{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,21]],"date-time":"2025-10-21T15:42:04Z","timestamp":1761061324322,"version":"build-2065373602"},"reference-count":61,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,4,1]],"date-time":"2021-04-01T00:00:00Z","timestamp":1617235200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,4,1]],"date-time":"2021-04-01T00:00:00Z","timestamp":1617235200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001871","name":"Funda\u00e7\u00e3o para a Ci\u00eancia e a Tecnologia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001871","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2021,4]]},"DOI":"10.1016\/j.biochi.2021.02.007","type":"journal-article","created":{"date-parts":[[2021,2,15]],"date-time":"2021-02-15T04:50:18Z","timestamp":1613364618000},"page":"78-88","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":12,"special_numbering":"C","title":["Structural and functional impact of clinically relevant E1\u03b1 variants causing pyruvate dehydrogenase complex deficiency"],"prefix":"10.1016","volume":"183","author":[{"given":"Hana","family":"Pavlu-Pereira","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Diana","family":"Lousa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Catarina S.","family":"Tom\u00e9","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cristina","family":"Florindo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria Jo\u00e3o","family":"Silva","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Isabel Tavares","family":"de Almeida","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paula","family":"Leandro","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Isabel","family":"Rivera","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jo\u00e3o B.","family":"Vicente","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2021.02.007_bib1","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.011597698","article-title":"The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes","volume":"98","author":"Zhou","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.biochi.2021.02.007_bib2","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1042\/BST0340217","article-title":"Regulation of the pyruvate dehydrogenase complex","author":"Patel","year":"2006","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.biochi.2021.02.007_bib3","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.str.2007.10.024","article-title":"Structures of the human pyruvate dehydrogenase complex cores: a highly conserved catalytic center with flexible N-terminal domains","volume":"16","author":"Yu","year":"2008","journal-title":"Structure"},{"key":"10.1016\/j.biochi.2021.02.007_bib4","doi-asserted-by":"crossref","first-page":"2325","DOI":"10.1021\/acs.biochem.8b00357","article-title":"Atomic structure of the E2 inner core of human pyruvate dehydrogenase complex","volume":"57","author":"Jiang","year":"2018","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2021.02.007_bib5","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1212\/WNL.49.6.1655","article-title":"Outcome of pyruvate dehydrogenase deficiency treated with ketogenic diets. Studies in patients with identical mutations","volume":"49","author":"Wexler","year":"1997","journal-title":"Neurology"},{"key":"10.1016\/j.biochi.2021.02.007_bib6","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1111\/j.1651-2227.1996.tb14104.x","article-title":"Pyruvate dehydrogenase deficiency in a child responsive to thiamine treatment","volume":"85","author":"Pastoris","year":"1996","journal-title":"Acta Paediatr. Int. J. Paediatr."},{"key":"10.1016\/j.biochi.2021.02.007_bib7","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1203\/01.PDR.0000057987.46622.64","article-title":"Differential effect of DCA treatment on the pyruvate dehydrogenase complex in patients with severe PDHC deficiency","volume":"53","author":"Fouque","year":"2003","journal-title":"Pediatr. Res."},{"key":"10.1016\/j.biochi.2021.02.007_bib8","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.3004986","article-title":"Phenylbutyrate therapy for pyruvate dehydrogenase complex deficiency and lactic acidosis","volume":"5","author":"Ferriero","year":"2013","journal-title":"Sci. Transl. Med."},{"key":"10.1016\/j.biochi.2021.02.007_bib9","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1111\/j.1432-1033.1987.tb13601.x","article-title":"Electron microscopic study on the size of pyruvate dehydrogenase complex in situ","volume":"169","author":"Sumegi","year":"1987","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.biochi.2021.02.007_bib10","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1002\/ijc.31812","article-title":"Microenvironmental control of glucose metabolism in tumors by regulation of pyruvate dehydrogenase","volume":"144","author":"Golias","year":"2019","journal-title":"Int. J. Canc."},{"key":"10.1016\/j.biochi.2021.02.007_bib11","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1007\/978-3-319-46503-6_19","article-title":"The pyruvate dehydrogenase complex and related assemblies in health and disease","author":"Byron","year":"2017","journal-title":"Subcell. Biochem."