{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T16:23:30Z","timestamp":1790871810587,"version":"4.1.0"},"reference-count":51,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2011,7,1]],"date-time":"2011-07-01T00:00:00Z","timestamp":1309478400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2011,7,1]],"date-time":"2011-07-01T00:00:00Z","timestamp":1309478400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,6,8]],"date-time":"2022-06-08T00:00:00Z","timestamp":1654646400000},"content-version":"vor","delay-in-days":3995,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","exphem.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Experimental Hematology"],"published-print":{"date-parts":[[2011,7]]},"DOI":"10.1016\/j.exphem.2011.05.003","type":"journal-article","created":{"date-parts":[[2011,5,12]],"date-time":"2011-05-12T12:47:42Z","timestamp":1305204462000},"page":"784-794","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":45,"title":["Abnormal mitoferrin-1 expression in patients with erythropoietic protoporphyria"],"prefix":"10.1016","volume":"39","author":[{"given":"Yongming","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nathaniel B.","family":"Langer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"George C.","family":"Shaw","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guang","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liangtao","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jerry","family":"Kaplan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barry H.","family":"Paw","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph R.","family":"Bloomer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.exphem.2011.05.003_bib1","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1186\/1750-1172-4-19","article-title":"Erythropoietic protoporphyria","volume":"4","author":"Lecha","year":"2009","journal-title":"Orphanet J Rare Dis"},{"key":"10.1016\/j.exphem.2011.05.003_bib2","first-page":"148","article-title":"Molecular and cellular mechanisms of porphyrin photosensitization","volume":"3","author":"Poh-Fitzpatrick","year":"1986","journal-title":"Photodermatology"},{"key":"10.1016\/j.exphem.2011.05.003_bib3","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1067\/mjd.2000.107498","article-title":"Vascular changes in erythropoietic protoporphyria: histopathologic and immunohistochemical study","volume":"43","author":"Timonen","year":"2000","journal-title":"J Am Acad Dermatol"},{"key":"10.1016\/j.exphem.2011.05.003_bib4","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1016\/0002-9343(75)90644-0","article-title":"Hepatic disease in erythropoietic protoporphyria","volume":"58","author":"Bloomer","year":"1975","journal-title":"Am J Med"},{"key":"10.1016\/j.exphem.2011.05.003_bib5","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/S0009-9120(89)80081-5","article-title":"Hepatobiliary implications and complications in protoporphyria, a 20 year study","volume":"22","author":"Doss","year":"1989","journal-title":"Clin Biochem"},{"key":"10.1016\/j.exphem.2011.05.003_bib6","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1172\/JCI110046","article-title":"Protoporphyrin-induced cholestasis in the isolated in situ perfused rat liver","volume":"67","author":"Avner","year":"1981","journal-title":"J Clin Invest"},{"key":"10.1016\/j.exphem.2011.05.003_bib7","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1002\/hep.1840110316","article-title":"Early involvement of hepatic parenchymal cells in erythrohepatic protoporphyria? An ultrastructural study of patients with and without overt liver disease and the effect of chenodeoxycholic acid treatment","volume":"11","author":"Rademakers","year":"1990","journal-title":"Hepatology"},{"key":"10.1016\/j.exphem.2011.05.003_bib8","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1016\/S0016-5085(99)70464-6","article-title":"Biliary fibrosis associated with altered bile composition in a mouse model of erythropoietic protoporphyria","volume":"117","author":"Meerman","year":"1999","journal-title":"Gastroenterology"},{"key":"10.1016\/j.exphem.2011.05.003_bib9","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1007\/s007950000005","article-title":"An ultrastructural study of the liver in erythropoietic protoporphyria","volume":"33","author":"Komatsu","year":"2000","journal-title":"Med Electron Microsc"},{"key":"10.1016\/j.exphem.2011.05.003_bib10","doi-asserted-by":"crossref","first-page":"1590","DOI":"10.1002\/lt.20620","article-title":"Liver transplantation for