Heme (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Heme" in English language version.

refsWebsite

Global rank English rank

63nih.gov

4^th place

44doi.org

2^nd place

12semanticscholar.org

11^th place

8^th place

8worldcat.org

5^th place

6web.archive.org

1^st place

4harvard.edu

18^th place

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1sciencedirect.com

149^th place

178^th place

1iupac.org

538^th place

863^rd place

1ed.ac.uk

1,871^st place

1,234^th place

1handle.net

102^nd place

76^th place

1udel.edu

4,858^th place

3,506^th place

1jbc.org

4,455^th place

5,199^th place

1umassmed.edu

low place

1elsevier.com

610^th place

704^th place

1wired.com

193^rd place

152^nd place

1economist.com

254^th place

236^th place

1archive.org

6^th place

1thoughtco.com

1,430^th place

1,166^th place

1fiocruz.br

low place

1wcrf.org

low place

archive.org

Lehninger's Principles of Biochemistry (5th ed.). New York: W. H. Freeman and Company. 2008. pp. 876. ISBN 978-0-7167-7108-1.

doi.org

Hodgson E, Roe RM, Mailman RB, Chambers JE, eds. (2015). "H". Dictionary of Toxicology (3rd ed.). Academic Press. pp. 173–184. doi:10.1016/B978-0-12-420169-9.00008-4. ISBN 978-0-12-420169-9. Retrieved 2024-02-21.
Bloomer JR (1998). "Liver metabolism of porphyrins and haem". Journal of Gastroenterology and Hepatology. 13 (3): 324–329. doi:10.1111/j.1440-1746.1998.01548.x. PMID 9570250. S2CID 25224821.
Dutt S, Hamza I, Bartnikas TB (2022-08-22). "Molecular Mechanisms of Iron and Heme Metabolism". Annual Review of Nutrition. 42 (1): 311–335. doi:10.1146/annurev-nutr-062320-112625. ISSN 0199-9885. PMC 9398995. PMID 35508203.
Chemistry IU (2009). "Hemes (heme derivatives)". IUPAC Compendium of Chemical Terminology. IUPAC. doi:10.1351/goldbook.H02773. ISBN 978-0-9678550-9-7. Archived from the original on 22 August 2017. Retrieved 28 April 2018.
Poulos TL (2014-04-09). "Heme Enzyme Structure and Function". Chemical Reviews. 114 (7): 3919–3962. doi:10.1021/cr400415k. ISSN 0009-2665. PMC 3981943. PMID 24400737.
Paoli M (2002). "Structure-function relationships in heme-proteins" (PDF). DNA Cell Biol. 21 (4): 271–280. doi:10.1089/104454902753759690. hdl:20.500.11820/67200894-eb9f-47a2-9542-02877d41fdd7. PMID 12042067. S2CID 12806393. Archived (PDF) from the original on 2018-07-24.
Alderton W (2001). "Nitric oxide synthases: structure, function and inhibition". Biochem. J. 357 (3): 593–615. doi:10.1042/bj3570593. PMC 1221991. PMID 11463332.
Milani M (2005). "Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins". J. Inorg. Biochem. 99 (1): 97–109. doi:10.1016/j.jinorgbio.2004.10.035. PMID 15598494.
Hardison R (1999). "The Evolution of Hemoglobin: Studies of a very ancient protein suggest that changes in gene regulation are an important part of the evolutionary story". American Scientist. 87 (2): 126. doi:10.1511/1999.20.809 (inactive 11 March 2025). S2CID 123532036.{{cite journal}}: CS1 maint: DOI inactive as of March 2025 (link)
Poulos T (2014). "Heme Enzyme Structure and Function". Chem. Rev. 114 (7): 3919–3962. doi:10.1021/cr400415k. PMC 3981943. PMID 24400737.
Thom CS (2013). "Hemoglobin Variants: Biochemical Properties and Clinical Correlates". Cold Spring Harbor Perspectives in Medicine. 3 (3): a011858. doi:10.1101/cshperspect.a011858. PMC 3579210. PMID 23388674.
Ackers GK, Holt JM (2006). "Asymmetric cooperativity in a symmetric tetramer: human hemoglobin". J. Biol. Chem. 281 (17): 11441–3. doi:10.1074/jbc.r500019200. PMID 16423822. S2CID 6696041.
Caughey WS, Smythe GE, O'Keeffe DH, Maskasky JE, Smith ML (1975). "Heme A of Cytochrome c Oxidase: Structure and properties: comparisons with hemes B, C, and S and derivatives". J. Biol. Chem. 250 (19): 7602–7622. doi:10.1016/S0021-9258(19)40860-0. PMID 170266.
