{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T20:44:40Z","timestamp":1788295480228,"version":"build-2803163510"},"reference-count":157,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2019,1,1]],"date-time":"2019-01-01T00:00:00Z","timestamp":1546300800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,1,1]],"date-time":"2019-01-01T00:00:00Z","timestamp":1546300800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2019,6,15]],"date-time":"2019-06-15T00:00:00Z","timestamp":1560556800000},"content-version":"vor","delay-in-days":165,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 DK116548"],"award-info":[{"award-number":["R01 DK116548"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 HL124232"],"award-info":[{"award-number":["R01 HL124232"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01 HL125774"],"award-info":[{"award-number":["R01 HL125774"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["U54 DK083909"],"award-info":[{"award-number":["U54 DK083909"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["DK034933"],"award-info":[{"award-number":["DK034933"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100007270","name":"University of Michigan","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007270","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","cmghjournal.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cellular and Molecular Gastroenterology and Hepatology"],"published-print":{"date-parts":[[2019]]},"DOI":"10.1016\/j.jcmgh.2019.06.006","type":"journal-article","created":{"date-parts":[[2019,6,21]],"date-time":"2019-06-21T17:16:26Z","timestamp":1561137386000},"page":"535-548","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":74,"title":["Porphyrin-Induced Protein Oxidation and Aggregation as a Mechanism of Porphyria-Associated Cell Injury"],"prefix":"10.1016","volume":"8","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-8775-2963","authenticated-orcid":false,"given":"Dhiman","family":"Maitra","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3493-2960","authenticated-orcid":false,"given":"Juliana","family":"Bragazzi Cunha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jared S.","family":"Elenbaas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Herbert L.","family":"Bonkovsky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jordan A.","family":"Shavit","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8624-2347","authenticated-orcid":false,"given":"M. Bishr","family":"Omary","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jcmgh.2019.06.006_bib1","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/BF02110037","article-title":"Structure and function of ferrochelatase","volume":"27","author":"Ferreira","year":"1995","journal-title":"J\u00a0Bioenerg Biomembr"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib2","doi-asserted-by":"crossref","first-page":"2453","DOI":"10.1021\/jp013155h","article-title":"Aggregation behavior of protoporphyrin IX in aqueous solutions:\u2009 clear evidence of vesicle formation","volume":"106","author":"Scolaro","year":"2002","journal-title":"J\u00a0Phys Chem B"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib3","doi-asserted-by":"crossref","first-page":"23711","DOI":"10.1074\/jbc.M114.636001","article-title":"Ambient light promotes selective subcellular proteotoxicity after endogenous and exogenous porphyrinogenic stress","volume":"290","author":"Maitra","year":"2015","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib4","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1016\/S0140-6736(09)61925-5","volume":"375","author":"Puy","year":"2010","journal-title":"Porphyrias. Lancet"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib5","article-title":"Fall von pemphigus leprosus, kompliziert durch lepra visceralis","author":"Schultz","year":"1874","journal-title":"Diss. med. Greifswald"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib6","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/0020-711X(80)90219-0","article-title":"A\u00a0short history of porphyrins and the porphyrias","volume":"11","author":"With","year":"1980","journal-title":"Int J Biochem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib7","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.jcmgh.2019.06.006_bib8","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1111\/j.1478-3231.2012.02794.x","article-title":"Hepatitis C, porphyria cutanea tarda and liver iron: an update","volume":"32","author":"Ryan Caballes","year":"2012","journal-title":"Liver Int"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib9","doi-asserted-by":"crossref","first-page":"4496","DOI":"10.1182\/blood-2012-05-423186","article-title":"The porphyrias: advances in diagnosis and treatment","volume":"120","author":"Balwani","year":"2012","journal-title":"Blood"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib10","article-title":"Porphyria diagnostics-part 1: a brief overview of the porphyrias","volume":"86","author":"Ramanujam","year":"2015","journal-title":"Curr Protoc Hum Genet"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib11","doi-asserted-by":"crossref","DOI":"10.1016\/j.ymgme.2019.03.002","article-title":"Pathogenesis and clinical features of the acute hepatic porphyrias (AHPs)","author":"Bonkovsky","year":"2019","journal-title":"Mol Genet Metab"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib12","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/0738-081X(93)90162-6","article-title":"Drug-induced cutaneous porphyria","volume":"11","author":"Ayala","year":"1993","journal-title":"Clin Dermatol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib13","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1016\/j.amjmed.2014.06.036","article-title":"Acute porphyrias in the USA: features of 108 subjects from porphyrias consortium","volume":"127","author":"Bonkovsky","year":"2014","journal-title":"Am J Med"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib14","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/S0190-9622(94)70029-X","article-title":"Acute hereditary coproporphyria induced by the androgenic\/anabolic steroid methandrostenolone (Dianabol)","volume":"30","author":"Lane","year":"1994","journal-title":"J\u00a0Am Acad Dermatol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib15","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1002\/hep.27086","article-title":"Liver