{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T08:50:44Z","timestamp":1785919844518,"version":"3.56.0"},"reference-count":47,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,12,10]],"date-time":"2025-12-10T00:00:00Z","timestamp":1765324800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100013578","name":"Abraham Lincoln Brigade Archives","doi-asserted-by":"publisher","award":["2022086950"],"award-info":[{"award-number":["2022086950"]}],"id":[{"id":"10.13039\/100013578","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100013578","name":"Abraham Lincoln Brigade Archives","doi-asserted-by":"publisher","award":["2023087670"],"award-info":[{"award-number":["2023087670"]}],"id":[{"id":"10.13039\/100013578","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100013578","name":"Abraham Lincoln Brigade Archives","doi-asserted-by":"publisher","award":["2021085252"],"award-info":[{"award-number":["2021085252"]}],"id":[{"id":"10.13039\/100013578","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001671","name":"European Synchrotron Radiation Facility","doi-asserted-by":"publisher","award":["MX2281"],"award-info":[{"award-number":["MX2281"]}],"id":[{"id":"10.13039\/501100001671","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001671","name":"European Synchrotron Radiation Facility","doi-asserted-by":"publisher","award":["MX2454"],"award-info":[{"award-number":["MX2454"]}],"id":[{"id":"10.13039\/501100001671","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001671","name":"European Synchrotron Radiation Facility","doi-asserted-by":"publisher","award":["MX2527"],"award-info":[{"award-number":["MX2527"]}],"id":[{"id":"10.13039\/501100001671","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001671","name":"European Synchrotron Radiation Facility","doi-asserted-by":"publisher","award":["MX2353"],"award-info":[{"award-number":["MX2353"]}],"id":[{"id":"10.13039\/501100001671","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100014440","name":"Spain Ministry of Science Innovation and Universities","doi-asserted-by":"publisher","award":["PID2020-116261GB-I00\/AEI\/10.13039\/501100011033"],"award-info":[{"award-number":["PID2020-116261GB-I00\/AEI\/10.13039\/501100011033"]}],"id":[{"id":"10.13039\/100014440","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002924","name":"Federaci\u00f3n Espa\u00f1ola de Enfermedades Raras","doi-asserted-by":"publisher","award":["C-EXP-120-UGR23"],"award-info":[{"award-number":["C-EXP-120-UGR23"]}],"id":[{"id":"10.13039\/501100002924","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004837","name":"Ministerio de Ciencia e Innovaci\u00f3n","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004837","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2026,1]]},"DOI":"10.1016\/j.ijbiomac.2025.149491","type":"journal-article","created":{"date-parts":[[2025,12,5]],"date-time":"2025-12-05T08:03:44Z","timestamp":1764921824000},"page":"149491","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"P1","title":["New human bisphosphoglycerate mutase structures provide insights into the structural basis of BPGM deficiency and citrate inhibition"],"prefix":"10.1016","volume":"338","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6675-1550","authenticated-orcid":false,"given":"Sergio","family":"Mart\u00ednez-Rodr\u00edguez","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jes\u00fas M.","family":"Torres","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pilar","family":"S\u00e1nchez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Esperanza","family":"Ortega","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos\u00e9 Antonio","family":"Gavira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"3","key":"10.1016\/j.ijbiomac.2025.149491_bb0005","doi-asserted-by":"crossref","DOI":"10.1111\/apha.14081","article-title":"Erythrocyte metabolism","volume":"240","author":"Chatzinikolaou","year":"2024","journal-title":"Acta Physiol (Oxford)"},{"issue":"13","key":"10.1016\/j.ijbiomac.2025.149491_bb0010","doi-asserted-by":"crossref","first-page":"4034","DOI":"10.1182\/blood-2005-04-1622","article-title":"The energy-less red blood cell is lost: erythrocyte enzyme abnormalities of glycolysis","volume":"106","author":"Van Wijk","year":"2005","journal-title":"Blood"},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.149491_bb0015","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/S0021-9258(19)51175-9","article-title":"The formation of 2,3-diphosphoglycerate in rabbit erythrocytes: the existence of a diphosphoglycerate mutase","volume":"183","author":"Rapoport","year":"1950","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.149491_bb0020","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1042\/bj1540449","article-title":"The regulatory principles of glycolysis in erythrocytes in vivo and in vitro. A minimal comprehensive model describing steady states, quasi-steady states and time-dependent processes","volume":"154","author":"Rapoport","year":"1976","journal-title":"Biochem. J."