Hegg EL (2004). "Heme A Synthase Does Not Incorporate Molecular Oxygen into the Formyl Group of Heme A". Biochemistry. 43 (27): 8616–8624. doi:10.1021/bi049056m. PMID 15236569.
Yoshikawa S (2012). "Structural studies on bovine heart cytochrome c oxidase". Biochim. Biophys. Acta. 1817 (4): 579–589. doi:10.1016/j.bbabio.2011.12.012. PMID 22236806.
Rae T, Goff H (1998). "The heme prosthetic group of lactoperoxidase. Structural characteristics of heme l and heme l-peptides". The Journal of Biological Chemistry. 273 (43): 27968–27977. doi:10.1074/jbc.273.43.27968. PMID 9774411. S2CID 25780396.
Purdy M (1983). "Effect of growth phase and cell envelope structure on susceptibility of Salmonella triumphant to the lactoperoxidase-thiocyanate-hydrogen peroxide system". Infect. Immun. 39 (3): 1187–95. doi:10.1128/IAI.39.3.1187-1195.1983. PMC 348082. PMID 6341231.
Ohshima H (2003). "Chemical basis of inflammation-induced carcinogenesis". Arch. Biochem. Biophys. 417 (1): 3–11. doi:10.1016/s0003-9861(03)00283-2. PMID 12921773.
Henderson J (2003). "Phagocytes produce 5-chlorouracil and 5-bromouracil, two mutagenic products of myeloperoxidase, in human inflammatory tissue". J. Biol. Chem. 278 (26): 23522–8. doi:10.1074/jbc.m303928200. PMID 12707270. S2CID 19631565.
Murshudov G, Grebenko A, Barynin V, Dauter Z, Wilson K, Vainshtein B, Melik-Adamyan W, Bravo J, Ferrán J, Ferrer JC, Switala J, Loewen PC, Fita I (1996). "Structure of the heme d of Penicillium vitale and Escherichia coli catalases" (PDF). The Journal of Biological Chemistry. 271 (15): 8863–8868. doi:10.1074/jbc.271.15.8863. PMID 8621527. Archived (PDF) from the original on 2018-07-24.
Belevich I (2005). "Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability". FEBS Letters. 579 (21): 4567–70. Bibcode:2005FEBSL.579.4567B. doi:10.1016/j.febslet.2005.07.011. PMID 16087180. S2CID 36465802.
Puustinen A, Wikström M. (1991). "The heme groups of cytochrome o from Escherichia coli". Proc. Natl. Acad. Sci. U.S.A. 88 (14): 6122–6. Bibcode:1991PNAS...88.6122P. doi:10.1073/pnas.88.14.6122. PMC 52034. PMID 2068092.
Caughey WS, York JL (1962). "Isolation and some properties of the green heme of cytochrome oxidase from beef heart muscle". J. Biol. Chem. 237 (7): 2414–6. doi:10.1016/S0021-9258(19)63456-3. PMID 13877421.
Caughey WS, Smythe GA, O'Keeffe DH, Maskasky JE, Smith ML (1975). "Heme A of cytochrome c oxidase. Structure and properties: comparisons with hemes B, C, and S and derivatives". J. Biol. Chem. 250 (19): 7602–22. doi:10.1016/S0021-9258(19)40860-0. PMID 170266.
Battersby AR (2000). "Tetrapyrroles: The pigments of life". Natural Product Reports. 17 (6): 507–526. doi:10.1039/B002635M. PMID 11152419.
Sridevi K (28 April 2018). Upregulation of Heme Pathway Enzyme ALA Synthase-1 by Glutethimide and 4,6-Dioxoheptanoic Acid and Downregulation by Glucose and Heme: A Dissertation. EScholarship@UMMS (Thesis). University of Massachusetts Medical School. doi:10.13028/yyrz-qa79. Archived from the original on 8 August 2016. Retrieved 28 April 2018.
Kumar S, Bandyopadhyay U (July 2005). "Free heme toxicity and its detoxification systems in human". Toxicology Letters. 157 (3): 175–188. doi:10.1016/j.toxlet.2005.03.004. PMID 15917143.
Puy H, Gouya L, Deybach JC (March 2010). "Porphyrias". The Lancet. 375 (9718): 924–937. doi:10.1016/S0140-6736(09)61925-5. PMID 20226990. S2CID 208791867.
Fraser RZ, Shitut M, Agrawal P, Mendes O, Klapholz S (2018-04-11). "Safety Evaluation of Soy Leghemoglobin Protein Preparation Derived FromPichia pastoris, Intended for Use as a Flavor Catalyst in Plant-Based Meat". International Journal of Toxicology. 37 (3): 241–262. doi:10.1177/1091581818766318. ISSN 1091-5818. PMC 5956568. PMID 29642729.
