Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Micah A. Gygi"'
Autor:
Michelle S. Prew, Christina M. Camara, Thomas Botzanowski, Jamie A. Moroco, Noah B. Bloch, Hannah R. Levy, Hyuk-Soo Seo, Sirano Dhe-Paganon, Gregory H. Bird, Henry D. Herce, Micah A. Gygi, Silvia Escudero, Thomas E. Wales, John R. Engen, Loren D. Walensky
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Prew et al. uncovered a structural basis for human VLCAD deficiency that arises from point mutations within the enzyme’s membrane-binding region, which was shown to fold as a putative α-helical hairpin. Helix-breaking mutations selectively disrupt
Externí odkaz:
https://doaj.org/article/e862c131a10741b096477d28809d47d0
Autor:
Michelle S, Prew, Christina M, Camara, Thomas, Botzanowski, Jamie A, Moroco, Noah B, Bloch, Hannah R, Levy, Hyuk-Soo, Seo, Sirano, Dhe-Paganon, Gregory H, Bird, Henry D, Herce, Micah A, Gygi, Silvia, Escudero, Thomas E, Wales, John R, Engen, Loren D, Walensky
Publikováno v:
Nature communications. 13(1)
Very long-chain acyl-CoA dehydrogenase (VLCAD) is an inner mitochondrial membrane enzyme that catalyzes the first and rate-limiting step of long-chain fatty acid oxidation. Point mutations in human VLCAD can produce an inborn error of metabolism call
Autor:
Micah A. Gygi, Jeremy D. O’Connell, Steven P. Gygi, Jonathon J. O’Brien, Joao A. Paulo, Robert A. Everley
Publikováno v:
Journal of Proteomics. 148:85-93
The budding yeast Saccharomyces cerevisiae is a model system for investigating biological processes. Cellular events are known to be dysregulated due to shifts in carbon sources. However, the comprehensive proteomic alterations thereof have not been