{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T08:56:15Z","timestamp":1790758575094,"version":"4.1.0"},"reference-count":104,"publisher":"Elsevier BV","issue":"49","license":[{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,1,13]],"date-time":"2021-01-13T00:00:00Z","timestamp":1610496000000},"content-version":"vor","delay-in-days":43,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100005440","name":"HHS | NIH | Center for Scientific Review","doi-asserted-by":"publisher","award":["R01-GM084383"],"award-info":[{"award-number":["R01-GM084383"]}],"id":[{"id":"10.13039\/100005440","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000289","name":"Cancer Research UK","doi-asserted-by":"publisher","award":["24759"],"award-info":[{"award-number":["24759"]}],"id":[{"id":"10.13039\/501100000289","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000268","name":"UKRI | Biotechnology and Biological Sciences Research Council","doi-asserted-by":"publisher","award":["POCMiB016"],"award-info":[{"award-number":["POCMiB016"]}],"id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100004440","name":"Wellcome Trust","doi-asserted-by":"publisher","award":["106244\/Z\/14\/Z"],"award-info":[{"award-number":["106244\/Z\/14\/Z"]}],"id":[{"id":"10.13039\/100004440","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2020,12]]},"DOI":"10.1074\/jbc.ra120.013998","type":"journal-article","created":{"date-parts":[[2020,9,15]],"date-time":"2020-09-15T20:45:17Z","timestamp":1600202717000},"page":"16545-16561","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":21,"title":["Biochemical and biophysical analyses of hypoxia sensing prolyl hydroxylases from Dictyostelium discoideum and Toxoplasma gondii"],"prefix":"10.1016","volume":"295","author":[{"given":"Tongri","family":"Liu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2141-5988","authenticated-orcid":false,"given":"Martine I.","family":"Abboud","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rasheduzzaman","family":"Chowdhury","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony","family":"Tumber","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adam P.","family":"Hardy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kerstin","family":"Lippl","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1094-0349","authenticated-orcid":false,"given":"Christopher T.","family":"Lohans","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8646-062X","authenticated-orcid":false,"given":"Elisabete","family":"Pires","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James","family":"Wickens","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4664-6942","authenticated-orcid":false,"given":"Michael A.","family":"McDonough","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9077-965X","authenticated-orcid":false,"given":"Christopher M.","family":"West","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0290-6565","authenticated-orcid":false,"given":"Christopher J.","family":"Schofield","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA120.013998_bib1","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1203\/00006450-200105000-00002","article-title":"Hypoxia-inducible factor 1: control of oxygen homeostasis in health and disease","volume":"49","author":"Semenza","year":"2001","journal-title":"Pediatr. Res"},{"key":"10.1074\/jbc.RA120.013998_bib2","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1126\/science.1059796","article-title":"Targeting of HIF-\u03b1 to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation","volume":"292","author":"Jaakkola","year":"2001","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.013998_bib3","doi-asserted-by":"crossref","first-page":"1308","DOI":"10.1039\/b701676j","article-title":"The human oxygen sensing machinery and its manipulation","volume":"37","author":"Chowdhury","year":"2008","journal-title":"Chem. Soc. Rev"},{"key":"10.1074\/jbc.RA120.013998_bib4","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/S0955-0674(00)00194-0","article-title":"HIF-1 and mechanisms of hypoxia sensing","volume":"13","author":"Semenza","year":"2001","journal-title":"Curr. Opin. Cell. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib5","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/j.molcel.2008.04.009","article-title":"Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway","volume":"30","author":"Kaelin","year":"2008","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA120.013998_bib6","doi-asserted-by":"crossref","first-page":"C550","DOI":"10.1152\/ajpcell.00176.2011","article-title":"Hypoxia: cross talk between oxygen sensing and the cell cycle machinery","volume":"301","author":"Semenza","year":"2011","journal-title":"Am. J. Physiol. Cell Physiol"},{"key":"10.1074\/jbc.RA120.013998_bib7","doi-asserted-by":"crossref","first-page":"20661","DOI":"10.1074\/jbc.M116.749291","article-title":"Tuning the transcriptional response to hypoxia by