Maines MD (July 1988). "Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications". The FASEB Journal. 2 (10): 2557–2568. doi:10.1096/fasebj.2.10.3290025. ISSN 0892-6638. PMID 3290025. S2CID 22652094.
Hanafy K (2013). "Carbon Monoxide and the brain: time to rethink the dogma". Curr. Pharm. Des. 19 (15): 2771–5. doi:10.2174/1381612811319150013. PMC 3672861. PMID 23092321.
Abraham N, Kappas A (2008). "Pharmacological and clinical aspects of heme oxygenase". Pharmacol. Rev. 60 (1): 79–127. doi:10.1124/pr.107.07104. PMID 18323402. S2CID 12792155.
King C, Rios G, Green M, Tephly T (2000). "UDP-Glucuronosyltransferases". Current Drug Metabolism. 1 (2): 143–161. doi:10.2174/1389200003339171. PMID 11465080.
Hall B, Levy S, Dufault-Thompson K, Arp G, Zhong A, Ndjite GM, Weiss A, Braccia D, Jenkins C, Grant MR, Abeysinghe S, Yang Y, Jermain MD, Wu CH, Ma B (2024-01-03). "BilR is a gut microbial enzyme that reduces bilirubin to urobilinogen". Nature Microbiology. 9 (1): 173–184. doi:10.1038/s41564-023-01549-x. ISSN 2058-5276. PMC 10769871. PMID 38172624.
Bunn HF, Jandl JH (Sep 1966). "Exchange of heme among hemoglobin molecules". Proc. Natl. Acad. Sci. USA. 56 (3): 974–978. Bibcode:1966PNAS...56..974B. doi:10.1073/pnas.56.3.974. PMC 219955. PMID 5230192.
Smith ML, Paul J, Ohlsson PI, Hjortsberg K, Paul KG (Feb 1991). "Heme-protein fission under nondenaturing conditions". Proc. Natl. Acad. Sci. USA. 88 (3): 882–886. Bibcode:1991PNAS...88..882S. doi:10.1073/pnas.88.3.882. PMC 50918. PMID 1846966.
Everse J, Hsia N (1197). "The toxicities of native and modified hemoglobins". Free Radical Biology and Medicine. 22 (6): 1075–1099. doi:10.1016/S0891-5849(96)00499-6. PMID 9034247.
Kumar S, Bandyopadhyay U (July 2005). "Free heme toxicity and its detoxification systems in humans". Toxicology Letters. 157 (3): 175–188. doi:10.1016/j.toxlet.2005.03.004. PMID 15917143.
Pamplona A, Ferreira A, Balla J, Jeney V, Balla G, Epiphanio S, Chora A, Rodrigues CD, Gregoire IP, Cunha-Rodrigues M, Portugal S, Soares MP, Mota MM (Jun 2007). "Heme oxygenase-1 and carbon monoxide suppress the pathogenesis of experimental cerebral malaria". Nature Medicine. 13 (6): 703–710. doi:10.1038/nm1586. PMID 17496899. S2CID 20675040.
Larsen R, Gozzelino R, Jeney V, Tokaji L, Bozza FA, Japiassú AM, Bonaparte D, Cavalcante MM, Chora A, Ferreira A, Marguti I, Cardoso S, Sepúlveda N, Smith A, Soares MP (2010). "A central role for free heme in the pathogenesis of severe sepsis". Science Translational Medicine. 2 (51): 51ra71. doi:10.1126/scitranslmed.3001118. PMID 20881280. S2CID 423446.
Bastide NM, Pierre FH, Corpet DE (Feb 2011). "Heme iron from meat and risk of colorectal cancer: a meta-analysis and a review of the mechanisms involved". Cancer Prevention Research (Philadelphia, Pa.). 4 (2): 177–184. doi:10.1158/1940-6207.CAPR-10-0113. ISSN 1940-6215. PMID 21209396.
Chang, Vicky C; Cotterchio, Michelle; Khoo, Edwin (2019). "Iron intake, body iron status, and risk of breast cancer: a systematic review and meta-analysis". BMC Cancer. 19 (1): 543. doi:10.1186/s12885-019-5642-0. PMC 6555759. PMID 31170936.{{cite journal}}: CS1 maint: multiple names: authors list (link)
Bustad HJ, Vorland M, Ronneseth E, Sandberg S, Martinez A, Toska K (August 8, 2013). "Conformational stability and activity analysis of two hydroxymethylbilane synthase mutants, K132N and V215E, with different phenotypic association with acute intermittent porphyria". Bioscience Reports. 33 (4): 617–626. doi:10.1042/BSR20130045. PMC 3738108. PMID 23815679.
Badenas C, To Figueras J, Phillips JD, Warby CA, Muñoz C, Herrero C (April 2009). "Identification and characterization of novel uroporphyrinogen decarboxylase gene mutations in a large series of porphyria cutanea tarda patients and relatives". Clinical Genetics. 75 (4): 346–353. doi:10.1111/j.1399-0004.2009.01153.x. PMC 3804340. PMID 19419417.

