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pro vyhledávání: '"Michel A. Struwe"'
Autor:
Sophia Rixen, Patrick M. Indorf, Christian Kubitza, Michel A. Struwe, Cathrin Klopp, Axel J. Scheidig, Thomas Kunze, Bernd Clement
Publikováno v:
Molecules, Vol 28, Iss 17, p 6384 (2023)
The mitochondrial amidoxime reducing component (mARC) is a human molybdoenzyme known to catalyze the reduction of various N-oxygenated substrates. The physiological function of mARC enzymes, however, remains unknown. In this study, we examine the red
Externí odkaz:
https://doaj.org/article/96401eb5c24d4951a7e7703198414bbe
Autor:
Bernd Clement, Michel A. Struwe
Publikováno v:
Molecules, Vol 28, Iss 12, p 4713 (2023)
The mitochondrial amidoxime-reducing component (mARC) is the most recently discovered molybdoenzyme in humans after sulfite oxidase, xanthine oxidase and aldehyde oxidase. Here, the timeline of mARC’s discovery is briefly described. The story begin
Externí odkaz:
https://doaj.org/article/e6a1536a62424605b9902f53cc6e37e7
Publikováno v:
Hepatology Communications, Vol 6, Iss 11, Pp 3277-3278 (2022)
Externí odkaz:
https://doaj.org/article/8cb6a995d8b34859a8285296448611ed
Publikováno v:
Hepatology Communications. 6:3277-3278
Autor:
Palraj Kalimuthu, Daniel Ellis, Paul V. Bernhardt, Martin L. Kirk, Zhenyao Luo, Bernd Clement, Bostjan Kobe, Jeffrey Harmer, Qifeng Zhong, Ulrike Kappler, K.C. Khadanand, Michel A. Struwe, Jing Yang, Alastair G. McEwan
Publikováno v:
The Journal of Biological Chemistry
MtsZ is a molybdenum-containing methionine sulfoxide reductase that supports virulence in the human respiratory pathogen Haemophilus influenzae (Hi). HiMtsZ belongs to a group of structurally and spectroscopically uncharacterized S-/N-oxide reductase