},{"key":"10.1016\/j.ijbiomac.2025.149491_bb0025","series-title":"Hemoglobin. Essentials of Medical Biochemistry","first-page":"355","volume":"vol. Jan 1","author":"Bhagavan","year":"2011"},{"issue":"9","key":"10.1016\/j.ijbiomac.2025.149491_bb0030","doi-asserted-by":"crossref","first-page":"3593","DOI":"10.1073\/pnas.91.9.3593","article-title":"A recombinant bisphosphoglycerate mutase variant with acid phosphatase homology degrades 2,3-diphosphoglycerate","volume":"vol. 91","author":"Garel","year":"1994","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"issue":"8","key":"10.1016\/j.ijbiomac.2025.149491_bb0035","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1002\/ajh.25150","article-title":"Genotype-phenotype correlation of hereditary erythrocytosis mutations, a single center experience","volume":"93","author":"Oliveira","year":"2018","journal-title":"Am. J. Hematol."},{"issue":"5","key":"10.1016\/j.ijbiomac.2025.149491_bb0040","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.3324\/haematol.2021.280516","article-title":"Erythrocytosis associated with EPAS1(HIF2A), EGLN1(PHD2), VHL, EPOR or BPGM mutations: the Mayo Clinic experience","volume":"107","author":"Gangat","year":"2022","journal-title":"Haematologica"},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.149491_bb0045","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1002\/ajh.20014","article-title":"Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency","volume":"75","author":"Hoyer","year":"2004","journal-title":"Am. J. Hematol."},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.149491_bb0050","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1111\/bjh.18485","article-title":"Heterozygosity for bisphosphoglycerate mutase deficiency expressing clinically as congenital erythrocytosis: a case series and literature review","volume":"200","author":"van Dijk","year":"2023","journal-title":"Br. J. Haematol."},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.149491_bb0055","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1002\/humu.22448","article-title":"Genetic basis of congenital erythrocytosis: mutation update and online databases","volume":"35","author":"Bento","year":"2014","journal-title":"Hum. Mutat."},{"issue":"10","key":"10.1016\/j.ijbiomac.2025.149491_bb0060","doi-asserted-by":"crossref","first-page":"e201","DOI":"10.3324\/haematol.2014.109306","article-title":"Erythrocytosis associated with a novel missense mutation in the BPGM gene","volume":"99","author":"Petousi","year":"2014","journal-title":"Haematologica"},{"issue":"14","key":"10.1016\/j.ijbiomac.2025.149491_bb0065","doi-asserted-by":"crossref","first-page":"7837","DOI":"10.1016\/S0021-9258(18)83118-0","article-title":"Isolation, characterization, and structure of a mutant 89 Arg \u2192 Cys bisphosphoglycerate mutase","volume":"264","author":"Rosa","year":"1989","journal-title":"J. Biol. Chem."},{"issue":"11","key":"10.1016\/j.ijbiomac.2025.149491_bb0070","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.3324\/haematol.2016.144063","article-title":"Gene panel sequencing improves the diagnostic work-up of patients with idiopathic erythrocytosis and identifies new mutations","volume":"101","author":"Camps","year":"2016","journal-title":"Haematologica"},{"issue":"10","key":"10.1016\/j.ijbiomac.2025.149491_bb0075","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1038\/nchembio.2453","article-title":"Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate","volume":"13","author":"Oslund","year":"2017","journal-title":"Nat. Chem. Biol."},{"issue":"3","key":"10.1016\/j.ijbiomac.2025.149491_bb0080","doi-asserted-by":"crossref","DOI":"10.1016\/j.tmrv.2023.150748","article-title":"Biphosphoglycerate mutase: a novel therapeutic target for malaria?","volume":"37","author":"Azzuolo","year":"2023","journal-title":"Transfus. Med. Rev."