{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T05:12:59Z","timestamp":1788412379969,"version":"build-2803163510"},"reference-count":48,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2014,2,21]],"date-time":"2014-02-21T00:00:00Z","timestamp":1392940800000},"content-version":"vor","delay-in-days":385,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chemistry &amp; Biology"],"published-print":{"date-parts":[[2013,2]]},"DOI":"10.1016\/j.chembiol.2013.01.009","type":"journal-article","created":{"date-parts":[[2013,2,21]],"date-time":"2013-02-21T14:52:04Z","timestamp":1361458324000},"page":"212-222","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"title":["Catalytic Site Conformations in Human PNP by 19F-NMR and Crystallography"],"prefix":"10.1016","volume":"20","author":[{"given":"Javier","family":"Suarez","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antti\u00a0M.","family":"Haapalainen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sean\u00a0M.","family":"Cahill","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Meng-Chiao","family":"Ho","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Funing","family":"Yan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven\u00a0C.","family":"Almo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vern\u00a0L.","family":"Schramm","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.chembiol.2013.01.009_bib1","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1182\/blood-2010-02-272039","article-title":"Phase 2 and pharmacodynamic study of oral forodesine in patients with advanced, fludarabine-treated chronic lymphocytic leukemia","volume":"116","author":"Balakrishnan","year":"2010","journal-title":"Blood"},{"key":"10.1016\/j.chembiol.2013.01.009_bib2","doi-asserted-by":"crossref","first-page":"e26916","DOI":"10.1371\/journal.pone.0026916","article-title":"Plasmodium falciparum parasites are killed by a transition state analogue of purine nucleoside phosphorylase in a primate animal model","volume":"6","author":"Cassera","year":"2011","journal-title":"PLoS ONE"},{"key":"10.1016\/j.chembiol.2013.01.009_bib3","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: all-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.chembiol.2013.01.009_bib4","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1107\/S0907444994003112","article-title":"The CCP4 suite: programs for protein crystallography","volume":"50","year":"1994","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"Web Server issue","key":"10.1016\/j.chembiol.2013.01.009_bib5","doi-asserted-by":"crossref","first-page":"W375","DOI":"10.1093\/nar\/gkm216","article-title":"MolProbity: all-atom contacts and structure validation for proteins and nucleic acids","volume":"35","author":"Davis","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.chembiol.2013.01.009_bib6","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/S0006-291X(03)01431-1","article-title":"Crystal structure of human purine nucleoside phosphorylase at 2.3A resolution","volume":"308","author":"de Azevedo","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.chembiol.2013.01.009_bib7","doi-asserted-by":"crossref","first-page":"9516","DOI":"10.1021\/ja049296p","article-title":"Activating the phosphate nucleophile at the catalytic site of purine nucleoside phosphorylase: a vibrational spectroscopic study","volume":"126","author":"Deng","year":"2004","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.chembiol.2013.01.009_bib8","doi-asserted-by":"crossref","first-page":"5226","DOI":"10.1021\/bi9005896","article-title":"Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside phosphorylase","volume":"48","author":"Edwards","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib9","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.chembiol.2013.01.009_bib10","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1021\/bi002499f","article-title":"Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis","volume":"40","author":"Fedorov","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib11","doi-asserted-by":"crossref","first-page":"3202","DOI":"10.1021\/bi702491d","article-title":"Tryptophan-free human PNP reveals catalytic site interactions","volume":"47","author":"Ghanem","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib12","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/j.chembiol.2009.07.012","article-title":"Ribocation transition state capture and rebound in human purine nucleoside phosphorylase","volume":"16","author":"Ghanem","year":"2009","journal-title":"Chem. Biol."},{"key":"10.1016\/j.chembiol.2013.01.009_bib13","doi-asserted-by":"crossref","first-page":"3658","DOI":"10.1021\/bi802339c","article-title":"Loop-tryptophan human purine nucleoside phosphorylase reveals submillisecond protein dynamics","volume":"48","author":"Ghanem","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib14","doi-asserted-by":"crossref","first-page":"1010","DOI":"10.1016\/S0140-6736(75)91950-9","article-title":"Nucleoside-phosphorylase deficiency in a child with severely defective T-cell immunity and normal B-cell immunity","volume":"1","author":"Giblett","year":"1975","journal-title":"Lancet"},{"key":"10.1016\/j.chembiol.2013.01.009_bib15","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1146\/annurev.biochem.75.103004.142800","article-title":"Relating protein motion to catalysis","volume":"75","author":"Hammes-Schiffer","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.chembiol.2013.01.009_bib16","doi-asserted-by":"crossref","first-page":"16263","DOI":"10.1021\/jp108056s","article-title":"Conformational dynamics in human purine nucleoside phosphorylase with reactants and transition-state analogues","volume":"114","author":"Hirschi","year":"2010","journal-title":"J.