},{"key":"10.1016\/j.biochi.2021.02.007_bib12","doi-asserted-by":"crossref","first-page":"19772","DOI":"10.1074\/jbc.M601140200","article-title":"A\u00a0new level of architectural complexity in the human pyruvate dehydrogenase complex","volume":"281","author":"Smolle","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2021.02.007_bib13","doi-asserted-by":"crossref","first-page":"6277","DOI":"10.1021\/bi700083z","article-title":"Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex","volume":"46","author":"Seifert","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2021.02.007_bib14","doi-asserted-by":"crossref","first-page":"5587","DOI":"10.1093\/emboj\/cdf574","article-title":"Molecular architecture and mechanism of an icosahedral pyruvate dehydrogenase complex: a multifunctional catalytic machine","volume":"21","author":"Milne","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.biochi.2021.02.007_bib15","doi-asserted-by":"crossref","first-page":"13086","DOI":"10.1074\/jbc.M806563200","article-title":"Subunit and catalytic component stoichiometries of an in\u00a0vitro reconstituted human pyruvate dehydrogenase complex","volume":"284","author":"Brautigam","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2021.02.007_bib16","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1002\/humu.9319","article-title":"A\u00a0novel mutation in the dihydrolipoamide dehydrogenase E3 subunit gene (DLD) resulting in an atypical form of \u03b1-ketoglutarate dehydrogenase deficiency","volume":"25","author":"Odi\u00e8vre","year":"2005","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.biochi.2021.02.007_bib17","doi-asserted-by":"crossref","first-page":"7556","DOI":"10.1016\/S0021-9258(19)43864-7","article-title":"Rapid intersite transfer of acetyl groups and movement of pyruvate dehydrogenase component in the kidney pyruvate dehydrogenase complex","volume":"255","author":"Cate","year":"1980","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2021.02.007_bib18","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1046\/j.1432-1327.1998.2520045.x","article-title":"Kinetics and specificity of reductive acylation of wild-type and mutated lipoyl domains of 2-oxo-acid dehydrogenase complexes from Azotobacter vinelandii","volume":"252","author":"Berg","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.biochi.2021.02.007_bib19","doi-asserted-by":"crossref","first-page":"13204","DOI":"10.1074\/jbc.RA118.003996","article-title":"Pyruvate dehydrogenase complex deficiency is linked to regulatory loop disorder in the \u03b1V138M variant of human pyruvate dehydrogenase","volume":"293","author":"Whitley","year":"2018","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2021.02.007_bib20","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-020-18401-z","article-title":"Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex","volume":"11","author":"Forsberg","year":"2020","journal-title":"Nat. Commun."},{"key":"10.1016\/j.biochi.2021.02.007_bib21","doi-asserted-by":"crossref","DOI":"10.1093\/hmg\/ddz177","article-title":"Underlying molecular alterations in human dihydrolipoamide dehydrogenase deficiency revealed by structural analyses of disease-causing enzyme variants","author":"Szabo","year":"2019","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.biochi.2021.02.007_bib22","doi-asserted-by":"crossref","first-page":"5330","DOI":"10.1073\/pnas.86.14.5330","article-title":"Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit","volume":"86","author":"Ho","year":"1989","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.biochi.2021.02.007_bib23","doi-asserted-by":"crossref","first-page":"5731","DOI":"10.1074\/jbc.M007558200","article-title":"Probing the mechanism of inactivation of human pyruvate dehydrogenase by phosphorylation of three sites","volume":"276","author":"Korotchkina","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2021.02.007_bib24","doi-asserted-by":"crossref","first-page":"21240","DOI":"10.1074\/jbc.M300339200","article-title":"Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase","volume":"278","author":"Ciszak","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2021.02.007_bib25","doi-asserted-by":"crossref","first-page":"1849","DOI":"10.1016\/j.str.2008.10.010","article-title":"Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops","volume":"16","author":"Kato","year":"2008","journal-title":"Structure"},{"key":"10.1016\/j.biochi.2021.02.007_bib26","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1146\/annurev.genom.7.080505.115737","article-title":"Protein misfolding and human disease","volume":"7","author":"Gregersen","year":"2006","journal-title":"Annu. Rev. Genom. Hum. Genet."},{"key":"10.1016\/j.biochi.2021.02.007_bib27","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1007\/s10545-016-9923-3","article-title":"From structural biology to designing therapy for inborn errors of metabolism","volume":"39","author":"Yue","year":"2016","journal-title":"J.\u00a0Inherit. Metab. Dis."},{"key":"10.1016\/j.biochi.2021.02.007_bib28","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/j.ymgme.2012.03.017","article-title":"The spectrum of pyruvate dehydrogenase complex deficiency: clinical, biochemical and genetic features in 371 patients","volume":"106","author":"Patel","year":"2012","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.biochi.2021.02.007_bib29","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.ymgme.2011.08.008","article-title":"Molecular characterization of 82 patients with pyruvate dehydrogenase complex deficiency. Structural implications of novel amino acid substitutions in E1 protein","volume":"104","author":"Imbard","year":"2011","journal-title":"Mol. Genet. Metabol."