Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Salete M, Newton"'
Publikováno v:
Frontiers in Microbiology, Vol 15 (2024)
We studied the Escherichia coli outer membrane protein Fiu, a presumed transporter of monomeric ferric catecholates, by introducing Cys residues in its surface loops and modifying them with fluorescein maleimide (FM). Fiu-FM bound iron complexes of t
Externí odkaz:
https://doaj.org/article/251b280807874e81b191f2004fc73118
Autor:
Yoriko Lill, Lorne D Jordan, Chuck R Smallwood, Salete M Newton, Markus A Lill, Phillip E Klebba, Ken Ritchie
Publikováno v:
PLoS ONE, Vol 11, Iss 12, p e0160862 (2016)
The important process of nutrient uptake in Escherichia coli, in many cases, involves transit of the nutrient through a class of beta-barrel proteins in the outer membrane known as TonB-dependent transporters (TBDTs) and requires interaction with the
Externí odkaz:
https://doaj.org/article/0b6af7436f2c49a4afb520b16da9efeb
Autor:
Hualiang Pi, Shari A Jones, Lynn E Mercer, Jessica P Meador, Joyce E Caughron, Lorne Jordan, Salete M Newton, Tyrrell Conway, Phillip E Klebba
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e50020 (2012)
We investigated the importance of the production of catecholate siderophores, and the utilization of their iron (III) complexes, to colonization of the mouse intestinal tract by Escherichia coli. First, a ΔtonB strain was completely unable to coloni
Externí odkaz:
https://doaj.org/article/e84fd54a7f9c4b158c5cf197632bf44a
Autor:
Aritri, Majumdar, Vy, Trinh, Kyle J, Moore, Chuck R, Smallwood, Ashish, Kumar, Taihao, Yang, Daniel C, Scott, Noah J, Long, Salete M, Newton, Phillip E, Klebba
Publikováno v:
J Biol Chem
The Escherichia coli outer membrane receptor FepA transports ferric enterobactin (FeEnt) by an energy- and TonB-dependent, but otherwise a mechanistically undetermined process involving its internal 150-residue N-terminal globular domain (N-domain).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::bfebdc7fd8b429d222dd4c7b439a286e
https://pubmed.ncbi.nlm.nih.gov/32098871
https://pubmed.ncbi.nlm.nih.gov/32098871