Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Robert H. Guy"'
Autor:
Steffen Hering, Stanislav Beyl, Anna Stary, Eugen Timin, Michaela Kudrnac, Annette Hohaus, Robert H. Guy
Publikováno v:
Journal of Biological Chemistry. 282:3864-3870
Voltage-gated calcium channels are in a closed conformation at rest and open temporarily when the membrane is depolarized. To gain insight into the molecular architecture of Cav1.2, we probed the closed and open conformations with the charged phenyla
Autor:
Eugen Timin, Khac-Minh Thai, Andrea Schiesaro, A. Windisch, Anna Weinzinger, Daniela Stork, Steffen Hering, Robert H. Guy, Gerhard F. Ecker
Publikováno v:
ChemMedChem. 5(3)
The inner cavity of the hERG potassium ion channel can accommodate large, structurally diverse compounds that can be trapped in the channel by closure of the activation gate. A small set of propafenone derivatives was synthesized, and both use-depend
Autor:
Andriy Anishkin, Adina L. Milac, Sarosh N. Fatakia, Robert H. Guy, Carson C. Chow, Sergei Sukharev
Publikováno v:
ResearcherID
Two-pore-domain background potassium (K2P) channels comprise a distinct gene family of widely distributed, well modulated channels. K2P channels have two similar or identical subunits, each of which has four transmembrane (TM) and two pore-forming (P
Autor:
Robert H. Guy, Eugen Timin, Michaela Kudrnac, Steffen Hering, Stanislav Beyl, Anna Stary, Annette Hohaus
Publikováno v:
Channels (Austin, Tex.). 2(2)
Calcium channel family members activate at different membrane potentials, which enables tissue specific calcium entry. Pore mutations affecting this voltage dependence are associated with channelopathies. In this review we analyze the link between vo
Autor:
Mutsumi Yamagami, Naoki Kato, Akihiro Hazama, Masaro Akai, Shinobu Goshima, Lalu Zulkifli, Nobuyuki Matsuda, Robert H. Guy, Nobuyuki Uozumi, Yasuhiro Kato
Publikováno v:
ResearcherID
Studies suggest that Ktr/Trk/HKT-type transporters have evolved from multiple gene fusions of simple K(+) channels of the KcsA type into proteins that span the membrane at least eight times. Several positively charged residues are present in the eigh
Autor:
Stanislav, Beyl, Eugen N, Timin, Annette, Hohaus, Anna, Stary, Michaela, Kudrnac, Robert H, Guy, Steffen, Hering
Publikováno v:
The Journal of biological chemistry. 282(6)
Voltage-gated calcium channels are in a closed conformation at rest and open temporarily when the membrane is depolarized. To gain insight into the molecular architecture of Ca(v)1.2, we probed the closed and open conformations with the charged pheny