inhibiting hypoxia-inducible factor (HIF) prolyl and asparaginyl hydroxylases","volume":"291","author":"Chan","year":"2016","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib8","doi-asserted-by":"crossref","first-page":"3627","DOI":"10.1007\/s00018-019-03387-9","article-title":"A long hypoxia-inducible factor 3 isoform 2 is a transcription activator that regulates erythropoietin","volume":"77","author":"Tolonen","year":"2019","journal-title":"Cell Mol. Life Sci"},{"key":"10.1074\/jbc.RA120.013998_bib9","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1038\/embor.2010.170","article-title":"The hypoxia-inducible transcription factor pathway regulates oxygen sensing in the simplest animal, Trichoplax adhaerens","volume":"12","author":"Loenarz","year":"2011","journal-title":"EMBO Rep"},{"key":"10.1074\/jbc.RA120.013998_bib10","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1002\/cmdc.201900557","article-title":"Structure-activity relationship and crystallographic studies on 4-hydroxypyrimidine HIF prolyl hydroxylase domain inhibitors","volume":"15","author":"Holt-Martyn","year":"2020","journal-title":"ChemMedChem"},{"key":"10.1074\/jbc.RA120.013998_bib11","doi-asserted-by":"crossref","first-page":"20712","DOI":"10.1074\/jbc.R115.662627","article-title":"Protein hydroxylation catalyzed by 2-oxoglutarate-dependent oxygenases","volume":"290","author":"Markolovic","year":"2015","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib12","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1002\/cmdc.201600012","article-title":"Targeting protein-protein interactions in the HIF system","volume":"11","author":"Wilkins","year":"2016","journal-title":"ChemMedChem"},{"key":"10.1074\/jbc.RA120.013998_bib13","doi-asserted-by":"crossref","first-page":"4364","DOI":"10.1039\/c0cs00203h","article-title":"Inhibition of 2-oxoglutarate dependent oxygenases","volume":"40","author":"Rose","year":"2011","journal-title":"Chem. Soc. Rev"},{"key":"10.1074\/jbc.RA120.013998_bib14","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1053\/j.ajkd.2016.12.011","article-title":"Hypoxia-inducible factor prolyl hydroxylase inhibitors: a potential new treatment for anemia in patients with CKD","volume":"69","author":"Gupta","year":"2017","journal-title":"Am. J. Kidney Dis"},{"key":"10.1074\/jbc.RA120.013998_bib15","doi-asserted-by":"crossref","first-page":"7651","DOI":"10.1039\/C7SC02103H","article-title":"Molecular and cellular mechanisms of HIF prolyl hydroxylase inhibitors in clinical trials","volume":"8","author":"Yeh","year":"2017","journal-title":"Chem. Sci"},{"key":"10.1074\/jbc.RA120.013998_bib16","doi-asserted-by":"crossref","first-page":"9814","DOI":"10.1073\/pnas.0601283103","article-title":"Cellular oxygen sensing: crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)","volume":"103","author":"McDonough","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.013998_bib17","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1016\/S0959-440X(99)00036-6","article-title":"Structural and mechanistic studies on 2-oxoglutarate-dependent oxygenases and related enzymes","volume":"9","author":"Schofield","year":"1999","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib18","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1016\/j.sbi.2012.10.001","article-title":"Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases","volume":"22","author":"Aik","year":"2012","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib19","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1016\/j.jinorgbio.2006.01.024","article-title":"Structural studies on 2-oxoglutarate oxygenases and related double-stranded \u03b2-helix fold proteins","volume":"100","author":"Clifton","year":"2006","journal-title":"J. Inorg. Biochem"},{"key":"10.1074\/jbc.RA120.013998_bib20","series-title":"2-Oxoglutarate-dependent oxygenases","first-page":"59","article-title":"Introduction to structural studies on 2-oxoglutarate-dependent oxygenases and related enzymes","author":"Aik","year":"2015"},{"key":"10.1074\/jbc.RA120.013998_bib21","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1016\/j.sbi.2010.08.006","article-title":"Structural studies on human 2-oxoglutarate dependent oxygenases","volume":"20","author":"McDonough","year":"2010","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib22","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms11974","article-title":"Arginine demethylation is catalyzed by a subset of JmjC histone lysine demethylases","volume":"7","author":"Walport","year":"2016","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.RA120.013998_bib23","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1038\/nature13263","article-title":"Ribosomal oxygenases are structurally conserved from prokaryotes to humans","volume":"510","author":"Chowdhury","year":"2014","journal-title":"Nature"},{"key":"10.1074\/jbc.RA120.013998_bib24","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1007\/s00424-015-1719-z","article-title":"Regulation