},{"key":"10.1016\/j.ijbiomac.2025.149491_bb0085","first-page":"51","article-title":"Novel Bis-phosphoglycerate mutase modulators for treating sickle cell disease","volume":"13","author":"Sabnis","year":"2022","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ijbiomac.2025.149491_bb0090","series-title":"WO2022056449A1 - Compounds as Modulators of Bis-Phosphoglycerate Mutase for the Treatment of Sickle Cell Disease","year":"2022"},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.149491_bb0095","doi-asserted-by":"crossref","DOI":"10.1111\/apha.14242","article-title":"Beyond hemoglobin: critical role of 2,3-bisphosphoglycerate mutase in kidney function and injury","volume":"241","author":"Kulow","year":"2025","journal-title":"Acta Physiol (Oxford)"},{"issue":"37","key":"10.1016\/j.ijbiomac.2025.149491_bb0100","doi-asserted-by":"crossref","first-page":"39132","DOI":"10.1074\/jbc.M405982200","article-title":"Crystal structure of human bisphosphoglycerate mutase","volume":"279","author":"Wang","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"51","key":"10.1016\/j.ijbiomac.2025.149491_bb0105","doi-asserted-by":"crossref","first-page":"39642","DOI":"10.1074\/jbc.M606421200","article-title":"Seeing the process of histidine phosphorylation in human Bisphosphoglycerate mutase","volume":"281","author":"Wang","year":"2006","journal-title":"J. Biol. Chem."},{"issue":"Pt 11","key":"10.1016\/j.ijbiomac.2025.149491_bb0110","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1107\/S1744309110035475","article-title":"Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding","volume":"66","author":"Patterson","year":"2010","journal-title":"Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun."},{"issue":"Pt 4","key":"10.1016\/j.ijbiomac.2025.149491_bb0115","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1107\/S2059798322001802","article-title":"Molecular insight into 2-phosphoglycolate activation of the phosphatase activity of bisphosphoglycerate mutase","volume":"78","author":"Aljahdali","year":"2022","journal-title":"Acta crystallographica. Section D, Structural biology."},{"issue":"9","key":"10.1016\/j.ijbiomac.2025.149491_bb0120","doi-asserted-by":"crossref","first-page":"3946","DOI":"10.1039\/c3cp53935k","article-title":"Insights into the phosphatase and the synthase activities of human bisphosphoglycerate mutase: a quantum mechanics\/molecular mechanics simulation","volume":"16","author":"Chu","year":"2014","journal-title":"Phys. Chem. Chem. Phys."},{"key":"10.1016\/j.ijbiomac.2025.149491_bb0125","first-page":"211","article-title":"The enzymology of 2,3-bisphosphoglycerate","volume":"51","author":"Rose","year":"1980","journal-title":"Adv. Enzymol. Relat. Areas Mol. Biol."},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.149491_bb0130","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1042\/BJ20071097","article-title":"The histidine phosphatase superfamily: structure and function","volume":"409","author":"Rigden","year":"2008","journal-title":"Biochem. J."},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.149491_bb0135","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1016\/j.bbrc.2005.03.243","article-title":"Crystal structure of human B-type phosphoglycerate mutase bound with citrate","volume":"331","author":"Wang","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"Pt 3","key":"10.1016\/j.ijbiomac.2025.149491_bb0140","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1042\/BJ20040752","article-title":"6-Phosphofructo-2-kinase\/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis","volume":"381","author":"Rider","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.ijbiomac.2025.149491_bb0145","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.ijbiomac.2021.02.153","article-title":"Structural analysis of EhPSP in complex with 3-phosphoglyceric acid from Entamoeba histolytica reveals a basis for its lack of phosphoglycerate mutase activity","volume":"178","author":"Kumari","year":"2021","journal-title":"Int. J. Biol. Macromol."},{"issue":"22","key":"10.1016\/j.ijbiomac.2025.149491_bb0150","doi-asserted-by":"crossref","first-page":"14045","DOI":"10.1074\/jbc.272.22.14045","article-title":"Critical role of human bisphosphoglycerate mutase Cys22 in the phosphatase activator-binding site","volume":"272","author":"Ravel","year":"1997","journal-title":"J. Biol. Chem."},{"issue":"10","key":"10.1016\/j.ijbiomac.2025.149491_bb0155","doi-asserted-by":"crossref","first-page":"2778","DOI":"10.1021\/ci200227u","article-title":"LigPlot+: multiple ligand-protein interaction diagrams for drug discovery","volume":"51","author":"Laskowski","year":"2011","journal-title":"J. Chem. Inf. Model."},{"issue":"14 S","key":"10.1016\/j.ijbiomac.2025.149491_bb0160","doi-asserted-by":"crossref","first-page":"S50","DOI":"10.1002\/mus.880181412","article-title":"Molecular genetic studies in muscle phosphoglycerate mutase (PGAM-M) deficiency","volume":"3","author":"Tsujino","year":"1995","journal-title":"Muscle Nerve Suppl."