},{"key":"10.1016\/j.biochi.2021.02.007_bib30","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1006\/abbi.1999.1231","article-title":"Characterization of point mutations in patients with pyruvate dehydrogenase deficiency: role of methionine- 181, proline-188, and arginine- 349 in the \u03b1 subunit","volume":"367","author":"Tripatara","year":"1999","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.biochi.2021.02.007_bib31","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1006\/abbi.2001.2576","article-title":"Differential effects of two mutations at arginine-234 in the \u03b1 subunit of human pyruvate dehydrogenase","volume":"395","author":"Jacobia","year":"2001","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.biochi.2021.02.007_bib32","doi-asserted-by":"crossref","first-page":"3009","DOI":"10.1007\/s00018-018-2775-2","article-title":"Folding and assembly defects of pyruvate dehydrogenase deficiency-related variants in the E1\u03b1 subunit of the pyruvate dehydrogenase complex","volume":"75","author":"Drakulic","year":"2018","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.biochi.2021.02.007_bib33","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1002\/(SICI)1098-1004(200003)15:3<209::AID-HUMU1>3.0.CO;2-K","article-title":"Mutations in the X-linked pyruvate dehydrogenase (E1) \u03b1 subunit gene (PDHA1) in patients with a pyruvate dehydrogenase complex deficiency","volume":"15","author":"Lissens","year":"2000","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.biochi.2021.02.007_bib34","doi-asserted-by":"crossref","DOI":"10.1186\/s13023-020-01586-3","article-title":"Pyruvate dehydrogenase complex deficiency: updating the clinical, metabolic and mutational landscapes in a cohort of Portuguese patients","volume":"15","author":"Pavlu-Pereira","year":"2020","journal-title":"Orphanet J. Rare Dis."},{"year":"1982","series-title":"Molecular Cloning: a Laboratory Manual","author":"Maniatis","key":"10.1016\/j.biochi.2021.02.007_bib35"},{"key":"10.1016\/j.biochi.2021.02.007_bib36","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1007\/s10545-013-9647-6","article-title":"Reduced response of Cystathionine Beta-Synthase (CBS) to S-Adenosylmethionine (SAM): identification and functional analysis of CBS gene mutations in Homocystinuria patients","volume":"37","author":"Mendes","year":"2014","journal-title":"J.\u00a0Inherit. Metab. Dis."},{"key":"10.1016\/j.biochi.2021.02.007_bib37","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A\u00a0rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.biochi.2021.02.007_bib38","doi-asserted-by":"crossref","first-page":"2212","DOI":"10.1038\/nprot.2007.321","article-title":"The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability","volume":"2","author":"Niesen","year":"2007","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.biochi.2021.02.007_bib39","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1002\/mgg3.94","article-title":"Functional and structural impact of the most prevalent missense mutations in classic galactosemia","volume":"2","author":"Coelho","year":"2014","journal-title":"Mol. Genet. Genom. Med."},{"key":"10.1016\/j.biochi.2021.02.007_bib40","doi-asserted-by":"crossref","first-page":"37223","DOI":"10.1074\/jbc.M103069200","article-title":"Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase","volume":"276","author":"Korotchkina","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2021.02.007_bib41","doi-asserted-by":"crossref","first-page":"W296","DOI":"10.1093\/nar\/gky427","article-title":"SWISS-MODEL: homology modelling of protein structures and complexes","volume":"46","author":"Waterhouse","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.biochi.2021.02.007_bib42","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/0010-4655(95)00042-E","article-title":"GROMACS: a message-passing parallel molecular dynamics implementation","volume":"91","author":"Berendsen","year":"1995","journal-title":"Comput. Phys. Commun."},{"key":"10.1016\/j.biochi.2021.02.007_bib43","doi-asserted-by":"crossref","first-page":"3696","DOI":"10.1021\/acs.jctc.5b00255","article-title":"ff14SB: improving the accuracy of protein side chain and backbone parameters from ff99SB","volume":"11","author":"Maier","year":"2015","journal-title":"J.\u00a0Chem. Theor. Comput."},{"key":"10.1016\/j.biochi.2021.02.007_bib44","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1063\/1.445869","article-title":"Comparison of simple potential functions for simulating liquid water","volume":"79","author":"Jorgensen","year":"1983","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.biochi.2021.02.007_bib45","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/j.jmgm.2005.12.005","article-title":"Automatic atom type and bond type perception in molecular mechanical calculations","volume":"25","author":"Wang","year":"2006","journal-title":"J.\u00a0Mol. Graph. Model."