L
Ludmila Kolmakova-Partensky
Researcher at Howard Hughes Medical Institute
Publications - 10
Citations - 1066
Ludmila Kolmakova-Partensky is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: Antiporter & Arginine. The author has an hindex of 9, co-authored 10 publications receiving 983 citations. Previous affiliations of Ludmila Kolmakova-Partensky include Brandeis University.
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Journal ArticleDOI
Structure of a prokaryotic virtual proton pump at 3.2 A resolution.
Yiling Fang,Hariharan Jayaram,Tania Shane,Ludmila Kolmakova-Partensky,Fang Wu,Carole Williams,Yong Xiong,Christopher Miller +7 more
TL;DR: A crystal structure of AdiC is described, which shows that the protein is captured in an outward-open, substrate-free conformation with transmembrane architecture remarkably similar to that seen in four other families of apparently unrelated transport proteins.
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Functional Reconstitution of a Prokaryotic K+ Channel
TL;DR: SliK-mediated ionic flux shows strong selectivity for K+ over Na+ and is inhibited by micromolar concentrations of Ba2+, mirroring the basic permeation characteristic of eukaryotic K+ channels studied by electrophysiological methods.
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Ionic currents mediated by a prokaryotic homologue of CLC Cl- channels.
TL;DR: Mutation of a conserved glutamate residue found in the selectivity filter eliminates the pH-dependence of both currents and 36Cl− flux and appears to trap CLC-ec1 in a constitutively active state, which correlate well with known characteristics of eukaryotic CLC channels.
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Three-dimensional structure of a voltage-gated potassium channel at 2.5 nm resolution.
TL;DR: The two-domain architecture of the Shaker channel is consistent with the recently proposed "hanging gondola" model for the T1 domain, putting the T2 domain at a distance from the membrane domain but attached to it by thin connectors, allowing cytoplasmic access of ions and the N-terminal inactivation domain to the pore region.
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A family of fluoride-specific ion channels with dual-topology architecture
TL;DR: It is shown that a recently discovered family of F− exporter proteins, purified and reconstituted in liposomes and planar phospholipid bilayers, form constitutively open anion channels with extreme selectivity for F− over Cl−.