transplantation in the management of porphyria","volume":"60","author":"Singal","year":"2014","journal-title":"Hepatology"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib16","doi-asserted-by":"crossref","DOI":"10.1016\/j.jcmgh.2019.05.010","article-title":"Oxygen and conformation dependent, light-enhanced, reversible protein aggregation and oxidation by porphyrins","author":"Maitra","year":"2019","journal-title":"Cell Mol Gastroenterol Hepatol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib17","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1038\/ng0296-195","article-title":"Porphobilinogen deaminase deficiency in mice causes a neuropathy resembling that of human hepatic porphyria","volume":"12","author":"Lindberg","year":"1996","journal-title":"Nat Genet"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib18","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1086\/502667","article-title":"Uroporphyrinogen III synthase knock-in mice have the human congenital erythropoietic porphyria phenotype, including the characteristic light-induced cutaneous lesions","volume":"78","author":"Bishop","year":"2006","journal-title":"Am J Hum Genet"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib19","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.ygeno.2005.08.018","article-title":"A\u00a0knock-in mouse model of congenital erythropoietic porphyria","volume":"87","author":"Ged","year":"2006","journal-title":"Genomics"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib20","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1073\/pnas.98.1.259","article-title":"A\u00a0mouse model of familial porphyria cutanea tarda","volume":"98","author":"Phillips","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib21","first-page":"1005","article-title":"A\u00a0mouse model of hereditary coproporphyria identified in an ENU mutagenesis screen","volume":"10","author":"Conway","year":"2017","journal-title":"Dis Model Mech"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib22","first-page":"71","article-title":"A\u00a0mouse model for South African (R59W) variegate porphyria: construction and initial characterization","volume":"48","author":"Medlock","year":"2002","journal-title":"Cell Mol Biol (Noisy-le-grand)"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib23","doi-asserted-by":"crossref","first-page":"1730","DOI":"10.1172\/JCI115491","article-title":"Erythropoietic protoporphyria in the house mouse. A recessive inherited ferrochelatase deficiency with anemia, photosensitivity, and liver disease","volume":"88","author":"Tutois","year":"1991","journal-title":"J\u00a0Clin Invest"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib24","first-page":"225","article-title":"Modeling the ferrochelatase c.315\u201348C modifier mutation for erythropoietic protoporphyria (EPP) in mice","volume":"10","author":"Barman-Aksozen","year":"2017","journal-title":"Dis Model Mech"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib25","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/1011-1344(95)07117-K","article-title":"Topical application of 5-aminolevulinic acid, DMSO and EDTA: protoporphyrin IX accumulation in skin and tumours of mice","volume":"28","author":"Malik","year":"1995","journal-title":"J\u00a0Photochem Photobiol B"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib26","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1002\/ijc.2910520318","article-title":"Distribution and photosensitizing efficiency of porphyrins induced by application of exogenous 5-aminolevulinic acid in mice bearing mammary carcinoma","volume":"52","author":"Peng","year":"1992","journal-title":"Int J Cancer"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib27","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/0016-5085(92)90860-2","article-title":"Selective accumulation of endogenously produced porphyrins in a liver metastasis model in rats","volume":"103","author":"Van Hillegersberg","year":"1992","journal-title":"Gastroenterology"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib28","doi-asserted-by":"crossref","first-page":"5079","DOI":"10.1073\/pnas.0700547104","article-title":"A\u00a0porphomethene inhibitor of uroporphyrinogen decarboxylase causes porphyria cutanea tarda","volume":"104","author":"Phillips","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib29","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1016\/S0006-291X(80)80026-X","article-title":"Inhibition of hepatic ferrochelatase by the 4 isomers of N-methylprotoporphyrin IX","volume":"97","author":"Ortiz de Montellano","year":"1980","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib30","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/0003-9861(81)90350-7","article-title":"Identification of N-methylprotoporphyrin IX in livers of untreated mice and mice treated with 3, 5-diethoxycarbonyl-1,4-dihydrocollidine: source of the methyl group","volume":"212","author":"Tephly","year":"1981","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib31","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1053\/j.gastro.2009.12.055","article-title":"Gender dimorphic formation of mouse Mallory-Denk bodies and the role of xenobiotic metabolism and oxidative stress","volume":"138","author":"Hanada","year":"2010","journal-title":"Gastroenterology"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib32","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/189499a0","article-title":"Acquired porphyria in man and rat due to hexachlorobenzene intoxication","volume":"189","author":"Ockner","year":"1961","journal-title":"Nature"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib33","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/0041-008X(80)90379-8","article-title":"Dependence of the porphyrogenic effect of 2,3,7,8-tetrachlorodibenzo(p)dioxin upon inheritance of aryl hydrocarbon hydroxylase responsiveness","volume":"53","author":"Jones","year":"1980","journal-title":"Toxicol Appl Pharmacol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib34","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1006\/geno.1993.1242","article-title":"Ferrochelatase structural mutant (Fechm1Pas) in the house mouse","volume":"16","author":"Boulechfar","year":"1993","journal-title":"Genomics"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib35","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S0925-4439(98)00096-9","article-title":"Targeted