of carotid body oxygen sensing by hypoxia-inducible factors","volume":"468","author":"Prabhakar","year":"2016","journal-title":"Pflugers Arch"},{"key":"10.1074\/jbc.RA120.013998_bib25","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1042\/BJ20140754","article-title":"Chromatin and oxygen sensing in the context of JmjC histone demethylases","volume":"462","author":"Shmakova","year":"2014","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.RA120.013998_bib26","article-title":"JmjC histone demethylases act as chromatin oxygen sensors","volume":"6","author":"Batie","year":"2019","journal-title":"Mol. Cell. Oncol"},{"key":"10.1074\/jbc.RA120.013998_bib27","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1126\/science.aaw1026","article-title":"Histone demethylase KDM6A directly senses oxygen to control chromatin and cell fate","volume":"363","author":"Chakraborty","year":"2019","journal-title":"Science"},{"key":"10.1074\/jbc.RA120.013998_bib28","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.46490","article-title":"Lack of activity of recombinant HIF prolyl hydroxylases (PHDs) on reported non-HIF substrates","volume":"8","author":"Cockman","year":"2019","journal-title":"Elife"},{"key":"10.1074\/jbc.RA120.013998_bib29","first-page":"272","article-title":"Ancient atmospheres and the evolution of oxygen sensing via the hypoxia-inducible factor in metazoans","volume":"25","author":"Taylor","year":"2010","journal-title":"Physiology (Bethesda)"},{"key":"10.1074\/jbc.RA120.013998_bib30","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1196\/annals.1391.004","article-title":"Oxygen, hypoxia, and stress","volume":"1113","author":"Taylor","year":"2007","journal-title":"Ann. N.Y. Acad. Sci"},{"key":"10.1074\/jbc.RA120.013998_bib31","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1016\/j.bbamcr.2009.01.014","article-title":"Role of the intracellular localization of HIF-prolyl hydroxylases","volume":"1793","author":"Yasumoto","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA120.013998_bib32","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.mib.2015.04.006","article-title":"Oxygen sensing by protozoans: how they catch their breath","volume":"26","author":"West","year":"2015","journal-title":"Curr. Opin. Microbiol"},{"key":"10.1074\/jbc.RA120.013998_bib33","doi-asserted-by":"crossref","first-page":"13331","DOI":"10.1073\/pnas.1409916111","article-title":"Human oxygen sensing may have origins in prokaryotic elongation factor Tu prolyl-hydroxylation","volume":"111","author":"Scotti","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA120.013998_bib34","doi-asserted-by":"crossref","first-page":"57","DOI":"10.2147\/HP.S174655","article-title":"Born to sense: biophysical analyses of the oxygen sensing prolyl hydroxylase from the simplest animal Trichoplax adhaerens","volume":"6","author":"Lippl","year":"2018","journal-title":"Hypoxia (Auckl.)"},{"key":"10.1074\/jbc.RA120.013998_bib35","doi-asserted-by":"crossref","first-page":"104","DOI":"10.12688\/wellcomeopenres.12871.1","article-title":"Pseudomonas expression of an oxygen sensing prolyl hydroxylase homologue regulates neutrophil host responses in vitro in vivo","volume":"2","author":"Dickinson","year":"2017","journal-title":"Wellcome Open Res"},{"key":"10.1074\/jbc.RA120.013998_bib36","doi-asserted-by":"crossref","first-page":"3349","DOI":"10.1242\/dev.000893","article-title":"Prolyl 4-hydroxylase-1 mediates O2 signaling during development of Dictyostelium","volume":"134","author":"West","year":"2007","journal-title":"Development"},{"key":"10.1074\/jbc.RA120.013998_bib37","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1093\/glycob\/cwz049","article-title":"Skp1 isoforms are differentially modified by a dual function prolyl 4-hydroxylase\/N-acetylglucosaminyltransferase in a plant pathogen","volume":"29","author":"van der Wel","year":"2019","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.RA120.013998_bib38","doi-asserted-by":"crossref","first-page":"18897","DOI":"10.1074\/jbc.M117.809160","article-title":"O2 sensing-associated glycosylation exposes the F-box-combining site of the dictyostelium Skp1 subunit in E3 ubiquitin ligases","volume":"292","author":"Sheikh","year":"2017","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib39","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1093\/glycob\/11.4.283","article-title":"Analysis of Skp1 glycosylation and nuclear enrichment in dictyostelium","volume":"11","author":"Sassi","year":"2001","journal-title":"Glycobiology"},{"key":"10.1074\/jbc.RA120.013998_bib40","doi-asserted-by":"crossref","first-page":"46527","DOI":"10.1074\/jbc.M208824200","article-title":"A bifunctional diglycosyltransferase forms the Fuc\u03b11,2Gal\u03b21,3-disaccharide on Skp1 in the cytoplasm of dictyostelium","volume":"277","author":"Van Der