},{"key":"10.1016\/j.biochi.2021.02.007_bib46","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1002\/jcc.20035","article-title":"Development and testing of a general amber force field","volume":"25","author":"Wang","year":"2004","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.biochi.2021.02.007_bib47","doi-asserted-by":"crossref","first-page":"10269","DOI":"10.1021\/j100142a004","article-title":"A\u00a0well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model","volume":"97","author":"Bayly","year":"1993","journal-title":"J.\u00a0Phys. Chem."},{"year":"2009","series-title":"Gaussian 09 Revision A.1","author":"Frisch","key":"10.1016\/j.biochi.2021.02.007_bib48"},{"key":"10.1016\/j.biochi.2021.02.007_bib49","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: an N\u00b7log(N) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.biochi.2021.02.007_bib50","article-title":"Canonical sampling through velocity rescaling","volume":"126","author":"Bussi","year":"2007","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.biochi.2021.02.007_bib51","doi-asserted-by":"crossref","first-page":"7182","DOI":"10.1063\/1.328693","article-title":"Polymorphic transitions in single crystals: a new molecular dynamics method","volume":"52","author":"Parrinello","year":"1981","journal-title":"J.\u00a0Appl. Phys."},{"key":"10.1016\/j.biochi.2021.02.007_bib52","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H","article-title":"LINCS: a linear constraint solver for molecular simulations","volume":"18","author":"Hess","year":"1997","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.biochi.2021.02.007_bib53","doi-asserted-by":"crossref","first-page":"952","DOI":"10.1002\/jcc.540130805","article-title":"Settle: an analytical version of the SHAKE and RATTLE algorithm for rigid water models","volume":"13","author":"Miyamoto","year":"1992","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.biochi.2021.02.007_bib54","doi-asserted-by":"crossref","first-page":"13615","DOI":"10.1038\/s41598-019-49944-x","article-title":"Structure of full-length wild-type human phenylalanine hydroxylase by small angle X-ray scattering reveals substrate-induced conformational stability","volume":"9","author":"Tom\u00e9","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.biochi.2021.02.007_bib55","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1038\/s41598-018-36994-w","article-title":"Screening pyridine derivatives against human hydrogen sulfide-synthesizing enzymes by orthogonal methods","volume":"9","author":"Zuhra","year":"2019","journal-title":"Sci. Rep."},{"key":"10.1016\/j.biochi.2021.02.007_bib56","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1007\/s00431-008-0700-7","article-title":"Pyruvate dehydrogenase deficiency: identification of a novel mutation in the PDHA1 gene which responds to amino acid supplementation","volume":"168","author":"Silva","year":"2009","journal-title":"Eur. J. Pediatr."},{"key":"10.1016\/j.biochi.2021.02.007_bib57","doi-asserted-by":"crossref","first-page":"12775","DOI":"10.1021\/bi061582l","article-title":"Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation","volume":"45","author":"Seifert","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2021.02.007_bib58","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1016\/0006-291X(72)90684-5","article-title":"Function of the nonidentical subunits of mammalian pyruvate dehydrogenase","volume":"48","author":"Roche","year":"1972","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2021.02.007_bib59","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1002\/humu.1380030210","article-title":"Pyruvate dehydrogenase deficiency in a male caused by a point mutation (F205L) in the E1\u03b1 subunit","volume":"3","author":"Dahl","year":"1994","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.biochi.2021.02.007_bib60","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/S0925-4439(02)00142-4","article-title":"Thiamine-responsive pyruvate dehydrogenase deficiency in two patients caused by a point mutation (F205L and L216F) within the thiamine pyrophosphate binding region","volume":"1588","author":"Naito","year":"2002","journal-title":"Biochim. Biophys. Acta (BBA) - Mol. Basis Dis."},{"key":"10.1016\/j.biochi.2021.02.007_bib61","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1007\/s10545-014-9712-9","article-title":"Defects of thiamine transport and metabolism","volume":"37","author":"Brown","year":"2014","journal-title":"J.\u00a0Inherit. Metab. Dis."}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908421000432?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908421000432?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:17:11Z","timestamp":1759540631000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908421000432"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,4]]},"references-count":61,"alternative-id":["S0300908421000432"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2021.02.007","relation":{},"ISSN":["0300-9084"],"issn-type":[{"type":"print","value":"0300-9084"}],"subject":[],"published":{"date-parts":[[2021,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural and functional impact of clinically relevant E1\u03b1 variants causing pyruvate dehydrogenase complex deficiency","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2021.02.007","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier B.V. and Soci\u00e9t\u00e9 Fran\u00e7aise de Biochimie et Biologie Mol\u00e9culaire (SFBBM). All rights reserved.","name":"copyright","label":"Copyright"}]}}