |
Roberts BR, Wood ZA, Jönsson TJ, Poole LB, Karplus PA. Oxidized and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF Protein Science. 14: 2414-2420. PMID 16131664 DOI: 10.1110/Ps.051459705 |
0.702 |
|
| 2005 |
Parsonage D, Youngblood DS, Sarma GN, Wood ZA, Karplus PA, Poole LB. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin Biochemistry. 44: 10583-10592. PMID 16060667 DOI: 10.1021/Bi050448I |
0.686 |
|
| 2005 |
Sarma GN, Nickel C, Rahlfs S, Fischer M, Becker K, Karplus PA. Crystal structure of a novel Plasmodium falciparum 1-Cys peroxiredoxin. Journal of Molecular Biology. 346: 1021-34. PMID 15701514 DOI: 10.1016/j.jmb.2004.12.022 |
0.376 |
|
| 2004 |
Karplus PA, Faber HR. Structural Aspects of Plant Ferredoxin : NADP(+) Oxidoreductases. Photosynthesis Research. 81: 303-15. PMID 16034534 DOI: 10.1023/B:PRES.0000036884.57303.2e |
0.301 |
|
| 2004 |
Finnerty CM, Chambers D, Ingraffea J, Faber HR, Karplus PA, Bretscher A. The EBP50-moesin interaction involves a binding site regulated by direct masking on the FERM domain Journal of Cell Science. 117: 1547-1552. PMID 15020681 DOI: 10.1242/Jcs.01038 |
0.796 |
|
| 2003 |
Sarma GN, Savvides SN, Becker K, Schirmer M, Schirmer RH, Karplus PA. Glutathione reductase of the malarial parasite Plasmodium falciparum: crystal structure and inhibitor development. Journal of Molecular Biology. 328: 893-907. PMID 12729762 DOI: 10.1016/S0022-2836(03)00347-4 |
0.612 |
|
| 2003 |
Wood ZA, Poole LB, Karplus PA. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science. 300: 650-653. PMID 12714747 DOI: 10.1126/Science.1080405 |
0.664 |
|
| 2003 |
Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA. Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions. The Journal of Biological Chemistry. 278: 4949-56. PMID 12429733 DOI: 10.1074/Jbc.M210601200 |
0.607 |
|
| 2002 |
Wood ZA, Poole LB, Hantgan RR, Karplus PA. Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins Biochemistry. 41: 5493-5504. PMID 11969410 DOI: 10.1021/Bi012173M |
0.693 |
|
| 2002 |
Finnerty CM, Charrier V, Claiborne A, Karplus PA. Crystallization and preliminary crystallographic analysis of the soluble alpha-glycerophosphate oxidase from Streptococcus sp. Acta Crystallographica. Section D, Biological Crystallography. 58: 165-6. PMID 11752801 DOI: 10.1107/S0907444901018169 |
0.751 |
|
| 2002 |
Savvides SN, Scheiwein M, Bohme CC, Arteel GE, Karplus PA, Becker K, Schirmer RH. Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite. The Journal of Biological Chemistry. 277: 2779-84. PMID 11705998 DOI: 10.1074/Jbc.M108190200 |
0.646 |
|
| 2001 |
Aliverti A, Faber R, Finnerty CM, Ferioli C, Pandini V, Negri A, Karplus PA, Zanetti G. Biochemical and crystallographic characterization of ferredoxin-NADP(+) reductase from nonphotosynthetic tissues. Biochemistry. 40: 14501-8. PMID 11724563 DOI: 10.1021/bi011224c |
0.789 |
|
| 2001 |
Wood ZA, Poole LB, Karplus PA. Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis Biochemistry. 40: 3900-3911. PMID 11300769 DOI: 10.1021/Bi002765P |
0.703 |
|
| 2000 |
Rodriguez E, Wood ZA, Karplus PA, Lei XG. Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris Archives of Biochemistry and Biophysics. 382: 105-112. PMID 11051103 DOI: 10.1006/Abbi.2000.2021 |
0.652 |
|
| 2000 |