disruption of the mouse ferrochelatase gene producing an exon 10 deletion","volume":"1453","author":"Magness","year":"1999","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib36","doi-asserted-by":"crossref","first-page":"1470","DOI":"10.1182\/blood-2001-12-0283","article-title":"An exon 10 deletion in the mouse ferrochelatase gene has a dominant-negative effect and causes mild protoporphyria","volume":"100","author":"Magness","year":"2002","journal-title":"Blood"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib37","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1086\/498620","article-title":"Contribution of a common single-nucleotide polymorphism to the genetic predisposition for erythropoietic protoporphyria","volume":"78","author":"Gouya","year":"2006","journal-title":"Am J Hum Genet"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib38","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1039\/C6CC08473G","article-title":"Synthesis and cellular activity of stereochemically-pure 2'-O-(2-methoxyethyl)-phosphorothioate oligonucleotides","volume":"53","author":"Li","year":"2017","journal-title":"Chem Commun (Camb)"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib39","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/j.ajhg.2014.02.010","article-title":"Antisense oligonucleotide-based therapy in human erythropoietic protoporphyria","volume":"94","author":"Oustric","year":"2014","journal-title":"Am J Hum Genet"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib40","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.3727\/096368913X666980","article-title":"Hepatocyte transplantation ameliorates the metabolic abnormality in a mouse model of acute intermittent porphyria","volume":"23","author":"Yin","year":"2014","journal-title":"Cell Transplant"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib41","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1038\/mt.2010.210","article-title":"Sustained enzymatic correction by rAAV-mediated liver gene therapy protects against induced motor neuropathy in acute porphyria mice","volume":"19","author":"Unzu","year":"2011","journal-title":"Mol Ther"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib42","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1038\/mt.2009.250","article-title":"AAV8-mediated gene therapy prevents induced biochemical attacks of acute intermittent porphyria and improves neuromotor function","volume":"18","author":"Yasuda","year":"2010","journal-title":"Mol Ther"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib43","doi-asserted-by":"crossref","DOI":"10.1016\/j.ymgme.2019.01.007","article-title":"Murine models of the human porphyrias: contributions toward understanding disease pathogenesis and the development of new therapies","author":"Yasuda","year":"2019","journal-title":"Mol Genet Metab"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib44","first-page":"493","article-title":"Chemical screening in zebrafish for novel biological and therapeutic discovery","volume":"105","author":"Tan","year":"2011","journal-title":"Methods Cell Biol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib45","doi-asserted-by":"crossref","first-page":"2337","DOI":"10.1172\/JCI60434","article-title":"Hooked! Modeling human disease in zebrafish","volume":"122","author":"Santoriello","year":"2012","journal-title":"J\u00a0Clin Invest"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib46","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.cbpa.2019.02.005","article-title":"Developing zebrafish disease models for in\u00a0vivo small molecule screens","volume":"50","author":"Lam","year":"2019","journal-title":"Curr Opin Chem Biol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib47","doi-asserted-by":"crossref","first-page":"1132","DOI":"10.1016\/j.exphem.2008.04.008","article-title":"montalcino, A zebrafish model for variegate porphyria","volume":"36","author":"Dooley","year":"2008","journal-title":"Exp Hematol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib48","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1038\/3041","article-title":"A\u00a0zebrafish model for hepatoerythropoietic porphyria","volume":"20","author":"Wang","year":"1998","journal-title":"Nat Genet"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib49","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1016\/S0960-9822(00)00653-9","article-title":"Zebrafish dracula encodes ferrochelatase and its mutation provides a model for erythropoietic protoporphyria","volume":"10","author":"Childs","year":"2000","journal-title":"Curr Biol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib50","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1242\/dev.123.1.311","article-title":"Characterization of zebrafish mutants with defects in embryonic hematopoiesis","volume":"123","author":"Ransom","year":"1996","journal-title":"Development"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib51","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/S0959-437X(00)00074-5","article-title":"Zebrafish: a model system for the study of human disease","volume":"10","author":"Dooley","year":"2000","journal-title":"Curr Opin Genet Dev"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib52","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1016\/j.devcel.2015.01.032","article-title":"A\u00a0CRISPR\/Cas9 vector system for tissue-specific gene disruption in zebrafish","volume":"32","author":"Ablain","year":"2015","journal-title":"Dev Cell"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib53","doi-asserted-by":"crossref","first-page":"1798","DOI":"10.1096\/fj.201500111R","article-title":"A\u00a0precursor-inducible zebrafish model of acute protoporphyria with hepatic protein aggregation and multiorganelle stress","volume":"30","author":"Elenbaas","year":"2016","journal-title":"FASEB J"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib54","article-title":"Zebrafish as a model system to\u00a0delineate the role of heme and iron metabolism during erythropoiesis","author":"Zhang","year":"2018","journal-title":"Mol Genet Metab"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib55","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.bbamcr.2006.05.005","article-title":"Biosynthesis of heme in