economist.com

"Silicon Valley gets a taste for food". The Economist. 2015-03-05. ISSN 0013-0613. Retrieved 2019-04-08.

ed.ac.uk

pure.ed.ac.uk

Paoli M (2002). "Structure-function relationships in heme-proteins" (PDF). DNA Cell Biol. 21 (4): 271–280. doi:10.1089/104454902753759690. hdl:20.500.11820/67200894-eb9f-47a2-9542-02877d41fdd7. PMID 12042067. S2CID 12806393. Archived (PDF) from the original on 2018-07-24.

elsevier.com

linkinghub.elsevier.com

Puy H, Gouya L, Deybach JC (March 2010). "Porphyrias". The Lancet. 375 (9718): 924–937. doi:10.1016/S0140-6736(09)61925-5. PMID 20226990. S2CID 208791867.

fiocruz.br

arca.fiocruz.br

Larsen R, Gozzelino R, Jeney V, Tokaji L, Bozza FA, Japiassú AM, Bonaparte D, Cavalcante MM, Chora A, Ferreira A, Marguti I, Cardoso S, Sepúlveda N, Smith A, Soares MP (2010). "A central role for free heme in the pathogenesis of severe sepsis". Science Translational Medicine. 2 (51): 51ra71. doi:10.1126/scitranslmed.3001118. PMID 20881280. S2CID 423446.