Pearson MA, Park IS, Schaller RA, Michel LO, Karplus PA, Hausinger RP. Kinetic and structural characterization of urease active site variants. Biochemistry. 39: 8575-84. PMID 10913264 DOI: 10.1021/Bi000613O |
0.303 |
|
| 2000 |
Savvides SN, Boone T, Karplus PA. Flt3 ligand structure and unexpected commonalities of helical bundles and cystine knots Nature Structural Biology. 7: 486-491. PMID 10881197 DOI: 10.1038/75896 |
0.553 |
|
| 2000 |
Pearson MA, Reczek D, Bretscher A, Karplus PA. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain Cell. 101: 259-270. PMID 10847681 DOI: 10.1016/S0092-8674(00)80836-3 |
0.604 |
|
| 1999 |
Finnerty CM, Karplus PA, Granados RR. The insect immune protein scolexin is a novel serine proteinase homolog. Protein Science : a Publication of the Protein Society. 8: 242-8. PMID 10210202 DOI: 10.1110/ps.8.1.242 |
0.785 |
|
| 1999 |
Fox KM, Karplus PA. The flavin environment in old yellow enzyme. An evaluation of insights from spectroscopic and artificial flavin studies. The Journal of Biological Chemistry. 274: 9357-62. PMID 10092614 DOI: 10.1074/jbc.274.14.9357 |
0.352 |
|
| 1998 |
Aliverti A, Deng Z, Ravasi D, Piubelli L, Karplus PA, Zanetti G. Probing the function of the invariant glutamyl residue 312 in spinach ferredoxin-NADP+ reductase Journal of Biological Chemistry. 273: 34008-34015. PMID 9852055 DOI: 10.1074/jbc.273.51.34008 |
0.341 |
|
| 1998 |
Brown BJ, Deng Z, Karplus PA, Massey V. On the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194. The Journal of Biological Chemistry. 273: 32753-62. PMID 9830019 DOI: 10.1074/Jbc.273.49.32753 |
0.316 |
|
| 1998 |
Pearson MA, Karplus PA, Dodge RW, Laity JH, Scheraga HA. Crystal structures of two mutants that have implications for the folding of bovine pancreatic ribonuclease A. Protein Science : a Publication of the Protein Society. 7: 1255-8. PMID 9605332 DOI: 10.1002/Pro.5560070522 |
0.365 |
|
| 1998 |
Pearson MA, Schaller RA, Michel LO, Karplus PA, Hausinger RP. Chemical rescue of Klebsiella aerogenes urease variants lacking the carbamylated-lysine nickel ligand Biochemistry. 37: 6214-6220. PMID 9558361 DOI: 10.1021/Bi980021U |
0.305 |
|
| 1998 |
Becker K, Savvides SN, Keese M, Schirmer RH, Karplus PA. Enzyme inactivation through sulfhydryl oxidation by physiologic NO- carriers Nature Structural Biology. 5: 267-271. PMID 9546215 DOI: 10.1038/Nsb0498-267 |
0.6 |
|
| 1998 |
Irwin D, Shin DH, Zhang S, Barr BK, Sakon J, Karplus PA, Wilson DB. Roles of the catalytic domain and two cellulose binding domains of Thermomonospora fusca E4 in cellulose hydrolysis Journal of Bacteriology. 180: 1709-1714. PMID 9537366 |
0.639 |
|
| 1997 |
Himmel ME, Karplus PA, Sakon J, Adney WS, Baker JO, Thomas SR. Polysaccharide hydrolase folds diversity of structure and convergence of function. Applied Biochemistry and Biotechnology. 63: 315-25. PMID 18576090 DOI: 10.1007/BF02920433 |
0.341 |
|
| 1997 |
Pearson MA, Michel LO, Hausinger RP, Karplus PA. Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease Biochemistry. 36: 8164-8172. PMID 9201965 DOI: 10.1021/Bi970514J |
0.335 |
|
| 1996 |
Rozwarski DA, Diederichs K, Hecht R, Boone T, Karplus PA. Refined crystal structure and mutagenesis of human granulocyte- macrophage colony-stimulating factor Proteins: Structure, Function and Genetics. 26: 304-313. PMID 8953651 DOI: 10.1002/(SICI)1097-0134(199611)26:3<304::AID-PROT6>3.0.CO;2-D |