\u00a0Phys. Chem. B"},{"key":"10.1016\/j.chembiol.2013.01.009_bib17","doi-asserted-by":"crossref","first-page":"4805","DOI":"10.1073\/pnas.0913439107","article-title":"Four generations of transition-state analogues for human purine nucleoside phosphorylase","volume":"107","author":"Ho","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2013.01.009_bib18","doi-asserted-by":"crossref","first-page":"5502","DOI":"10.1021\/bi00184a019","article-title":"19F NMR spectroscopy of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase: equilibrium folding and ligand binding studies","volume":"33","author":"Hoeltzli","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib19","unstructured":"Hollister, A.S., Michael A., Becker, M.A., Terkeltaub, R., Waugh, A., Lyman, A., Amy Flynt, A., and FitzPatrick, D. (2011). BCX4208 synergistically lowers serum uric acid (sUA) levels when combined with allopurinol in patients with gout: results of a phase 2 dose-ranging trial. ACR\/ARHP Poster Session B, Abs. 1018."},{"key":"10.1016\/j.chembiol.2013.01.009_bib20","doi-asserted-by":"crossref","first-page":"3219","DOI":"10.1074\/jbc.M105905200","article-title":"Transition state analogue inhibitors of purine nucleoside phosphorylase from Plasmodium falciparum","volume":"277","author":"Kicska","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.chembiol.2013.01.009_bib21","doi-asserted-by":"crossref","first-page":"1771","DOI":"10.1016\/S0021-9258(18)93510-6","article-title":"Purine nucleoside phosphorylase from human erythroyctes. II. Kinetic analysis and substrate-binding studies","volume":"243","author":"Kim","year":"1968","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.chembiol.2013.01.009_bib22","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pnmrs.2011.06.003","article-title":"Current applications of 19F NMR to studies of protein structure and dynamics","volume":"62","author":"Kitevski-LeBlanc","year":"2012","journal-title":"Prog. Nucl. Magn. Reson. Spectrosc."},{"key":"10.1016\/j.chembiol.2013.01.009_bib23","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1007\/s10858-009-9359-2","article-title":"Approaches for the measurement of solvent exposure in proteins by 19F NMR","volume":"45","author":"Kitevski-LeBlanc","year":"2009","journal-title":"J.\u00a0Biomol. NMR"},{"key":"10.1016\/j.chembiol.2013.01.009_bib24","doi-asserted-by":"crossref","first-page":"13212","DOI":"10.1021\/bi00211a033","article-title":"Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction","volume":"32","author":"Kline","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib25","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1006\/jmbi.1996.0730","article-title":"Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15 A resolution","volume":"265","author":"Koellner","year":"1997","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.chembiol.2013.01.009_bib26","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1093\/nar\/28.8.1665","article-title":"The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework","volume":"28","author":"Krebs","year":"2000","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.chembiol.2013.01.009_bib27","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1107\/S0021889892009944","article-title":"PROCHECK: a program to check the stereochemical quality of protein structures","volume":"26","author":"Laskowski","year":"1993","journal-title":"J.\u00a0Appl. Cryst."},{"key":"10.1016\/j.chembiol.2013.01.009_bib28","doi-asserted-by":"crossref","first-page":"1458","DOI":"10.1021\/bi0359123","article-title":"Transition state analysis for human and Plasmodium falciparum purine nucleoside phosphorylases","volume":"43","author":"Lewandowicz","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib29","doi-asserted-by":"crossref","first-page":"6057","DOI":"10.1021\/bi0343830","article-title":"Over-the-barrier transition state analogues and crystal structure with Mycobacterium tuberculosis purine nucleoside phosphorylase","volume":"42","author":"Lewandowicz","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib30","doi-asserted-by":"crossref","first-page":"1106","DOI":"10.1126\/science.1215802","article-title":"Biased signaling pathways in \u03b22-adrenergic receptor characterized by 19F-NMR","volume":"335","author":"Liu","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.chembiol.2013.01.009_bib31","doi-asserted-by":"crossref","first-page":"4257","DOI":"10.1021\/bi00231a022","article-title":"19F NMR studies of the D-galactose chemosensory receptor. 2. Ca(II) binding yields a local structural change","volume":"30","author":"Luck","year":"1991","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib32","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J.\u00a0Appl. Cryst."