handle.net

hdl.handle.net

Paoli M (2002). "Structure-function relationships in heme-proteins" (PDF). DNA Cell Biol. 21 (4): 271–280. doi:10.1089/104454902753759690. hdl:20.500.11820/67200894-eb9f-47a2-9542-02877d41fdd7. PMID 12042067. S2CID 12806393. Archived (PDF) from the original on 2018-07-24.

harvard.edu

ui.adsabs.harvard.edu

Belevich I (2005). "Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability". FEBS Letters. 579 (21): 4567–70. Bibcode:2005FEBSL.579.4567B. doi:10.1016/j.febslet.2005.07.011. PMID 16087180. S2CID 36465802.
Puustinen A, Wikström M. (1991). "The heme groups of cytochrome o from Escherichia coli". Proc. Natl. Acad. Sci. U.S.A. 88 (14): 6122–6. Bibcode:1991PNAS...88.6122P. doi:10.1073/pnas.88.14.6122. PMC 52034. PMID 2068092.
Bunn HF, Jandl JH (Sep 1966). "Exchange of heme among hemoglobin molecules". Proc. Natl. Acad. Sci. USA. 56 (3): 974–978. Bibcode:1966PNAS...56..974B. doi:10.1073/pnas.56.3.974. PMC 219955. PMID 5230192.
Smith ML, Paul J, Ohlsson PI, Hjortsberg K, Paul KG (Feb 1991). "Heme-protein fission under nondenaturing conditions". Proc. Natl. Acad. Sci. USA. 88 (3): 882–886. Bibcode:1991PNAS...88..882S. doi:10.1073/pnas.88.3.882. PMC 50918. PMID 1846966.

iupac.org

goldbook.iupac.org

Chemistry IU (2009). "Hemes (heme derivatives)". IUPAC Compendium of Chemical Terminology. IUPAC. doi:10.1351/goldbook.H02773. ISBN 978-0-9678550-9-7. Archived from the original on 22 August 2017. Retrieved 28 April 2018.

jbc.org

Murshudov G, Grebenko A, Barynin V, Dauter Z, Wilson K, Vainshtein B, Melik-Adamyan W, Bravo J, Ferrán J, Ferrer JC, Switala J, Loewen PC, Fita I (1996). "Structure of the heme d of Penicillium vitale and Escherichia coli catalases" (PDF). The Journal of Biological Chemistry. 271 (15): 8863–8868. doi:10.1074/jbc.271.15.8863. PMID 8621527. Archived (PDF) from the original on 2018-07-24.