mammals","volume":"1763","author":"Ajioka","year":"2006","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib56","doi-asserted-by":"crossref","first-page":"36579","DOI":"10.1074\/jbc.M113.511642","article-title":"Effect of molecular characteristics on cellular uptake, subcellular localization, and phototoxicity of Zn(II) N-alkylpyridylporphyrins","volume":"288","author":"Ezzeddine","year":"2013","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib57","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1002\/jcp.10273","article-title":"Subcellular localization of Photofrin determines the death phenotype of human epidermoid carcinoma A431 cells triggered by photodynamic therapy: when plasma membranes are the main targets","volume":"194","author":"Hsieh","year":"2003","journal-title":"J\u00a0Cell Physiol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib58","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1038\/sj.bjc.6600664","article-title":"Endoplasmic reticulum and Golgi apparatus are the preferential sites of Foscan localisation in cultured tumour cells","volume":"88","author":"Teiten","year":"2003","journal-title":"Br J Cancer"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib59","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1111\/j.1751-1097.1991.tb02081.x","article-title":"Subcellular localization of porphyrins using confocal laser scanning microscopy","volume":"54","author":"Woodburn","year":"1991","journal-title":"Photochem Photobiol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib60","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/S1572-1000(05)00007-4","article-title":"Mechanisms in photodynamic therapy: part one-photosensitizers, photochemistry and cellular localization","volume":"1","author":"Castano","year":"2004","journal-title":"Photodiagnosis Photodyn Ther"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib61","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1111\/j.1751-1097.1991.tb02071.x","article-title":"Definition of type I and type II photosensitized oxidation","volume":"54","author":"Foote","year":"1991","journal-title":"Photochem Photobiol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib62","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1111\/j.0022-202X.2004.22601.x","article-title":"In\u00a0vivo oxygen radical generation in the skin of the protoporphyria model mouse with visible light exposure: an L-band ESR study","volume":"122","author":"Takeshita","year":"2004","journal-title":"J\u00a0Invest Dermatol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib63","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/1011-1344(91)80015-A","article-title":"Mechanisms of photosensitivity in porphyric patients with special emphasis on erythropoietic protoporphyria","volume":"10","author":"Brun","year":"1991","journal-title":"J\u00a0Photochem Photobiol B"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib64","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/S1011-1344(01)00207-X","article-title":"Photosensitized oxidation of membrane lipids: reaction pathways, cytotoxic effects, and cytoprotective mechanisms","volume":"63","author":"Girotti","year":"2001","journal-title":"J\u00a0Photochem Photobiol B"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib65","first-page":"3105","article-title":"Lamin aggregation is an early sensor of porphyria-induced liver injury","volume":"126","author":"Singla","year":"2013","journal-title":"J\u00a0Cell Sci"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib66","doi-asserted-by":"crossref","first-page":"11707","DOI":"10.1021\/ja504279r","article-title":"Far-red fluorescence probe for monitoring singlet oxygen during photodynamic therapy","volume":"136","author":"Kim","year":"2014","journal-title":"J\u00a0Am Chem Soc"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib67","doi-asserted-by":"crossref","first-page":"1639","DOI":"10.1002\/hep.21976","article-title":"Keratins let liver live: Mutations predispose to liver disease and crosslinking generates Mallory-Denk bodies","volume":"46","author":"Ku","year":"2007","journal-title":"Hepatology"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib68","first-page":"G1108","article-title":"The cytoskeleton of digestive epithelia in health and disease","volume":"277","author":"Ku","year":"1999","journal-title":"Am J Physiol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib69","doi-asserted-by":"crossref","first-page":"G628","DOI":"10.1152\/ajpgi.00455.2016","article-title":"Intermediate filament proteins of digestive organs: physiology and pathophysiology","volume":"312","author":"Omary","year":"2017","journal-title":"Am J Physiol Gastrointest Liver Physiol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib70","doi-asserted-by":"crossref","first-page":"1602","DOI":"10.1053\/j.gastro.2018.03.026","article-title":"Lamins and lamin-associated proteins in gastrointestinal health and disease","volume":"154","author":"Brady","year":"2018","journal-title":"Gastroenterology"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib71","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1002\/hep.25664","article-title":"Oxidative stress, Nrf2 and keratin up-regulation associate with Mallory-Denk body formation in mouse erythropoietic protoporphyria","volume":"56","author":"Singla","year":"2012","journal-title":"Hepatology"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib72","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0014-2999(02)01838-1","article-title":"The endoplasmic reticulum as an integrating signalling organelle: from neuronal signalling to neuronal death","volume":"447","author":"Verkhratsky","year":"2002","journal-title":"Eur J Pharmacol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib73","series-title":"Molecular Cell Biology","author":"Lodish","year":"2000"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib74","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.mrfmmm.2004.06.056","article-title":"ER stress and the unfolded protein response","volume":"569","author":"Schroder","year":"2005","journal-title":"Mutat Res"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib75","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.jhep.2018.09.023","article-title":"Loss of hepatocyte beta-catenin protects mice from experimental porphyria-associated liver