New roles for GAPDH, Hsp90, and NO in regulating heme allocation and hemeprotein function in mammals
Author:
Affiliation:
1. Department of Inflammation and Immunity , Lerner Research Institute, Cleveland Clinic , 9500 Euclid Avenue , Cleveland , OH 44195 , USA
2. Department of Biochemistry , Medical College of Wisconsin , Milwaukee , WI 53226 , USA
Abstract
Funder
National Institute of Health Grants – Programme Grants for Applied Research
Publisher
Walter de Gruyter GmbH
Subject
Clinical Biochemistry,Molecular Biology,Biochemistry
Link
https://www.degruyter.com/document/doi/10.1515/hsz-2022-0197/pdf
Reference81 articles.
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2. Aitken, A.E., Lee, C.M., and Morgan, E.T. (2008). Roles of nitric oxide in inflammatory downregulation of human cytochromes P450. Free Radic. Biol. Med. 44: 1161–1168, https://doi.org/10.1016/j.freeradbiomed.2007.12.010.
3. Albakri, Q.A. and Stuehr, D.J. (1996). Intracellular assembly of inducible NO synthase is limited by nitric oxide-mediated changes in heme insertion and availability. J. Biol. Chem. 271: 5414–5421, https://doi.org/10.1074/jbc.271.10.5414.
4. Badawy, A.A. (2017). Kynurenine pathway of tryptophan metabolism: regulatory and functional aspects. Int. J. Tryptophan Res. 10: 1178646917691938.
5. Baker, J.D., Ozsan, I., Rodriguez Ospina, S., Gulick, D., and Blair, L.J. (2019). Hsp90 heterocomplexes regulate steroid hormone receptors: from stress response to psychiatric disease. Int. J. Mol. Sci. 20: 79, doi:https://doi.org/10.3390/ijms20010079.
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