nih.gov

pubmed.ncbi.nlm.nih.gov

Bloomer JR (1998). "Liver metabolism of porphyrins and haem". Journal of Gastroenterology and Hepatology. 13 (3): 324–329. doi:10.1111/j.1440-1746.1998.01548.x. PMID 9570250. S2CID 25224821.
Dutt S, Hamza I, Bartnikas TB (2022-08-22). "Molecular Mechanisms of Iron and Heme Metabolism". Annual Review of Nutrition. 42 (1): 311–335. doi:10.1146/annurev-nutr-062320-112625. ISSN 0199-9885. PMC 9398995. PMID 35508203.
Ogun AS, Joy NV, Valentine M (2024), "Biochemistry, Heme Synthesis", StatPearls, Treasure Island (FL): StatPearls Publishing, PMID 30726014, retrieved 2024-02-22
Poulos TL (2014-04-09). "Heme Enzyme Structure and Function". Chemical Reviews. 114 (7): 3919–3962. doi:10.1021/cr400415k. ISSN 0009-2665. PMC 3981943. PMID 24400737.
Paoli M (2002). "Structure-function relationships in heme-proteins" (PDF). DNA Cell Biol. 21 (4): 271–280. doi:10.1089/104454902753759690. hdl:20.500.11820/67200894-eb9f-47a2-9542-02877d41fdd7. PMID 12042067. S2CID 12806393. Archived (PDF) from the original on 2018-07-24.
Alderton W (2001). "Nitric oxide synthases: structure, function and inhibition". Biochem. J. 357 (3): 593–615. doi:10.1042/bj3570593. PMC 1221991. PMID 11463332.
Milani M (2005). "Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins". J. Inorg. Biochem. 99 (1): 97–109. doi:10.1016/j.jinorgbio.2004.10.035. PMID 15598494.
Poulos T (2014). "Heme Enzyme Structure and Function". Chem. Rev. 114 (7): 3919–3962. doi:10.1021/cr400415k. PMC 3981943. PMID 24400737.
Thom CS (2013). "Hemoglobin Variants: Biochemical Properties and Clinical Correlates". Cold Spring Harbor Perspectives in Medicine. 3 (3): a011858. doi:10.1101/cshperspect.a011858. PMC 3579210. PMID 23388674.
Ackers GK, Holt JM (2006). "Asymmetric cooperativity in a symmetric tetramer: human hemoglobin". J. Biol. Chem. 281 (17): 11441–3. doi:10.1074/jbc.r500019200. PMID 16423822. S2CID 6696041.
Caughey WS, Smythe GE, O'Keeffe DH, Maskasky JE, Smith ML (1975). "Heme A of Cytochrome c Oxidase: Structure and properties: comparisons with hemes B, C, and S and derivatives". J. Biol. Chem. 250 (19): 7602–7622. doi:10.1016/S0021-9258(19)40860-0. PMID 170266.
Hegg EL (2004). "Heme A Synthase Does Not Incorporate Molecular Oxygen into the Formyl Group of Heme A". Biochemistry. 43 (27): 8616–8624. doi:10.1021/bi049056m. PMID 15236569.
Yoshikawa S (2012). "Structural studies on bovine heart cytochrome c oxidase". Biochim. Biophys. Acta. 1817 (4): 579–589. doi:10.1016/j.bbabio.2011.12.012. PMID 22236806.
Rae T, Goff H (1998). "The heme prosthetic group of lactoperoxidase. Structural characteristics of heme l and heme l-peptides". The Journal of Biological Chemistry. 273 (43): 27968–27977. doi:10.1074/jbc.273.43.27968. PMID 9774411. S2CID 25780396.
Purdy M (1983). "Effect of growth phase and cell envelope structure on susceptibility of Salmonella triumphant to the lactoperoxidase-thiocyanate-hydrogen peroxide system". Infect. Immun. 39 (3): 1187–95. doi:10.1128/IAI.39.3.1187-1195.1983. PMC 348082. PMID 6341231.
Ohshima H (2003). "Chemical basis of inflammation-induced carcinogenesis". Arch. Biochem. Biophys. 417 (1): 3–11. doi:10.1016/s0003-9861(03)00283-2. PMID 12921773.
Henderson J (2003). "Phagocytes produce 5-chlorouracil and 5-bromouracil, two mutagenic products of myeloperoxidase, in human inflammatory tissue". J. Biol. Chem. 278 (26): 23522–8. doi:10.1074/jbc.m303928200. PMID 12707270. S2CID 19631565.
Murshudov G, Grebenko A, Barynin V, Dauter Z, Wilson K, Vainshtein B, Melik-Adamyan W, Bravo J, Ferrán J, Ferrer JC, Switala J, Loewen PC, Fita I (1996). "Structure of the heme d of Penicillium vitale and Escherichia coli catalases" (PDF). The Journal of Biological Chemistry. 271 (15): 8863–8868. doi:10.1074/jbc.271.15.8863. PMID 8621527. Archived (PDF) from the original on 2018-07-24.