injury","volume":"70","author":"Saggi","year":"2019","journal-title":"J\u00a0Hepatol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib76","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1146\/annurev.biochem.67.1.425","article-title":"The ubiquitin system","volume":"67","author":"Hershko","year":"1998","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib77","doi-asserted-by":"crossref","first-page":"12","DOI":"10.2183\/pjab.85.12","article-title":"The proteasome: overview of structure and functions","volume":"85","author":"Tanaka","year":"2009","journal-title":"Proc Jpn Acad Ser B Phys Biol Sci"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib78","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1038\/cr.2016.86","article-title":"The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death","volume":"26","author":"Livneh","year":"2016","journal-title":"Cell Res"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib79","doi-asserted-by":"crossref","first-page":"10451","DOI":"10.1021\/ja300781u","article-title":"Cationic porphyrins are reversible proteasome inhibitors","volume":"134","author":"Santoro","year":"2012","journal-title":"J\u00a0Am Chem Soc"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib80","doi-asserted-by":"crossref","first-page":"jcs222836","DOI":"10.1242\/jcs.222836","article-title":"p62\/SQSTM1 - steering the cell through health and disease","volume":"131","author":"Sanchez-Martin","year":"2018","journal-title":"J\u00a0Cell Sci"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib81","doi-asserted-by":"crossref","first-page":"ra98","DOI":"10.1126\/scisignal.aac5418","article-title":"Tumor-selective proteotoxicity of verteporfin inhibits colon cancer progression independently of YAP1","volume":"8","author":"Zhang","year":"2015","journal-title":"Sci Signal"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib82","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0114964","article-title":"Induction of covalently crosslinked p62 oligomers with reduced binding to polyubiquitinated proteins by the autophagy inhibitor verteporfin","volume":"9","author":"Donohue","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib83","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1083\/jcb.200507002","article-title":"p62\/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death","volume":"171","author":"Bjorkoy","year":"2005","journal-title":"J\u00a0Cell Biol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib84","doi-asserted-by":"crossref","first-page":"2033","DOI":"10.1016\/j.yexcr.2007.04.024","article-title":"From Mallory to Mallory-Denk bodies: what, how and why?","volume":"313","author":"Zatloukal","year":"2007","journal-title":"Exp Cell Res"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib85","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1083\/jcb.201102142","article-title":"Energy determinants GAPDH and NDPK act as genetic modifiers for hepatocyte inclusion formation","volume":"195","author":"Snider","year":"2011","journal-title":"J\u00a0Cell Biol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib86","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1038\/bjc.2013.391","article-title":"Targeting tumour energy metabolism potentiates the cytotoxicity of 5-aminolevulinic acid photodynamic therapy","volume":"109","author":"Golding","year":"2013","journal-title":"Br J Cancer"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib87","doi-asserted-by":"crossref","first-page":"25865","DOI":"10.3390\/ijms161025865","article-title":"Aminolevulinic acid-based tumor detection and therapy: molecular mechanisms and strategies for enhancement","volume":"16","author":"Yang","year":"2015","journal-title":"Int J Mol Sci"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib88","doi-asserted-by":"crossref","first-page":"4526","DOI":"10.3748\/wjg.v16.i36.4526","article-title":"Liver disease and erythropoietic protoporphyria: a concise review","volume":"16","author":"Casanova-Gonzalez","year":"2010","journal-title":"World J Gastroenterol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib89","doi-asserted-by":"crossref","DOI":"10.1038\/s41436-019-0537-7","article-title":"International Porphyria Molecular Diagnostic Collaborative: an evidence-based database of verified pathogenic and benign variants for the porphyrias","author":"Chen","year":"2019","journal-title":"Genet Med"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib90","doi-asserted-by":"crossref","first-page":"E1519","DOI":"10.3390\/molecules21111519","article-title":"Characteristics of the protoporphyrin IX binding sites on human serum albumin using molecular docking","volume":"21","author":"Sulkowski","year":"2016","journal-title":"Molecules"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib91","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1042\/bj1910095","article-title":"Kinetics and mechanism of the interaction between human serum albumin and monomeric haemin","volume":"191","author":"Adams","year":"1980","journal-title":"Biochem J"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib92","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/0022-2836(84)90341-3","article-title":"Structure of haptoglobin and the haptoglobin-hemoglobin complex by electron microscopy","volume":"174","author":"Wejman","year":"1984","journal-title":"J\u00a0Mol Biol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib93","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1111\/j.1432-1033.1974.tb03386.x","article-title":"Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin","volume":"43","author":"Hrkal","year":"1974","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib94","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0925-4439(99)00027-7","article-title":"Kinetics of hemin distribution in plasma reveals its role in lipoprotein oxidation","volume":"1454","author":"Miller","year":"1999","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib95","doi-asserted-by":"crossref","first-page":"12353","DOI":"10.1038\/ncomms12353","article-title":"The severity of hereditary porphyria is modulated by the porphyrin exporter and Lan antigen ABCB6","volume":"7","author":"Fukuda","year":"2016","journal-title":"Nat Commun"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib96","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1146\/annurev.pharmtox.46.120604.141238","article-title":"Role of ABCG2\/BCRP in biology and