0.327 |
|
| 1996 |
Faerman CH, Savvides SN, Strickland C, Breidenbach MA, Ponasik JA, Ganem B, Ripoll D, Krauth-Siegel RL, Karplus PA. Charge is the major discriminating factor for glutathione reductase versus trypanothione reductase inhibitors. Bioorganic & Medicinal Chemistry. 4: 1247-53. PMID 8879546 DOI: 10.1016/0968-0896(96)00120-4 |
0.558 |
|
| 1996 |
Karplus PA. Experimentally observed conformation-dependent geometry and hidden strain in proteins Protein Science. 5: 1406-1420. PMID 8819173 |
0.307 |
|
| 1996 |
Jabri E, Karplus PA. Structures of the Klebsiella aerogenes urease apoenzyme and two active-site mutants. Biochemistry. 35: 10616-26. PMID 8718850 DOI: 10.1021/bi960424z |
0.303 |
|
| 1996 |
Savvides SN, Karplus PA. Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor Journal of Biological Chemistry. 271: 8101-8107. PMID 8626496 DOI: 10.1074/Jbc.271.14.8101 |
0.608 |
|
| 1996 |
Sakon J, Thomas S, Himmel M, Karplus PA. The roles of key residues in the 4/7 superfamily of glycosyl hydrolases revealed by cellulase:substrate complex Acta Crystallographica Section a Foundations of Crystallography. 52: C193-C194. DOI: 10.1107/S0108767396091581 |
0.675 |
|
| 1996 |
Savvides SN, Karplus PA. Characterization of a non-competitive inhibitor of human glutathione reductase Acta Crystallographica Section a Foundations of Crystallography. 52: C206-C207. DOI: 10.1107/S010876739609109X |
0.509 |
|
| 1995 |
Strickland CL, Puchalski R, Savvides SN, Karplus PA. Overexpression of Crithidia fasciculata trypanothione reductase and crystallization using a novel geometry. Acta Crystallographica. Section D, Biological Crystallography. 51: 337-41. PMID 15299300 DOI: 10.1107/S0907444994010772 |
0.573 |
|
| 1995 |
Karplus PA, Fox KM, Massey V. Flavoprotein structure and mechanism. 8. Structure-function relations for old yellow enzyme. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 9: 1518-26. PMID 8529830 |
0.305 |
|
| 1995 |
Bruns CM, Karplus PA. Refined crystal structure of spinach ferredoxin reductase at 1.7 Å resolution: Oxidized, reduced and 2′-phospho-5′-AMP bound states Journal of Molecular Biology. 247: 125-145. PMID 7897656 DOI: 10.1006/jmbi.1994.0127 |
0.334 |
|
| 1995 |
Jabri E, Carr MB, Hausinger RP, Karplus PA. The crystal structure of urease from Klebsiella aerogenes Science. 268: 998-1004. PMID 7754395 DOI: 10.1126/Science.7754395 |
0.307 |
|
| 1995 |
Whitaker RD, Cho Y, Cha J, Carrell HL, Glusker JP, Karplus PA, Batt CA. Probing the roles of active site residues in D-xylose isomerase. The Journal of Biological Chemistry. 270: 22895-906. PMID 7559425 DOI: 10.1074/Jbc.270.39.22895 |
0.325 |
|
| 1995 |
Ponasik JA, Strickland C, Faerman C, Savvides S, Karplus PA, Ganem B. Kukoamine A and other hydrophobic acylpolyamines: potent and selective inhibitors of Crithidia fasciculata trypanothione reductase. The Biochemical Journal. 311: 371-5. PMID 7487870 DOI: 10.1042/Bj3110371 |
0.553 |
|
| 1995 |
Strickland CL, Puchalski R, Savvides SN, Karplus PA. Overexpression of Crithidia fasciculata trypanothione reductase and crystallization using a novel ggeometry Acta Crystallographica - Section D Biological Crystallography. 51: 337-341. DOI: 10.1107/S0907444994010772 |
0.53 |
|
| 1994 |