erythropoietic protoporphyria liver disease","volume":"11","author":"McGuire","year":"2005","journal-title":"Liver Transplant"},{"key":"10.1016\/j.exphem.2011.05.003_bib11","first-page":"126","article-title":"Diminished erythroid ferrochelatase activity in protoporphyria","volume":"86","author":"Bottomley","year":"1975","journal-title":"J Lab Clin Med"},{"key":"10.1016\/j.exphem.2011.05.003_bib12","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1172\/JCI108189","article-title":"Heme synthetase deficiency in human protoporphyria. Demonstration of the defect in liver and cultured skin fibroblasts","volume":"56","author":"Bonkovsky","year":"1975","journal-title":"J Clin Invest"},{"key":"10.1016\/j.exphem.2011.05.003_bib13","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1172\/JCI106474","article-title":"Erythropoietic protoporphyria: evidence for multiple sites of excess protoporphyrin formation","volume":"50","author":"Scholnick","year":"1971","journal-title":"J\u00a0Clin Invest"},{"key":"10.1016\/j.exphem.2011.05.003_bib14","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1016\/S0016-5085(85)80085-8","article-title":"Protoporphyrin metabolic balance in human protoporphyria","volume":"88","author":"Poh-Fitzpatrick","year":"1985","journal-title":"Gastroenterology"},{"key":"10.1016\/j.exphem.2011.05.003_bib15","doi-asserted-by":"crossref","first-page":"1909","DOI":"10.1007\/PL00000672","article-title":"Ferrochelatase at the millennium: structures, mechanisms and [2Fe-2S] clusters","volume":"57","author":"Dailey","year":"2000","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.exphem.2011.05.003_bib16","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/84152","article-title":"The 2A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis","volume":"18","author":"Wu","year":"2001","journal-title":"Nat Struct Biol"},{"key":"10.1016\/j.exphem.2011.05.003_bib17","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1016\/S0006-291X(05)80099-3","article-title":"Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase","volume":"173","author":"Nakahashi","year":"1990","journal-title":"Biochem Biophys Res Comm"},{"key":"10.1016\/j.exphem.2011.05.003_bib18","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1111\/j.1432-1033.1992.tb16771.x","article-title":"Structure of the human ferrochelatase gene","volume":"205","author":"Taketani","year":"1992","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.exphem.2011.05.003_bib19","first-page":"187","article-title":"Screening for ferrochelatase mutations: molecular heterogeneity of erythropoietic protoporphyria","volume":"1225","author":"Wang","year":"1994","journal-title":"Biochem Biophys Acta"},{"key":"10.1016\/j.exphem.2011.05.003_bib20","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1086\/301870","article-title":"Systematic analysis of molecular defects in the ferrochelatase gene from patients with erythropoietic protoporphyria","volume":"62","author":"Rufenacht","year":"1998","journal-title":"Am J Hum Genet"},{"key":"10.1016\/j.exphem.2011.05.003_bib21","doi-asserted-by":"crossref","first-page":"3980","DOI":"10.1182\/blood.V91.10.3980","article-title":"Examination of ferrochelatase mutations that cause erythropoietic protoporphyria","volume":"91","author":"Sellers","year":"1998","journal-title":"Blood"},{"key":"10.1016\/j.exphem.2011.05.003_bib22","doi-asserted-by":"crossref","first-page":"2105","DOI":"10.1182\/blood.V93.6.2105.406k28_2105_2110","article-title":"Inheritance in erythropoietic protoporphyria: a common wild-type ferrochelatase allelic variant with low expression accounts for clinical manifestation","volume":"93","author":"Gouya","year":"1999","journal-title":"Blood"},{"key":"10.1016\/j.exphem.2011.05.003_bib23","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1038\/ng809","article-title":"The penetrance of dominant erythropoietic protoporphyria is modulated by expression of wildtype FECH","volume":"30","author":"Gouya","year":"2002","journal-title":"Nat Genet"},{"key":"10.1016\/j.exphem.2011.05.003_bib24","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.ymgme.2003.07.001","article-title":"Genotypic determinants of phenotype in North American patients with erythropoietic protoporphyria","volume":"80","author":"Risheg","year":"2003","journal-title":"Mol Genet Metab"},{"key":"10.1016\/j.exphem.2011.05.003_bib25","doi-asserted-by":"crossref","first-page":"2790","DOI":"10.1038\/sj.jid.5700924","article-title":"Gene dosage analysis identifies large deletions of FECH gene in 10% of families with