Zobrazeno 1 - 10
of 220
pro vyhledávání: '"Giovanna Ferro-Luzzi Ames"'
Autor:
Giovanna Ferro-Luzzi Ames, Iris Xiaoyan Wang, Calvin Hu, Pei-Qi Liu, Cheng E. Liu, Kishiko Nikaido
Publikováno v:
Journal of Bioenergetics and Biomembranes. 33:79-92
The bacterial histidine permease, an ABC transporter, from Salmonella typhimurium is composed of a membrane-bound complex, HisQMP2, comprising two hydrophobic subunits (HisQ and HisM), two copies of an ATP-hydrolyzing subunit, HisP, and a soluble rec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3382f1b6f271729c4df95ace1f1d3d28
https://doi.org/10.1023/a:1010797029183
https://doi.org/10.1023/a:1010797029183
Publikováno v:
Biochemistry. 39:14183-14195
The membrane-bound complex of the Salmonella typhimurium histidine permease, an ABC transporter (or traffic ATPase), is composed of two membrane proteins, HisQ and HisM, and two identical copies of an ATP-hydrolyzing protein, HisP. We have developed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::af3eab066e0aa11e88ced324158231b8
https://doi.org/10.1021/bi001066+
https://doi.org/10.1021/bi001066+
Publikováno v:
Journal of Biological Chemistry. 274:18310-18318
The membrane-bound complex of the prokaryotic histidine permease, a periplasmic protein-dependent ABC transporter, is composed of two hydrophobic subunits, HisQ and HisM, and two identical ATP-binding subunits, HisP, and is energized by ATP hydrolysi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26c5c056e325d9492aca3791b3995f38
https://doi.org/10.1074/jbc.274.26.18310
https://doi.org/10.1074/jbc.274.26.18310
Publikováno v:
Journal of Biological Chemistry. 274:739-747
The histidine permease of Salmonella typhimurium is an ABC transporter (traffic ATPase). The liganded soluble receptor, the histidine-binding protein HisJ, interacts with the membrane-bound complex HisQMP2 and stimulates its ATPase activity, which re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e91a979242e74341c63fcab2bc3644d4
https://doi.org/10.1074/jbc.274.2.739
https://doi.org/10.1074/jbc.274.2.739
Autor:
Iris Xiaoyan Wang, Giovanna Ferro-Luzzi Ames, Kishiko Nikaido, Pei-Qi Liu, Sung-Hou Kim, Li-Wei Hung
Publikováno v:
Nature. 396:703-707
ABC transporters (also known as traffic ATPases) form a large family of proteins responsible for the translocation of a variety of compounds across membranes of both prokaryotes and eukaryotes. The recently completed Escherichia coli genome sequence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82a7182ad51398d22525d9841969ba44
https://doi.org/10.1038/25393
https://doi.org/10.1038/25393
Autor:
Pei-Qi Liu, Giovanna Ferro-Luzzi Ames
Publikováno v:
Proceedings of the National Academy of Sciences. 95:3495-3500
The membrane-bound complex of the Salmonella typhimurium periplasmic histidine permease, a member of the ABC transporters (or traffic ATPases) superfamily, is composed of two integral membrane proteins, HisQ and HisM, and two copies of an ATP-binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e6f69393c3c54e8b4b40fbbb0e98ee4
https://doi.org/10.1073/pnas.95.7.3495
https://doi.org/10.1073/pnas.95.7.3495
Publikováno v:
Journal of Biological Chemistry. 272:27745-27752
The nucleotide-binding subunit, HisP, of the histidine permease, a traffic ATPase (ABC transporter), has been purified as a soluble protein and characterized. Addition of a 6-histidine extension (HisP(His6)) allows a rapid and effective metal affinit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dbd726207377ccc88f3198db34590039
https://doi.org/10.1074/jbc.272.44.27745
https://doi.org/10.1074/jbc.272.44.27745
Publikováno v:
Journal of Biological Chemistry. 271:21243-21250
The periplasmic histidine permease of Salmonella typhimurium is composed of a membrane-bound complex and a soluble histidine-binding protein (the periplasmic receptor), HisJ. Liganded receptor interacts with the membrane-bound complex, inducing ATP h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::436d9a3028e20984c962e427d9f37681
https://doi.org/10.1074/jbc.271.35.21243
https://doi.org/10.1074/jbc.271.35.21243
Publikováno v:
Journal of Biological Chemistry. 271:14264-14270
The histidine-binding protein, HisJ, is the soluble receptor for the periplasmic histidine permease of Salmonella typhimurium. The receptor binds the substrate in the periplasm, interacts with the membrane-bound complex, transmits a transmembrane sig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ad342bff9e60a82bbc85a5433452410
https://doi.org/10.1074/jbc.271.24.14264
https://doi.org/10.1074/jbc.271.24.14264
Autor:
Hendrik De Bondt, Anil K. Joshi, Giovanna Ferro-Luzzi Ames, Amnon Wolf, Byung-Ha Oh, Eudean W. Shaw
Publikováno v:
Journal of Biological Chemistry. 270:16097-16106
The periplasmic histidine-binding protein, HisJ, is a receptor for the histidine permease of Salmonella typhimurium. Receptors of this type are composed of two lobes that are far apart in the unliganded structure (open conformation) and drawn close t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::731c55a60407b776dbdb29fbc58668cf
https://doi.org/10.1074/jbc.270.27.16097
https://doi.org/10.1074/jbc.270.27.16097