Karplus PA, Bruns CM. Structure-function relations for ferredoxin reductase Journal of Bioenergetics and Biomembranes. 26: 89-99. PMID 8027025 DOI: 10.1007/BF00763221 |
0.321 |
|
| 1994 |
Fox KM, Karplus PA. Old yellow enzyme at 2 Å resolution: overall structure, ligand binding, and comparison with related flavoproteins Structure. 2: 1089-1105. PMID 7881908 DOI: 10.1016/S0969-2126(94)00111-1 |
0.33 |
|
| 1993 |
Spezio M, Wilson DB, Karplus PA. Crystal structure of the catalytic domain of a thermophilic endocellulase Biochemistry. 32: 9906-9916. PMID 8399160 |
0.396 |
|
| 1993 |
Correll CC, Ludwig ML, Bruns CM, Karplus PA. Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin. Protein Science : a Publication of the Protein Society. 2: 2112-33. PMID 8298460 DOI: 10.1002/Pro.5560021212 |
0.357 |
|
| 1993 |
Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin Journal of Molecular Biology. 229: 105-124. PMID 7678431 DOI: 10.1006/Jmbi.1993.1012 |
0.475 |
|
| 1991 |
Karplus PA, Daniels MJ, Herriott JR. Atomic structure of ferredoxin-NADP+ reductase: Prototype for a structurally novel flavoenzyme family Science. 251: 60-66. PMID 1986412 |
0.793 |
|
| 1991 |
Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clarpy J. Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex Science. 252: 839-842. PMID 1709302 DOI: 10.1126/Science.1709302 |
0.333 |
|
| 1989 |
Karplus PA, Pai EF, Schulz GE. A crystallographic study of the glutathione binding site of glutathione reductase at 0.3-nm resolution European Journal of Biochemistry. 178: 693-703. PMID 2912729 DOI: 10.1111/J.1432-1033.1989.Tb14500.X |
0.694 |
|
| 1989 |
Karplus PA, Schulz GE. Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: Substrate crystal structures at 2Å resolution Journal of Molecular Biology. 210: 163-180. PMID 2585516 DOI: 10.1016/0022-2836(89)90298-2 |
0.616 |
|
| 1988 |
Schulz GE, Karplus PA. High resolution structure and catalytic action of human glutathione reductase Biochemical Society Transactions. 16: 81-84. PMID 3371538 DOI: 10.1042/Bst0160081 |
0.517 |
|
| 1988 |
Karplus PA, Krauth-Siegel RL, Schirmer RH, Schulz GE. 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 European Journal of Biochemistry. 171: 193-198. PMID 3338461 DOI: 10.1111/J.1432-1033.1988.Tb13775.X |
0.543 |
|
| 1988 |
Pai EF, Karplus PA, Schulz GE. Crystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase Biochemistry®. 27: 4465-4474. PMID 2844232 |
0.676 |
|
| 1988 |
Dreusicke D, Karplus PA, Schulz GE. Refined structure of porcine cytosolic adenylate kinase at 2.1 Å resolution Journal of Molecular Biology. 199: 359-371. PMID 2832612 DOI: 10.1016/0022-2836(88)90319-1 |
0.579 |
|
| 1987 |
Karplus PA, Schulz GE. Refined structure of glutathione reductase at 1.54 Å resolution Journal of Molecular Biology. 195: 701-729. PMID 3656429 DOI: 10.1016/0022-2836(87)90191-4 |
0.571 |
|
| 1985 |
Karplus PA, Schulz GE. Prediction of chain flexibility in proteins - A tool for the selection of peptide antigens Naturwissenschaften. 72: 212-213. DOI: 10.1007/BF01195768 |
0.465 |
|
| 1984 |
Karplus PA, Walsh KA, Herriott JR. Amino acid sequence of spinach ferredoxin:NADP+ oxidoreductase Biochemistry. 23: 6576-6583. PMID 6529571 DOI: 10.1021/Bi00321A046 |
0.782 |
|
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