erythropoietic protoporphyria","volume":"127","author":"Whatley","year":"2007","journal-title":"J\u00a0Invest Dermatol"},{"key":"10.1016\/j.exphem.2011.05.003_bib26","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1016\/j.ajhg.2008.08.003","article-title":"C-terminal deletions in the ALAS2 gene lead to gain of function and cause x-linked dominant protoporphyria without anemia or iron overload","volume":"83","author":"Whatley","year":"2008","journal-title":"Am J Hum Genet"},{"key":"10.1016\/j.exphem.2011.05.003_bib27","doi-asserted-by":"crossref","first-page":"3274","DOI":"10.1182\/blood-2002-04-1212","article-title":"Involvement of ABC7 in the biosynthesis of heme in erythroid cells: interaction of ABC7 with ferrochelatase","volume":"101","author":"Taketani","year":"2003","journal-title":"Blood"},{"key":"10.1016\/j.exphem.2011.05.003_bib28","doi-asserted-by":"crossref","first-page":"1562","DOI":"10.1172\/JCI24141","article-title":"Heme-regulated eIF2-kinase modifies the phenotypic severity of murine models of erythropoietic protoporphyria and B-thalassemia","volume":"115","author":"Han","year":"2005","journal-title":"J Clin Invest"},{"key":"10.1016\/j.exphem.2011.05.003_bib29","doi-asserted-by":"crossref","first-page":"1084","DOI":"10.1182\/blood-2004-12-4703","article-title":"Microcytic anemia, erythropoietic protoporphyria and neurodegeration in mice with targeted deletion of iron-regulatory protein 2","volume":"106","author":"Cooperman","year":"2005","journal-title":"Blood"},{"key":"10.1016\/j.exphem.2011.05.003_bib30","doi-asserted-by":"crossref","first-page":"2580","DOI":"10.1182\/blood-2005-04-1365","article-title":"Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)","volume":"106","author":"Galy","year":"2005","journal-title":"Blood"},{"key":"10.1016\/j.exphem.2011.05.003_bib31","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1038\/nature04512","article-title":"Mitoferrin is essential for erythroid iron assimilation","volume":"440","author":"Shaw","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.exphem.2011.05.003_bib32","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1182\/blood-2009-12-259614","article-title":"Ferrochelatase forms an oligomeric complex with mitoferrin1 and Abcb10 for erythroid heme biosynthesis","volume":"116","author":"Chen","year":"2010","journal-title":"Blood"},{"key":"10.1016\/j.exphem.2011.05.003_bib33","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1172\/JCI1347","article-title":"Molecular defects in ferrochelatase in patients with protoporphyria requiring liver transplantation","volume":"102","author":"Bloomer","year":"1998","journal-title":"J Clin Invest"},{"key":"10.1016\/j.exphem.2011.05.003_bib34","first-page":"83","article-title":"Ferrochelatase gene mutations in erythropoietic protoporphyria: focus on liver disease","volume":"48","author":"Chen","year":"2002","journal-title":"Cell Mol Biol"},{"key":"10.1016\/j.exphem.2011.05.003_bib35","doi-asserted-by":"crossref","first-page":"33653","DOI":"10.1074\/jbc.M403146200","article-title":"A mitochondrial-vacuolar signaling pathway in yeast that affects iron and copper metabolism","volume":"279","author":"Li","year":"2004","journal-title":"J Biol Chem"},{"key":"10.1016\/j.exphem.2011.05.003_bib36","doi-asserted-by":"crossref","first-page":"16263","DOI":"10.1073\/pnas.0904519106","article-title":"Abcb10 physically interacts with mitoferrin1 (Slc25a37) to enhance its stability and function in the erythroid mitochondria","volume":"106","author":"Chen","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.exphem.2011.05.003_bib37","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1182\/blood-2007-01-068940","article-title":"Regulated Fox-2 isoform expression mediates protein 4.1R splicing during erythroid differentiation","volume":"111","author":"Yang","year":"2008","journal-title":"Blood"},{"key":"10.1016\/j.exphem.2011.05.003_bib38","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1002\/iub.139","article-title":"Transport proteins (carriers) of mitochondria","volume":"61","author":"Wohlrab","year":"2009","journal-title":"IUBMB Life"},{"key":"10.1016\/j.exphem.2011.05.003_bib39","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1128\/MCB.01685-08","article-title":"Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2","volume":"29","author":"Paradkar","year":"2009","journal-title":"Mol Cell Biol"},{"key":"10.1016\/j.exphem.2011.05.003_bib40","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1038\/ng1403","article-title":"Nonsense-mediated decay approaches