medicine","volume":"46","author":"Krishnamurthy","year":"2006","journal-title":"Annu Rev Pharmacol Toxicol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib97","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1038\/nature05125","article-title":"Identification of a mammalian mitochondrial porphyrin transporter","volume":"443","author":"Krishnamurthy","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib98","doi-asserted-by":"crossref","first-page":"2571","DOI":"10.1182\/blood-2004-04-1566","article-title":"Increased expression of the Abcg2 transporter during erythroid maturation plays a role in decreasing cellular protoporphyrin IX levels","volume":"105","author":"Zhou","year":"2005","journal-title":"Blood"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib99","first-page":"1009","article-title":"Liver disease in erythropoietic protoporphyria: insights and implications for management","volume":"56","author":"Anstey","year":"2007","journal-title":"Gut"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib100","doi-asserted-by":"crossref","first-page":"8670","DOI":"10.1016\/S0021-9258(19)40723-0","article-title":"Binding of nonsubstrate ligands to the glutathione S-transferases","volume":"250","author":"Ketley","year":"1975","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib101","doi-asserted-by":"crossref","first-page":"14521","DOI":"10.1016\/S0021-9258(17)38600-3","article-title":"A\u00a0protein of the Z class of liver cytosolic proteins in the rat that preferentially binds heme","volume":"260","author":"Vincent","year":"1985","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib102","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1002\/hep.1840100617","article-title":"Interaction of hemopexin, albumin and liver fatty acid-binding protein with protoporphyrin","volume":"10","author":"Knobler","year":"1989","journal-title":"Hepatology"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib103","doi-asserted-by":"crossref","first-page":"13398","DOI":"10.1021\/bi00041a017","article-title":"Purification, characterization, and cloning of a heme-binding protein (23 kDa) in rat liver cytosol","volume":"34","author":"Iwahara","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib104","doi-asserted-by":"crossref","first-page":"31388","DOI":"10.1074\/jbc.273.47.31388","article-title":"Molecular characterization of a newly identified heme-binding protein induced during differentiation of urine erythroleukemia cells","volume":"273","author":"Taketani","year":"1998","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib105","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/S0169-328X(99)00277-6","article-title":"Discovery of a putative heme-binding protein family (SOUL\/HBP) by 2-tissue\u00a0suppression subtractive hybridization and database searches","volume":"74","author":"Zylka","year":"1999","journal-title":"Brain Res Mol Brain Res"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib106","doi-asserted-by":"crossref","first-page":"8514","DOI":"10.1021\/bi300863a","article-title":"Heme binding properties of glyceraldehyde\u20133-phosphate dehydrogenase","volume":"51","author":"Hannibal","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib107","doi-asserted-by":"crossref","first-page":"14557","DOI":"10.1074\/jbc.RA118.004169","article-title":"Glyceraldehyde 3-phosphate dehydrogenase is a chaperone that allocates labile heme in cells","volume":"293","author":"Sweeny","year":"2018","journal-title":"J\u00a0Biol Chem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib108","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1016\/j.cell.2015.04.017","article-title":"Mitochondrial ClpX activates a key enzyme for heme biosynthesis and erythropoiesis","volume":"161","author":"Kardon","year":"2015","journal-title":"Cell"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib109","doi-asserted-by":"crossref","first-page":"E8045","DOI":"10.1073\/pnas.1700632114","article-title":"Mutation in human CLPX elevates levels of delta-aminolevulinate synthase and protoporphyrin IX to promote erythropoietic protoporphyria","volume":"114","author":"Yien","year":"2017","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib110","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1081\/DMR-100102336","article-title":"Quantification and significance of protein oxidation in biological samples","volume":"32","author":"Shacter","year":"2000","journal-title":"Drug Metab Rev"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib111","doi-asserted-by":"crossref","first-page":"1250","DOI":"10.1080\/10715760600918142","article-title":"Protein oxidation and aging","volume":"40","author":"Stadtman","year":"2006","journal-title":"Free Radic Res"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib112","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1042\/BJ20151227","article-title":"Protein oxidation and peroxidation","volume":"473","author":"Davies","year":"2016","journal-title":"Biochem J"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib113","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1039\/b307576c","article-title":"Reactive species formed on proteins exposed to singlet oxygen","volume":"3","author":"Davies","year":"2004","journal-title":"Photochem Photobiol Sci"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib114","doi-asserted-by":"crossref","first-page":"1321","DOI":"10.1111\/j.1751-1097.2011.00979.x","article-title":"Immunological detection of N-formylkynurenine in porphyrin-mediated photooxided lens alpha-crystallin","volume":"87","author":"Ehrenshaft","year":"2011","journal-title":"Photochem Photobiol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib115","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.toxlet.2005.03.004","article-title":"Free heme toxicity and its detoxification systems in human","volume":"157","author":"Kumar","year":"2005","journal-title":"Toxicol Lett"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib116","doi-asserted-by":"crossref","first-page":"963","DOI":"10.3233\/JAD-170711","article-title":"Free heme and amyloid-beta: a fatal liaison in Alzheimer's disease","volume":"61","author":"Chiziane","year":"2018","journal-title":"J\u00a0Alzheimers Dis"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib117","doi-asserted-by":"crossref","first-page":"26982","DOI":"10.1038\/srep26982","article-title":"Haem-assisted