},{"key":"10.1016\/j.chembiol.2013.01.009_bib33","doi-asserted-by":"crossref","first-page":"8615","DOI":"10.1021\/bi980658d","article-title":"One-third-the-sites transition-state inhibitors for purine nucleoside phosphorylase","volume":"37","author":"Miles","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib34","doi-asserted-by":"crossref","first-page":"859","DOI":"10.1107\/S0907444906019949","article-title":"HKL-3000: the integration of data reduction and structure solution\u2014from diffraction images to an initial model in minutes","volume":"62","author":"Minor","year":"2006","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.chembiol.2013.01.009_bib35","doi-asserted-by":"crossref","first-page":"5038","DOI":"10.1021\/bi700147b","article-title":"Neighboring group participation in the transition state of human purine nucleoside phosphorylase","volume":"46","author":"Murkin","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib36","doi-asserted-by":"crossref","first-page":"2166","DOI":"10.1021\/ja7104398","article-title":"Transition-state interactions revealed in purine nucleoside phosphorylase by binding isotope effects","volume":"130","author":"Murkin","year":"2008","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.chembiol.2013.01.009_bib37","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov","year":"1997","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.chembiol.2013.01.009_bib38","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1107\/S0907444903008126","article-title":"A graphical user interface to the CCP4 program suite","volume":"59","author":"Potterton","year":"2003","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.chembiol.2013.01.009_bib39","doi-asserted-by":"crossref","first-page":"842","DOI":"10.1021\/ja710733g","article-title":"L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase","volume":"130","author":"Rinaldo-Matthis","year":"2008","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.chembiol.2013.01.009_bib40","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1021\/bi061515r","article-title":"Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues","volume":"46","author":"Rinaldo-Matthis","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib41","doi-asserted-by":"crossref","first-page":"4078","DOI":"10.1529\/biophysj.107.121913","article-title":"Remote mutations and active site dynamics correlate with catalytic properties of purine nucleoside phosphorylase","volume":"94","author":"Saen-Oon","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.chembiol.2013.01.009_bib42","doi-asserted-by":"crossref","first-page":"16543","DOI":"10.1073\/pnas.0808413105","article-title":"Atomic detail of chemical transformation at the transition state of an enzymatic reaction","volume":"105","author":"Saen-Oon","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.chembiol.2013.01.009_bib43","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1093\/protein\/15.11.855","article-title":"19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesis and assignment of the 5-fluorotryptophan-labeled residues","volume":"15","author":"Salopek-Sondi","year":"2002","journal-title":"Protein Eng."},{"key":"10.1016\/j.chembiol.2013.01.009_bib44","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.abb.2004.08.035","article-title":"Enzymatic transition states: thermodynamics, dynamics and analogue design","volume":"433","author":"Schramm","year":"2005","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.chembiol.2013.01.009_bib45","doi-asserted-by":"crossref","first-page":"18103","DOI":"10.1074\/jbc.C400068200","article-title":"Plasmodium falciparum purine nucleoside phosphorylase: crystal structures, immucillin inhibitors, and dual catalytic function","volume":"279","author":"Shi","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.chembiol.2013.01.009_bib46","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1016\/S0076-6879(78)51074-4","article-title":"Purine nucleoside phosphorylase from human erythrocytes","volume":"51","author":"Stoeckler","year":"1978","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.chembiol.2013.01.009_bib47","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1021\/bi00542a016","article-title":"Human erythrocytic purine nucleoside phosphorylase: reaction with sugar-modified nucleoside substrates","volume":"19","author":"Stoeckler","year":"1980","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2013.01.009_bib48","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1107\/S0907444909042589","article-title":"Molecular replacement with MOLREP","volume":"66","author":"Vagin","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."}],"container-title":["Chemistry &amp; Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S107455211300032X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S107455211300032X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T07:19:40Z","timestamp":1761031180000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S107455211300032X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,2]]},"references-count":48,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2013,2]]}},"alternative-id":["S107455211300032X"],"URL":"https:\/\/doi.org\/10.1016\/j.chembiol.2013.01.009","relation":{},"ISSN":["1074-5521"],"issn-type":[{"value":"1074-5521","type":"print"}],"subject":[],"published":{"date-parts":[[2013,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Catalytic Site Conformations in Human PNP by 19F-NMR and Crystallography","name":"articletitle","label":"Article Title"},{"value":"Chemistry & Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.chembiol.2013.01.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2013 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}