the clinic","volume":"36","author":"Holbrook","year":"2004","journal-title":"Nat Genet"},{"key":"10.1016\/j.exphem.2011.05.003_bib41","doi-asserted-by":"crossref","first-page":"4685","DOI":"10.1046\/j.1432-1327.2000.01519.x","article-title":"Regulation of the expression of human ferrochelatase by intracellular iron levels","volume":"267","author":"Taketani","year":"2000","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.exphem.2011.05.003_bib42","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1182\/blood-2009-09-243105","article-title":"Post-translational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery","volume":"115","author":"Crooks","year":"2010","journal-title":"Blood"},{"key":"10.1016\/j.exphem.2011.05.003_bib43","doi-asserted-by":"crossref","first-page":"1035","DOI":"10.1038\/nature03887","article-title":"Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis","volume":"436","author":"Wingert","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.exphem.2011.05.003_bib44","doi-asserted-by":"crossref","first-page":"3494","DOI":"10.1093\/nar\/gkl498","article-title":"Defective splicing, disease and therapy: searching for master checkpoints in exon definition","volume":"34","author":"Buratti","year":"2006","journal-title":"Nucl Acid Res"},{"key":"10.1016\/j.exphem.2011.05.003_bib45","doi-asserted-by":"crossref","first-page":"4449","DOI":"10.1016\/j.febslet.2006.07.018","article-title":"NF1 mRNA biogenesis: effects of the genomic milieu in splicing regulation of the NF1 exon 37","volume":"580","author":"Baralle","year":"2006","journal-title":"FEBS Lett"},{"key":"10.1016\/j.exphem.2011.05.003_bib46","doi-asserted-by":"crossref","first-page":"2231","DOI":"10.1016\/j.febslet.2008.05.018","article-title":"The pathological splicing mutation c.6792C>G in NF1 exon 37 causes a change in tenancy between antagonistic splicing factors","volume":"582","author":"Skoko","year":"2008","journal-title":"FEBS Lett"},{"key":"10.1016\/j.exphem.2011.05.003_bib47","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/nature08909","article-title":"Expansion of the eukaryotic proteome by alternative splicing","volume":"463","author":"Nilsen","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.exphem.2011.05.003_bib48","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1093\/hmg\/11.1.87","article-title":"Mutations in HPRP3, a third member of pre-mRNA splicing factor genes, implicated in autosomal dominant retinitis pigmentosa","volume":"11","author":"Chakarova","year":"2002","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.exphem.2011.05.003_bib49","first-page":"1259","article-title":"Pre-mRNA splicing and retinitis pigmentosa","volume":"12","author":"Mordes","year":"2006","journal-title":"Mol Vis"},{"key":"10.1016\/j.exphem.2011.05.003_bib50","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/j.cell.2008.03.031","article-title":"SMN deficiency causes tissue-specific perturbations in the repertoire of snRNAs and widespread defects in splicing","volume":"133","author":"Zhang","year":"2008","journal-title":"Cell"},{"key":"10.1016\/j.exphem.2011.05.003_bib51","doi-asserted-by":"crossref","first-page":"5494","DOI":"10.1182\/blood-2010-11-319483","article-title":"Targeted deletion of the mouse Mitoferrin1 gene: from anemia to protoporphyria","volume":"117","author":"Troadec","year":"2011","journal-title":"Blood"}],"container-title":["Experimental Hematology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301472X11002256?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0301472X11002256?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T08:28:39Z","timestamp":1759566519000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0301472X11002256"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,7]]},"references-count":51,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2011,7]]}},"alternative-id":["S0301472X11002256"],"URL":"https:\/\/doi.org\/10.1016\/j.exphem.2011.05.003","relation":{},"ISSN":["0301-472X"],"issn-type":[{"value":"0301-472X","type":"print"}],"subject":[],"published":{"date-parts":[[2011,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Abnormal mitoferrin-1 expression in patients with erythropoietic protoporphyria","name":"articletitle","label":"Article Title"},{"value":"Experimental Hematology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.exphem.2011.05.003","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2011 ISEH - Society for Hematology and Stem Cells. Published by Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}