dityrosine-cross-linking of fibrinogen under non-thermal plasma exposure: one important mechanism of facilitated blood coagulation","volume":"6","author":"Ke","year":"2016","journal-title":"Sci Rep"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib118","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1007\/s00775-007-0276-0","article-title":"XH\/pi interactions with the pi system of porphyrin ring in porphyrin-containing proteins","volume":"12","author":"Stojanovic","year":"2007","journal-title":"J\u00a0Biol Inorg Chem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib119","doi-asserted-by":"crossref","first-page":"1867","DOI":"10.1016\/j.jinorgbio.2004.08.012","article-title":"pi interactions in the metal-porphyrin complexes with chelate ring as the H acceptor","volume":"98","author":"Medakovic","year":"2004","journal-title":"J\u00a0Inorg Biochem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib120","doi-asserted-by":"crossref","first-page":"1535","DOI":"10.1007\/s00726-012-1228-8","article-title":"Non-canonical interactions of porphyrins in porphyrin-containing proteins","volume":"43","author":"Stojanovic","year":"2012","journal-title":"Amino Acids"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib121","series-title":"Clinical biochemistry: metabolic and clinical aspects","first-page":"533","article-title":"CHAPTER 28 - the porphyrias: inherited disorders of haem synthesis","author":"Badminton","year":"2014"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib122","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1146\/annurev.biochem.73.011303.073823","article-title":"Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds","volume":"73","author":"Herrmann","year":"2004","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib123","doi-asserted-by":"crossref","first-page":"9568","DOI":"10.1039\/C6OB01633B","article-title":"Linker dependent chirality of solvent induced self-assembled structures of porphyrin-alpha-helical peptide conjugates","volume":"14","author":"Biscaglia","year":"2016","journal-title":"Org Biomol Chem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib124","doi-asserted-by":"crossref","first-page":"1403","DOI":"10.1021\/jm401653r","article-title":"Synthesis, spectroscopic, and photophysical characterization and photosensitizing activity toward prokaryotic and eukaryotic cells of porphyrin-magainin and -buforin conjugates","volume":"57","author":"Dosselli","year":"2014","journal-title":"J\u00a0Med Chem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib125","doi-asserted-by":"crossref","first-page":"2602","DOI":"10.1021\/bm100540t","article-title":"Nanometer to millimeter scale peptide-porphyrin materials","volume":"11","author":"Zaytsev","year":"2010","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib126","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1172\/JCI200421109","article-title":"Apolipoprotein A-I is a selective target for myeloperoxidase-catalyzed oxidation and functional impairment in subjects with cardiovascular disease","volume":"114","author":"Zheng","year":"2004","journal-title":"J\u00a0Clin Invest"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib127","doi-asserted-by":"crossref","first-page":"7024","DOI":"10.1021\/jacs.6b01555","article-title":"Role of distance in singlet oxygen applications: a model system","volume":"138","author":"Klaper","year":"2016","journal-title":"J\u00a0Am Chem Soc"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib128","doi-asserted-by":"crossref","first-page":"715","DOI":"10.1146\/annurev-biochem-061516-045037","article-title":"Oxidative stress","volume":"86","author":"Sies","year":"2017","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib129","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1093\/alcalc\/35.2.109","article-title":"Alcohol and porphyrin metabolism","volume":"35","author":"Doss","year":"2000","journal-title":"Alcohol Alcohol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib130","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1056\/NEJMra1608634","volume":"377","author":"Bissell","year":"2017","journal-title":"Porphyria. N Engl J Med"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib131","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1097\/00005792-197001000-00001","article-title":"Acute intermittent porphyria. A clinical and biochemical study of 46 patients","volume":"49","author":"Stein","year":"1970","journal-title":"Medicine (Baltimore)"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib132","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1002\/j.2040-4603.2013.tb00488.x","article-title":"Porphyrin and heme metabolism and the porphyrias","volume":"3","author":"Bonkovsky","year":"2013","journal-title":"Compr Physiol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib133","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 Transpl"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib134","doi-asserted-by":"crossref","first-page":"18238","DOI":"10.1073\/pnas.1314177110","article-title":"Therapeutic potential of proteasome inhibitors in congenital erythropoietic porphyria","volume":"110","author":"Blouin","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib135","doi-asserted-by":"crossref","first-page":"1565","DOI":"10.1093\/hmg\/ddx067","article-title":"Missense UROS mutations causing congenital erythropoietic porphyria reduce UROS homeostasis that can be rescued by proteasome inhibition","volume":"26","author":"Blouin","year":"2017","journal-title":"Hum Mol Genet"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib136","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.aat7467","article-title":"Repurposing ciclopirox as a pharmacological chaperone in a model of congenital erythropoietic porphyria","volume":"10","author":"Urquiza","year":"2018","journal-title":"Sci Transl Med"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib137","doi-asserted-by":"crossref","first-page":"1467","DOI":"10.1016\/j.bbapap.2010.12.015","article-title":"Molecular enzymology of 5-aminolevulinate synthase, the gatekeeper of heme biosynthesis","volume":"1814","author":"Hunter","year":"2011","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib138","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1042\/bst0300590","article-title":"Terminal steps of haem biosynthesis","volume":"30","author":"Dailey","year":"2002","journal-title":"Biochem