Assessment of the breadth of binding promiscuity of heme towards human proteins
Author:
Affiliation:
1. Centre de Recherche des Cordeliers, INSERM, CNRS, Sorbonne Université, Université de Paris , Centre de Recherche des Cordeliers 15, rue de l’Ecole de Médecine, F-75006 Paris , France
Abstract
Funder
European Research Council
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/hsz-2022-0226/pdf
Reference45 articles.
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2. Atamna, H. and Boyle, K. (2006). Amyloid-beta peptide binds with heme to form a peroxidase: relationship to the cytopathologies of Alzheimer’s disease. Proc. Natl. Acad. Sci. U.S.A. 103: 3381–3386, https://doi.org/10.1073/pnas.0600134103.
3. Barr, I., Smith, A.T., Chen, Y., Senturia, R., Burstyn, J.N., and Guo, F. (2012). Ferric, not ferrous, heme activates RNA-binding protein DGCR8 for primary microRNA processing. Proc. Natl. Acad. Sci. U.S.A. 109: 1919–1924, https://doi.org/10.1073/pnas.1114514109.
4. Bertini, I., Gray, H.B., Stiefel, E.I., and Valentine, J.S. (2007). Biological inorganic chemistry – structure & reactivity. Sausalito, California: University Science Books.
5. Bianchetti, C.M., Bingman, C.A., and Phillips, G.N.Jr. (2011). Structure of the C-terminal heme-binding domain of THAP domain containing protein 4 from Homo sapiens. Proteins 79: 1337–1341, https://doi.org/10.1002/prot.22944.
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