Wel","year":"2002","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib41","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.bbagen.2004.04.007","article-title":"Cytoplasmic glycosylation of protein-hydroxyproline and its relationship to other glycosylation pathways","volume":"1673","author":"West","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA120.013998_bib42","doi-asserted-by":"crossref","first-page":"28896","DOI":"10.1074\/jbc.M109.022574","article-title":"Role of a cytoplasmic dual-function glycosyltransferase in O2 regulation of development in dictyostelium","volume":"284","author":"Wang","year":"2009","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib43","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.bbagen.2009.11.006","article-title":"A cytoplasmic prolyl hydroxylation and glycosylation pathway modifies Skp1 and regulates O2-dependent development in dictyostelium","volume":"1800","author":"West","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1074\/jbc.RA120.013998_bib44","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1186\/1471-213X-12-31","article-title":"Role of the Skp1 prolyl-hydroxylation\/glycosylation pathway in oxygen dependent submerged development of dictyostelium","volume":"12","author":"Xu","year":"2012","journal-title":"BMC Dev. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib45","doi-asserted-by":"crossref","first-page":"2006","DOI":"10.1074\/jbc.M111.314021","article-title":"Skp1 prolyl 4-hydroxylase of dictyostelium mediates glycosylation-independent and -dependent responses to O2 without affecting Skp1 stability","volume":"287","author":"Zhang","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib46","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1038\/416703a","article-title":"Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex","volume":"416","author":"Zheng","year":"2002","journal-title":"Nature"},{"key":"10.1074\/jbc.RA120.013998_bib47","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.00234-19","article-title":"A toxoplasma prolyl hydroxylase mediates oxygen stress responses by regulating translation elongation","volume":"10","author":"Florimond","year":"2019","journal-title":"MBio"},{"key":"10.1074\/jbc.RA120.013998_bib48","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1016\/j.str.2009.06.002","article-title":"Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases","volume":"17","author":"Chowdhury","year":"2009","journal-title":"Structure"},{"key":"10.1074\/jbc.RA120.013998_bib49","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1039\/b511249b","article-title":"Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate","volume":"1","author":"McNeill","year":"2005","journal-title":"Mol. Biosyst"},{"key":"10.1074\/jbc.RA120.013998_bib50","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms12673","article-title":"Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases","volume":"7","author":"Chowdhury","year":"2016","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.RA120.013998_bib51","doi-asserted-by":"crossref","first-page":"18242","DOI":"10.1074\/jbc.273.29.18242","article-title":"The cytoplasmic F-box binding protein SKP1 contains a novel pentasaccharide linked to hydroxyproline in dictyostelium","volume":"273","author":"Teng-Umnuay","year":"1998","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib52","doi-asserted-by":"crossref","first-page":"30772","DOI":"10.1074\/jbc.M304982200","article-title":"Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor","volume":"278","author":"Hirsil\u00e4","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib53","doi-asserted-by":"crossref","first-page":"1700","DOI":"10.1021\/bi101977w","article-title":"Requirements for Skp1 processing by cytosolic prolyl 4(trans)-hydroxylase and \u03b1-N-acetylglucosaminyltransferase enzymes involved in O2 signaling in dictyostelium","volume":"50","author":"van der Wel","year":"2011","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013998_bib54","doi-asserted-by":"crossref","first-page":"19726","DOI":"10.1074\/jbc.M115.653014","article-title":"Kinetic investigations of the role of factor inhibiting hypoxia-inducible factor (FIH) as an oxygen sensor","volume":"290","author":"Tarhonskaya","year":"2015","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib55","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1042\/bj20021162","article-title":"Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyzes hydroxylation at the \u03b2-carbon of asparagine-803","volume":"367","author":"McNeill","year":"2002","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.RA120.013998_bib56","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1042\/BJ20140779","article-title":"Investigating the contribution of the active site environment to the slow reaction of hypoxia-inducible factor prolyl hydroxylase domain 2 with oxygen","volume":"463","author":"Tarhonskaya","year":"2014","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.RA120.013998_bib57","doi-asserted-by":"crossref","first-page":"14645","DOI":"10.1074\/jbc.M500600200","article-title":"The Skp1 prolyl hydroxylase from Dictyostelium is related to the hypoxia-inducible factor-\u03b1 class of animal prolyl 4-hydroxylases","volume":"280","author":"van der Wel","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib58","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1016\/j.ydbio.2010.10.013","article-title":"Prolyl hydroxylation- and glycosylation-dependent functions of Skp1 in O2-regulated development of dictyostelium","volume":"349","author":"Wang","year":"2011","journal-title":"Dev. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib59","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1074\/mcp.M114.044560","article-title":"Glycosylation of Skp1 promotes formation of Skp1-cullin-1-F-box protein complexes in dictyostelium","volume":"14","author":"Sheikh","year":"2015","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/jbc.RA120.013998_bib60","doi-asserted-by":"crossref","first-page":"2262","DOI":"10.1002\/cbic.201800246","article-title":"Studies on the substrate selectivity of the hypoxia-inducible factor prolyl hydroxylase 2 catalytic domain","volume":"19","author":"Abboud","year":"2018","journal-title":"ChemBioChem"},{"key":"10.1074\/jbc.RA120.013998_bib61","doi-asserted-by":"crossref","first-page":"3130","DOI":"10.1039\/C8CC00387D","article-title":"2-Oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2","volume":"54","author":"Abboud","year":"2018","journal-title":"Chem. Commun. (Camb.)"},{"key":"10.1074\/jbc.RA120.013998_bib62","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1042\/bj3070077","article-title":"Expression, purification and characterization of 1-aminocyclopropane-1-carboxylate oxidase from tomato in Escherichia coli","volume":"307","author":"Zhang","year":"1995","journal-title":"Biochem. J"},{"key":"10.1074\/jbc.RA120.013998_bib63","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-019-12711-7","article-title":"Aspartate\/asparagine-\u03b2-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern","volume":"10","author":"Pfeffer","year":"2019","journal-title":"Nat. Commun"},{"key":"10.1074\/jbc.RA120.013998_bib64","doi-asserted-by":"crossref","first-page":"4089","DOI":"10.1111\/j.1742-4658.2010.07804.x","article-title":"Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen","volume":"277","author":"Flashman","year":"2010","journal-title":"FEBS J"},{"key":"10.1074\/jbc.RA120.013998_bib65","doi-asserted-by":"crossref","first-page":"2253","DOI":"10.1021\/jacs.9b09236","article-title":"Mechanism of molecular oxygen diffusion in a hypoxia-sensing prolyl hydroxylase using multiscale simulation","volume":"142","author":"Domene","year":"2020","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA120.013998_bib66","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.jinorgbio.2013.05.006","article-title":"Substrate preference of the HIF-prolyl hydroxylase-2 (PHD2) and substrate-induced conformational change","volume":"126","author":"Pektas","year":"2013","journal-title":"J. Inorg. Biochem"},{"key":"10.1074\/jbc.RA120.013998_bib67","doi-asserted-by":"crossref","first-page":"2851","DOI":"10.1021\/bi501540c","article-title":"Increased turnover at limiting O2 concentrations by the Thr387 \u2192 Ala variant of HIF-prolyl hydroxylase PHD2","volume":"54","author":"Pektas","year":"2015","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013998_bib68","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/j.str.2015.01.014","article-title":"Structure of the ribosomal oxygenase OGFOD1 provides insights into the regio- and stereoselectivity of prolyl hydroxylases","volume":"23","author":"Horita","year":"2015","journal-title":"Structure"},{"key":"10.1074\/jbc.RA120.013998_bib69","doi-asserted-by":"crossref","first-page":"2405","DOI":"10.1016\/j.bmc.2019.01.018","article-title":"Inhibition of a viral prolyl hydroxylase","volume":"27","author":"Langley","year":"2019","journal-title":"Bioorg. Med. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib70","doi-asserted-by":"crossref","first-page":"6093","DOI":"10.1021\/acs.biochem.5b00789","article-title":"Structure and mechanism of a viral collagen prolyl hydroxylase","volume":"54","author":"Longbotham","year":"2015","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013998_bib71","doi-asserted-by":"crossref","first-page":"1802","DOI":"10.1074\/jbc.C200644200","article-title":"Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1\u03b1","volume":"278","author":"Elkins","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib72","doi-asserted-by":"crossref","first-page":"994","DOI":"10.1016\/j.jmb.2009.07.070","article-title":"Asparaginyl \u03b2-hydroxylation of proteins containing ankyrin repeat domains influences their stability and function","volume":"392","author":"Hardy","year":"2009","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib73","doi-asserted-by":"crossref","first-page":"7558","DOI":"10.1074\/jbc.M210385200","article-title":"Structure