Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Balasundaresan Dhakshnamoorthy"'
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Tetrameric cationic channels specificity is determined by the sequence and structural conformation of their selectivity filter. Here, the authors show that a cationic channel from Tsukamurella paurometabola is non-selective due to a Ca2+-binding moti
Externí odkaz:
https://doaj.org/article/54ddb1f1acfa493bbfb0cb50effbba4f
Autor:
Gopinath, Subash C. B.1, Balasundaresan, Dhakshnamoorthy1, Akitomi, Joe2, Mizuno, Hiroshi2 mizuno-hiroshi@aist.go.jp
Publikováno v:
Journal of Biochemistry. Nov2006, Vol. 140 Issue 5, p667-676. 10p.
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-11 (2016)
Nature Communications
Nature Communications
The selectivity filter is an essential functional element of K+ channels that is highly conserved both in terms of its primary sequence and its three-dimensional structure. Here, we investigate the properties of an ion channel from the Gram-positive
OmpF, a multiionic porin from Escherichia coli, is a useful protypical model system for addressing general questions about electrostatic interactions in the confinement of an aqueous molecular pore. Here, favorable anion locations in the OmpF pore we
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::740c2ead4439128f8b1f8c35af5a7483
https://europepmc.org/articles/PMC3868647/
https://europepmc.org/articles/PMC3868647/
Publikováno v:
Journal of structural biology. 183(3)
Anti-terminator proteins control gene expression by recognizing control signals within cognate transcripts and then preventing transcription termination. HutP is such a regulatory protein that regulates the expression of the histidine utilization ( h
The OmpF porin from the Escherichia coli outer membrane folds into a trimer of beta-barrels, each forming a wide aqueous pore allowing the passage of ions and small solutes. A long loop (L3) carrying multiple acidic residues folds into the beta-barre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c641fb5224023d639a4876dde239d23
https://europepmc.org/articles/PMC3584447/
https://europepmc.org/articles/PMC3584447/
Permeation Pathways of Cations and Anions in the OmpF Porin Channel using Anomalous X-Ray Scattering
Publikováno v:
Biophysical Journal. 104:183a
The outer membrane of Gram-negative bacteria is a highly specialized structure that lies outside the cytoplasmic membrane and peptidoglycan layer and forms the interface between the cell and its external environment. The outer membrane constitutes a
Publikováno v:
Acta Crystallographica Section A Foundations of Crystallography. 64:C350-C350
Akademický článek
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Autor:
Utsunomiya, Ryuji, Suto, Kyoko, Balasundaresan, Dhakshnamoorthy, Fukamizu, Akiyoshi, Kumar, Penmetcha K. R., Mizuno, Hiroshi
Publikováno v:
Acta Crystallographica: Section D (Wiley-Blackwell); Mar2006, Vol. 62 Issue 3, p331-338, 8p, 7 Diagrams, 1 Chart