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pro vyhledávání: '"Christopher Miller"'
Autor:
Christopher Miller
Publikováno v:
The Journal of General Physiology
Among coupled exchangers, CLCs uniquely catalyze the exchange of oppositely charged ions (ClCells are shielded from harmful molecules and other threats by a thin, flexible layer called the membrane. However, this barrier also prevents chloride, sodiu
Autor:
Nicholas B. Last, Christopher Miller
Publikováno v:
Journal of Molecular Biology. 427:3607-3612
Anion channels and antiporters of the ClC superfamily have been found to be exclusively dimeric in nature, even though each individual monomer contains the complete transport pathway. Here, we describe the destabilization through mutagenesis of the d
Autor:
Nicholas B. Last, Randy B. Stockbridge, Ashley E. Wilson, Tania Shane, Ludmila Kolmakova-Partensky, Akiko Koide, Shohei Koide, Christopher Miller
Fluoride/proton antiporters of the CLCF family combat F- toxicity in bacteria by exporting this halide from the cytoplasm. These transporters belong to the widespread CLC superfamily but display transport properties different from those of the well-s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afd57177a431f8740a095c03684f73f5
https://europepmc.org/articles/PMC6044475/
https://europepmc.org/articles/PMC6044475/
Publikováno v:
The Journal of General Physiology
Two subclades of the CLCF-type F−/H+ antiporters show differences in F−/Cl− selectivity.
Many bacterial species protect themselves against environmental F− toxicity by exporting this anion from the cytoplasm via CLCF F−/H+ antiporters,
Many bacterial species protect themselves against environmental F− toxicity by exporting this anion from the cytoplasm via CLCF F−/H+ antiporters,
Publikováno v:
The Journal of General Physiology
The leucine zipper, EF hand–containing transmembrane protein 1 (Letm1) gene encodes a mitochondrial inner membrane protein, whose depletion severely perturbs mitochondrial Ca2+ and K+ homeostasis. Here we expressed, purified, and reconstituted huma
Autor:
Renee Otten, Christopher Miller, Carole Williams, Tania Shane, Zasha Weinberg, Hyun Ho Lim, Randy B. Stockbridge
Publikováno v:
Proceedings of the National Academy of Sciences. 109:15289-15294
A subclass of bacterial CLC anion-transporting proteins, phylogenetically distant from long-studied CLCs, was recently shown to be specifically up-regulated by F - . We establish here that a set of randomly selected representatives from this “CLC F
Publikováno v:
Biochemistry. 51:1577-1585
From the viewpoint of enteric bacteria, the mammalian stomach, where pH can fall as low as 1.5, is a potentially lethal barrier that must be surmounted to colonize the intestinal tract. Many bacteria breach this host defense by activating multiple ex
Autor:
Christopher Miller, Hyun-Ho Lim
Publikováno v:
The Journal of General Physiology
CLC-ec1, a bacterial homologue of the CLC family's transporter subclass, catalyzes transmembrane exchange of Cl(-) and H(+). Mutational analysis based on the known structure reveals several key residues required for coupling H(+) to the stoichiometri
Publikováno v:
The Journal of General Physiology
The CLC-family protein CLC-ec1, a bacterial homologue of known structure, stoichiometrically exchanges two Cl(-) for one H(+) via an unknown membrane transport mechanism. This study examines mutations at a conserved tyrosine residue, Y445, that direc
Publikováno v:
Journal of Biological Chemistry. 282:176-182
The arginine-dependent extreme acid resistance response of Escherichia coli operates by decarboxylating arginine. AdiC, a membrane antiporter, catalyzes arginine influx coupled to efflux of the decarboxylation product agmatine, effectively exporting