of human FIH-1 reveals a unique active site pocket and interaction sites for HIF-1 and von Hippel-Lindau","volume":"278","author":"Lee","year":"2003","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib74","doi-asserted-by":"crossref","first-page":"3808","DOI":"10.1074\/jbc.M707411200","article-title":"Kinetic rationale for selectivity toward N- and C-terminal oxygen-dependent degradation domain substrates mediated by a loop region of hypoxia-inducible factor prolyl hydroxylases","volume":"283","author":"Flashman","year":"2008","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib75","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1006\/jmbi.2001.4649","article-title":"Kinetic and crystallographic studies on deacetoxycephalosporin C synthase (DAOCS)","volume":"308","author":"Lee","year":"2001","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib76","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1038\/nature08617","article-title":"Cancer-associated IDH1 mutations produce 2-hydroxyglutarate","volume":"462","author":"Dang","year":"2009","journal-title":"Nature"},{"key":"10.1074\/jbc.RA120.013998_bib77","first-page":"215","article-title":"The effects of 2-hydroxyglutarate on the tumorigenesis of gliomas","volume":"22","author":"Reiter-Brennan","year":"2018","journal-title":"Contemp. Oncol. (Pozn.)"},{"key":"10.1074\/jbc.RA120.013998_bib78","doi-asserted-by":"crossref","first-page":"3293","DOI":"10.1074\/jbc.M608337200","article-title":"Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates","volume":"282","author":"Hewitson","year":"2007","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib79","first-page":"34","article-title":"Histone demethylases and their roles in cancer epigenetics","volume":"1","author":"D'Oto","year":"2016","journal-title":"J. Med. Oncol. Ther"},{"key":"10.1074\/jbc.RA120.013998_bib80","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.1016\/j.chembiol.2010.09.016","article-title":"Structural and mechanistic studies on \u03b3-butyrobetaine hydroxylase","volume":"17","author":"Leung","year":"2010","journal-title":"Chem. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib81","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/978-1-4939-7665-2_2","article-title":"Kinetic analysis of HIF prolyl hydroxylases","volume":"1742","author":"Koivunen","year":"2018","journal-title":"Methods Mol. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib82","doi-asserted-by":"crossref","first-page":"25098","DOI":"10.1074\/jbc.M112.355446","article-title":"The Skp1 protein from Toxoplasma is modified by a cytoplasmic prolyl 4-hydroxylase associated with oxygen sensing in the social amoeba dictyostelium","volume":"287","author":"Xu","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA120.013998_bib83","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1007946","article-title":"Toxoplasma F-box protein 1 is required for daughter cell scaffold function during parasite replication","volume":"15","author":"Baptista","year":"2019","journal-title":"PLoS Pathog"},{"key":"10.1074\/jbc.RA120.013998_bib84","doi-asserted-by":"crossref","first-page":"1527","DOI":"10.1021\/acs.biochem.0c00094","article-title":"Skp1 dimerization conceals its F-Box protein binding site","volume":"59","author":"Kim","year":"2020","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013998_bib85","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1021\/acs.biochem.7b01033","article-title":"Glycosylation promotes the random coil to helix transition in a region of a protist Skp1 associated with F-box binding","volume":"57","author":"Xu","year":"2018","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013998_bib86","doi-asserted-by":"crossref","first-page":"2483","DOI":"10.1021\/bi500086p","article-title":"Studies on deacetoxycephalosporin C synthase support a consensus mechanism for 2-oxoglutarate dependent oxygenases","volume":"53","author":"Tarhonskaya","year":"2014","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA120.013998_bib87","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1128\/CMR.05013-11","article-title":"Epidemiology of and diagnostic strategies for toxoplasmosis","volume":"25","author":"Robert-Gangneux","year":"2012","journal-title":"Clin. Microbiol. Rev"},{"key":"10.1074\/jbc.RA120.013998_bib88","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.jsb.2010.06.008","article-title":"High-throughput production of human proteins for crystallization: the SGC experience","volume":"172","author":"Savitsky","year":"2010","journal-title":"J. Struct. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib89","doi-asserted-by":"crossref","DOI":"10.1098\/rstb.2017.0071","article-title":"Inhibitors of both the N-methyl lysyl- and arginyl-demethylase activities of the JmjC oxygenases","volume":"373","author":"Bonnici","year":"2018","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci"},{"key":"10.1074\/jbc.RA120.013998_bib90","doi-asserted-by":"crossref","DOI":"10.1002\/0471142727.mb1025s88","article-title":"Preparation of proteins and peptides for mass spectrometry analysis in a bottom-up proteomics workflow","volume":"10","author":"Gundry","year":"2009","journal-title":"Curr. Protoc. Mol. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib91","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.chroma.2003.10.029","article-title":"Comparison of protein precipitation methods for sample preparation prior to proteomic analysis","volume":"1023","author":"Jiang","year":"2004","journal-title":"J. Chromatogr. A"},{"key":"10.1074\/jbc.RA120.013998_bib92","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1007\/978-1-59745-281-6_34","article-title":"Tryptic digestion of in-gel proteins for mass spectrometry analysis","volume":"519","author":"Huynh","year":"2009","journal-title":"Methods Mol. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib93","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.O111.013698","article-title":"Ultra high resolution linear ion trap Orbitrap mass spectrometer (Orbitrap Elite) facilitates top down LC MS\/MS and versatile peptide fragmentation modes","volume":"11","author":"Michalski","year":"2012","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1074\/jbc.RA120.013998_bib94","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1111\/j.1758-2229.2012.00368.x","article-title":"Peak Studio: a tool for the visualization and analysis of fragment analysis files","volume":"4","author":"McCafferty","year":"2012","journal-title":"Environ. Microbiol. Rep"},{"key":"10.1074\/jbc.RA120.013998_bib95","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1107\/S0907444909047374","article-title":"Integration, scaling, space-group assignment and post-refinement","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.013998_bib96","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"Xds","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.013998_bib97","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.013998_bib98","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1107\/S2059798319011471","article-title":"Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix","volume":"75","author":"Liebschner","year":"2019","journal-title":"Acta Crystallogr. D Struct. Biol"},{"key":"10.1074\/jbc.RA120.013998_bib99","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography & NMR system: a new software suite for macromolecular structure determination","volume":"54","author":"Br\u00fcnger","year":"1998","journal-title":"Acta Crystallogr. D Biol. Crystallogr"},{"key":"10.1074\/jbc.RA120.013998_bib100","doi-asserted-by":"crossref","first-page":"2728","DOI":"10.1038\/nprot.2007.406","article-title":"Version 1.2 of the Crystallography and NMR system","volume":"2","author":"Brunger","year":"2007","journal-title":"Nat. Protoc"},{"key":"10.1074\/jbc.RA120.013998_bib101","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":"10.1074\/jbc.RA120.013998_bib102","doi-asserted-by":"crossref","first-page":"13830","DOI":"10.1021\/jacs.7b07374","article-title":"Visualizing the reaction cycle in an iron(II)- and 2-(oxo)-glutarate-dependent hydroxylase","volume":"139","author":"Mitchell","year":"2017","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA120.013998_bib103","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.molcel.2005.09.003","article-title":"Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase","volume":"20","author":"Hao","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA120.013998_bib104","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.aap9714","article-title":"Phosphorylation decelerates conformational dynamics in bacterial translation elongation factors","volume":"4","author":"Talavera","year":"2018","journal-title":"Sci. Adv"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817504743?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925817504743?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA120.013998","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,31]],"date-time":"2021-12-31T17:19:51Z","timestamp":1640971191000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925817504743"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,12]]},"references-count":104,"journal-issue":{"issue":"49","published-print":{"date-parts":[[2020,12]]}},"alternative-id":["S0021925817504743"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra120.013998","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2020,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Biochemical and biophysical analyses of hypoxia sensing prolyl hydroxylases from Dictyostelium discoideum and Toxoplasma gondii","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA120.013998","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Liu et al.","name":"copyright","label":"Copyright"}]}}