Belevich I (2005). "Oxygenated complex of cytochrome bd from Escherichia coli: stability and photolability". FEBS Letters. 579 (21): 4567–70. Bibcode:2005FEBSL.579.4567B. doi:10.1016/j.febslet.2005.07.011. PMID 16087180. S2CID 36465802.
Puustinen A, Wikström M. (1991). "The heme groups of cytochrome o from Escherichia coli". Proc. Natl. Acad. Sci. U.S.A. 88 (14): 6122–6. Bibcode:1991PNAS...88.6122P. doi:10.1073/pnas.88.14.6122. PMC 52034. PMID 2068092.
Caughey WS, York JL (1962). "Isolation and some properties of the green heme of cytochrome oxidase from beef heart muscle". J. Biol. Chem. 237 (7): 2414–6. doi:10.1016/S0021-9258(19)63456-3. PMID 13877421.
Caughey WS, Smythe GA, O'Keeffe DH, Maskasky JE, Smith ML (1975). "Heme A of cytochrome c oxidase. Structure and properties: comparisons with hemes B, C, and S and derivatives". J. Biol. Chem. 250 (19): 7602–22. doi:10.1016/S0021-9258(19)40860-0. PMID 170266.
Battersby AR (2000). "Tetrapyrroles: The pigments of life". Natural Product Reports. 17 (6): 507–526. doi:10.1039/B002635M. PMID 11152419.
Kumar S, Bandyopadhyay U (July 2005). "Free heme toxicity and its detoxification systems in human". Toxicology Letters. 157 (3): 175–188. doi:10.1016/j.toxlet.2005.03.004. PMID 15917143.
Puy H, Gouya L, Deybach JC (March 2010). "Porphyrias". The Lancet. 375 (9718): 924–937. doi:10.1016/S0140-6736(09)61925-5. PMID 20226990. S2CID 208791867.
Fraser RZ, Shitut M, Agrawal P, Mendes O, Klapholz S (2018-04-11). "Safety Evaluation of Soy Leghemoglobin Protein Preparation Derived FromPichia pastoris, Intended for Use as a Flavor Catalyst in Plant-Based Meat". International Journal of Toxicology. 37 (3): 241–262. doi:10.1177/1091581818766318. ISSN 1091-5818. PMC 5956568. PMID 29642729.
Maines MD (July 1988). "Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications". The FASEB Journal. 2 (10): 2557–2568. doi:10.1096/fasebj.2.10.3290025. ISSN 0892-6638. PMID 3290025. S2CID 22652094.
Hanafy K (2013). "Carbon Monoxide and the brain: time to rethink the dogma". Curr. Pharm. Des. 19 (15): 2771–5. doi:10.2174/1381612811319150013. PMC 3672861. PMID 23092321.
Abraham N, Kappas A (2008). "Pharmacological and clinical aspects of heme oxygenase". Pharmacol. Rev. 60 (1): 79–127. doi:10.1124/pr.107.07104. PMID 18323402. S2CID 12792155.
Florczyk U, Jozkowicz A, Dulak J (January–February 2008). "Biliverdin reductase: new features of an old enzyme and its potential therapeutic significance". Pharmacological Reports. 60 (1): 38–48. PMC 5536200. PMID 18276984.
King C, Rios G, Green M, Tephly T (2000). "UDP-Glucuronosyltransferases". Current Drug Metabolism. 1 (2): 143–161. doi:10.2174/1389200003339171. PMID 11465080.
Hall B, Levy S, Dufault-Thompson K, Arp G, Zhong A, Ndjite GM, Weiss A, Braccia D, Jenkins C, Grant MR, Abeysinghe S, Yang Y, Jermain MD, Wu CH, Ma B (2024-01-03). "BilR is a gut microbial enzyme that reduces bilirubin to urobilinogen". Nature Microbiology. 9 (1): 173–184. doi:10.1038/s41564-023-01549-x. ISSN 2058-5276. PMC 10769871. PMID 38172624.
Bunn HF, Jandl JH (Sep 1966). "Exchange of heme among hemoglobin molecules". Proc. Natl. Acad. Sci. USA. 56 (3): 974–978. Bibcode:1966PNAS...56..974B. doi:10.1073/pnas.56.3.974. PMC 219955. PMID 5230192.
Smith ML, Paul J, Ohlsson PI, Hjortsberg K, Paul KG (Feb 1991). "Heme-protein fission under nondenaturing conditions". Proc. Natl. Acad. Sci. USA. 88 (3): 882–886. Bibcode:1991PNAS...88..882S. doi:10.1073/pnas.88.3.882. PMC 50918. PMID 1846966.
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