Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Aaron T. Bozzi"'
Autor:
Aaron T Bozzi, Christina M Zimanyi, John M Nicoludis, Brandon K Lee, Casey H Zhang, Rachelle Gaudet
Publikováno v:
eLife, Vol 8 (2019)
Nramp family transporters—expressed in organisms from bacteria to humans—enable uptake of essential divalent transition metals via an alternating-access mechanism that also involves proton transport. We present high-resolution structures of Deino
Externí odkaz:
https://doaj.org/article/2ffaf0b83ca3479bb191db679e73d90c
Publikováno v:
Metallomics
Zinc is an essential transition metal nutrient for bacterial survival and growth but may become toxic when present at elevated levels. The Gram-positive bacterial pathogen Streptococcus pneumoniae is sensitive to zinc poisoning, which results in grow
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06925202301a0718e59643192fa3d4df
https://doi.org/10.1093/mtomcs/mfac001
https://doi.org/10.1093/mtomcs/mfac001
Publikováno v:
J Biol Chem
The natural resistance-associated macrophage protein (Nramp) family encompasses transition metal and proton cotransporters that are present in many organisms from bacteria to humans. Recent structures of Deinococcus radiodurans Nramp (DraNramp) in mu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e867766e8689b897aca78589484cca7f
https://doi.org/10.1074/jbc.ra119.011336
https://doi.org/10.1074/jbc.ra119.011336
Publikováno v:
The Journal of General Physiology
An Nramp transition metal transporter performs metal uniport, proton uniport, and proton–metal cotransport. Transmembrane voltage and pH gradients govern the rates of these processes, largely through a conserved salt-bridge network in the transmemb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7fcf6f3b3f1b78afc58c81d7bc764663
https://doi.org/10.1085/jgp.201912428
https://doi.org/10.1085/jgp.201912428
Autor:
Elizabeth M. Nolan, Aaron T. Bozzi
Publikováno v:
Biochemistry
The calgranulins form a class of S100 proteins in higher vertebrates that innate-immune cells release in abundance at infection sites. These proteins function by binding transition metal ions to prevent microbial pathogens from obtaining those essent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f241e0464bdcd22c335b2e42bd6d944
https://europepmc.org/articles/PMC7031041/
https://europepmc.org/articles/PMC7031041/
Autor:
Helen O. Leung, Mark D. Marshall, Aaron T. Bozzi, Jonah R. Horowitz, Andres C. Nino, Hannah K. Tandon, Leonard Yoon
Publikováno v:
Journal of Molecular Spectroscopy. 381:111520
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2cd2b6f575b2588d6a371c45ceb51eaf
https://doi.org/10.1016/j.jms.2021.111520
https://doi.org/10.1016/j.jms.2021.111520
Autor:
Rachelle Gaudet, Aaron T. Bozzi
Publikováno v:
J Mol Biol
The Natural resistance-associated macrophage protein (Nramp) family of transition metal transporters enables uptake and trafficking of essential micronutrients that all organisms must acquire to survive. Two decades after Nramps were identified as pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80516bfed3f7ac2b1a7f979c19e58e50
https://doi.org/10.1016/j.jmb.2021.166991
https://doi.org/10.1016/j.jmb.2021.166991
The natural resistance-associated macrophage protein (Nramp) family encompasses transition metal and proton co-transporters found in organisms from bacteria to humans. Recent structures ofDeinococcus radiodurans(Dra)Nramp in multiple conformations re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04f6336c207783a3f1a9d6f5521cde1d
Autor:
Christina M Zimanyi, Casey H Zhang, Aaron T. Bozzi, Brandon Lee, John M. Nicoludis, Rachelle Gaudet
Publikováno v:
eLife
eLife, Vol 8 (2019)
eLife, Vol 8 (2019)
Nramp family transporters—expressed in organisms from bacteria to humans—enable uptake of essential divalent transition metals via an alternating-access mechanism that also involves proton transport. We present high-resolution structures of Deino
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::463ec2954e1698b190f0c7033de4bf93
http://europepmc.org/articles/PMC6398981
http://europepmc.org/articles/PMC6398981