Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Breann L, Brown"'
Autor:
Jenny U. Tran, Breann L. Brown
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Pyridoxal 5′-phosphate (PLP)-dependent enzymes are found ubiquitously in nature and are involved in a variety of biological pathways, from natural product synthesis to amino acid and glucose metabolism. The first structure of a PLP-dependent enzyme
Externí odkaz:
https://doaj.org/article/42a3fe330d61492fafa42dd317a2c37e
Autor:
Jenny U. Tran, Breann L. Brown
Publikováno v:
Protein Science. 32
Autor:
Breann L, Brown, T M, Iverson
Publikováno v:
Nature chemical biology
The covalent attachment of one or multiple heme cofactors to their protein chain enables cytochromes c to be utilized in electron transfer and redox catalysis in extracytoplasmic environments. A dedicated heme maturation machinery, whose core compone
Autor:
Karl Herbine, Taku Kambayashi, Michael A. Kohanski, Danielle R. Reed, Brenal K. Singh, Breann L. Brown, De’Broski R. Herbert, Yukinori Tanaka, Edward M. Behrens, Bonnie Douglas, Paul J. Bryce, Tiffany Li Hui Tan, Annabel Ferguson, Li-Yin Hung, Christopher F. Pastore, Kelly Zullo, Nisha Vora, Cailu Lin, Noam A. Cohen
Publikováno v:
Sci Immunol
Interleukin-33 (IL-33) is a pleiotropic cytokine that can promote type 2 inflammation but also drives immunoregulation through Foxp3+Treg expansion. How IL-33 is exported from cells to serve this dual role in immunosuppression and inflammation remain
Autor:
Jessica L. Taylor, Breann L. Brown
Publikováno v:
Journal of Biological Chemistry. 298:101643
Heme is a critical biomolecule that is synthesized in vivo by several organisms such as plants, animals, and bacteria. Reflecting the importance of this molecule, defects in heme biosynthesis underlie several blood disorders in humans. Aminolevulinic
Publikováno v:
Protein Sci
The protein quality control network (pQC) plays critical roles in maintaining protein and cellular homeostasis, especially during stress. Lon is a major pQC AAA+ protease, conserved from bacteria to human mitochondria. It is the principal enzyme that
Autor:
Tina M. Iverson, Breann L. Brown
Publikováno v:
Nature Chemical Biology. 17:751-752
Heme-containing proteins support a broad range of cellular functions. A new crystal structure explains how an integral-membrane heme lyase attaches the hydrophobic heme to soluble proteins.
Autor:
Breann L Brown, Simina Grigoriu, Younghoon Kim, Jennifer M Arruda, Andrew Davenport, Thomas K Wood, Wolfgang Peti, Rebecca Page
Publikováno v:
PLoS Pathogens, Vol 5, Iss 12, p e1000706 (2009)
One mechanism by which bacteria survive environmental stress is through the formation of bacterial persisters, a sub-population of genetically identical quiescent cells that exhibit multidrug tolerance and are highly enriched in bacterial toxins. Rec
Externí odkaz:
https://doaj.org/article/77c21ffee5ab421db1e958b30a28de64
Publikováno v:
The FASEB Journal. 34:1-1
Publikováno v:
PMC
5-Aminolevulinic acid synthase (ALAS) catalyzes the first step in heme biosynthesis. We present the crystal structure of a eukaryotic ALAS from Saccharomyces cerevisiae. In this homodimeric structure, one ALAS subunit contains covalently bound cofact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afb403f21cd05b12deb7b24e0dc642ee
https://hdl.handle.net/1721.1/125924
https://hdl.handle.net/1721.1/125924