Soc Trans"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib139","doi-asserted-by":"crossref","first-page":"4569","DOI":"10.1172\/JCI62422","article-title":"The mitochondrial heme exporter FLVCR1b mediates erythroid differentiation","volume":"122","author":"Chiabrando","year":"2012","journal-title":"J\u00a0Clin Invest"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib140","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1126\/science.1151133","article-title":"A\u00a0heme export protein is required for red blood cell differentiation and iron homeostasis","volume":"319","author":"Keel","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib141","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1053\/j.gastro.2014.01.053","article-title":"Heme exporter FLVCR1a regulates heme synthesis and degradation and controls activity of cytochromes P450","volume":"146","author":"Vinchi","year":"2014","journal-title":"Gastroenterology"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib142","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3109\/03602532.2010.515222","article-title":"Cytochrome P450 regulation: the interplay between its heme and apoprotein moieties in synthesis, assembly, repair, and disposal","volume":"43","author":"Correia","year":"2011","journal-title":"Drug Metab Rev"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib143","doi-asserted-by":"crossref","first-page":"241","DOI":"10.3109\/10715769409147520","article-title":"Formation of hydroxyl radicals on reaction of hypochlorous acid with ferrocyanide, a model iron(II) complex","volume":"20","author":"Candeias","year":"1994","journal-title":"Free Radic Res"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib144","doi-asserted-by":"crossref","first-page":"7592","DOI":"10.1021\/jp710249d","article-title":"Irradiation of the porphyrin causes unfolding of the protein in the protoporphyrin IX\/beta-lactoglobulin noncovalent complex","volume":"112","author":"Fernandez","year":"2008","journal-title":"J\u00a0Phys Chem B"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib145","doi-asserted-by":"crossref","first-page":"6020","DOI":"10.1021\/jp900957d","article-title":"Photoinduced unfolding of beta-lactoglobulin mediated by a water-soluble porphyrin","volume":"113","author":"Belcher","year":"2009","journal-title":"J\u00a0Phys Chem B"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib146","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1111\/j.1751-1097.1991.tb03669.x","article-title":"The photodegradation of porphyrins in cells can be used to estimate the lifetime of singlet oxygen","volume":"53","author":"Moan","year":"1991","journal-title":"Photochem Photobiol"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib147","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/0003-9861(90)90647-H","article-title":"The enzymatic one-electron reduction of porphyrins to their anion free radicals","volume":"283","author":"Morehouse","year":"1990","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib148","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/0003-9861(87)90567-4","article-title":"The one-electron reduction of uroporphyrin I by rat hepatic microsomes","volume":"257","author":"Morehouse","year":"1987","journal-title":"Arch Biochem Biophys"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib149","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1007\/s10545-012-9576-9","article-title":"High risk of primary liver cancer in a cohort of 179 patients with acute hepatic porphyria","volume":"36","author":"Sardh","year":"2013","journal-title":"J\u00a0Inherit Metab Dis"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib150","series-title":"GeneReviews","article-title":"Variegate porphyria","author":"Singal","year":"1993"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib151","series-title":"GeneReviews","article-title":"Hereditary coproporphyria","author":"Wang","year":"1993"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib152","series-title":"GeneReviews","article-title":"Familial porphyria cutanea tarda","author":"Liu","year":"1993"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib153","series-title":"GeneReviews","article-title":"Congenital erythropoietic porphyria","author":"Erwin","year":"1993"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib154","series-title":"GeneReviews","article-title":"Erythropoietic protoporphyria, autosomal recessive","author":"Balwani","year":"1993"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib155","series-title":"GeneReviews","article-title":"X-linked protoporphyria","author":"Balwani","year":"1993"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib156","series-title":"GeneReviews","article-title":"Acute intermittent porphyria","author":"Whatley","year":"1993"},{"key":"10.1016\/j.jcmgh.2019.06.006_bib157","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1055\/s-2007-1007139","article-title":"Acute porphyrias: pathogenesis of neurological manifestations","volume":"18","author":"Meyer","year":"1998","journal-title":"Semin Liver Dis"}],"container-title":["Cellular and Molecular Gastroenterology and Hepatology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2352345X19300852?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2352345X19300852?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,11,6]],"date-time":"2025-11-06T18:22:11Z","timestamp":1762453331000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2352345X19300852"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019]]},"references-count":157,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2019]]}},"alternative-id":["S2352345X19300852"],"URL":"https:\/\/doi.org\/10.1016\/j.jcmgh.2019.06.006","relation":{},"ISSN":["2352-345X"],"issn-type":[{"value":"2352-345X","type":"print"}],"subject":[],"published":{"date-parts":[[2019]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Porphyrin-Induced Protein Oxidation and Aggregation as a Mechanism of Porphyria-Associated Cell Injury","name":"articletitle","label":"Article Title"},{"value":"Cellular and Molecular Gastroenterology and Hepatology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jcmgh.2019.06.006","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 The Authors. Published by Elsevier Inc. on behalf of the AGA Institute.","name":"copyright","label":"Copyright"}]}}