},{"issue":"4","key":"10.1016\/j.ijbiomac.2025.149491_bb0165","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1515\/hsz-2013-0271","article-title":"Citrate--new functions for an old metabolite","volume":"395","author":"Iacobazzi","year":"2014","journal-title":"Biol. Chem."},{"issue":"9","key":"10.1016\/j.ijbiomac.2025.149491_bb0170","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1111\/j.1537-2995.2006.00893.x","article-title":"Storage of red blood cells with improved maintenance of 2,3-bisphosphoglycerate","volume":"46","author":"H\u00f6gman","year":"2006","journal-title":"Transfusion"},{"key":"10.1016\/j.ijbiomac.2025.149491_bb0175","doi-asserted-by":"crossref","first-page":"3232","DOI":"10.1016\/S0021-9258(18)63045-5","article-title":"2,3-diphosphoglycerate phosphatase from human erythrocytes. General properties and activation by anions - PubMed","volume":"245","author":"Rose","year":"1970","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.ijbiomac.2025.149491_bb0180","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1007\/s40291-024-00703-3","article-title":"Diagnostic approaches to investigate JAK2-unmutated erythrocytosis based on a single tertiary center experience","volume":"28","author":"Lee","year":"2024","journal-title":"Mol. Diagn. Ther."},{"issue":"12","key":"10.1016\/j.ijbiomac.2025.149491_bb0185","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2020.108170","article-title":"Bisphosphoglycerate mutase deficiency protects against cerebral malaria and severe malaria-induced anemia","volume":"32","author":"Xu","year":"2020","journal-title":"Cell Rep."},{"issue":"Pt 2","key":"10.1016\/j.ijbiomac.2025.149491_bb0190","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."},{"issue":"Pt 7","key":"10.1016\/j.ijbiomac.2025.149491_bb0195","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1107\/S0907444913000061","article-title":"How good are my data and what is the resolution?","volume":"69","author":"Evans","year":"2013","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"Pt 6","key":"10.1016\/j.ijbiomac.2025.149491_bb0200","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1107\/S2059798323003595","article-title":"The CCP4 suite: integrative software for macromolecular crystallography","volume":"79","author":"Agirre","year":"2023","journal-title":"Acta crystallographica. Section D, Structural biology."},{"issue":"Pt 1","key":"10.1016\/j.ijbiomac.2025.149491_bb0205","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."},{"issue":"Pt 10","key":"10.1016\/j.ijbiomac.2025.149491_bb0210","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 crystallographica. Section D, Structural biology."},{"issue":"Pt 4","key":"10.1016\/j.ijbiomac.2025.149491_bb0215","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov","year":"2011","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"Pt 4","key":"10.1016\/j.ijbiomac.2025.149491_bb0220","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."},{"issue":"Pt 4","key":"10.1016\/j.ijbiomac.2025.149491_bb0225","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1107\/S0907444906005270","article-title":"Optimal description of a protein structure in terms of multiple groups undergoing TLS motion","volume":"62","author":"Painter","year":"2006","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.149491_bb0230","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1002\/pro.3330","article-title":"MolProbity: more and better reference data for improved all-atom structure validation","volume":"27","author":"Williams","year":"2018","journal-title":"Protein science\u202f: a publication of the Protein Society."},{"issue":"1","key":"10.1016\/j.ijbiomac.2025.149491_bb0235","doi-asserted-by":"crossref","DOI":"10.1186\/1471-2105-13-173","article-title":"Defining and searching for structural motifs using DeepView\/Swiss-PdbViewer","volume":"13","author":"Johansson","year":"2012","journal-title":"BMC bioinformatics."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025100482?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025100482?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,8,5]],"date-time":"2026-08-05T08:26:57Z","timestamp":1785918417000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813025100482"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,1]]},"references-count":47,"alternative-id":["S0141813025100482"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.149491","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2026,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"New human bisphosphoglycerate mutase structures provide insights into the structural basis of BPGM deficiency and citrate inhibition","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.149491","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"149491"}}