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The molecular mechanism of fluoride export by the eukaryotic fluoride channel FEX. [PDF]
Kang CY +5 more
europepmc +1 more source
Comparison among Amber-ff14SB, Amber-ff19SB, and CHARMM36 Force Fields for Ionic and Electroosmotic Flows in Biological Nanopores. [PDF]
Gargano S +4 more
europepmc +1 more source
The Numerous Ways Glutamate Transporters can go Wrong. [PDF]
Eyal S.
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Transport domain of the erythrocyte anion exchange protein
The Journal of Membrane Biology, 1990The anion transport domain of the anion exchange protein (AEP) of human erythrocyte membranes (band 3, 95 kD mol wt) was probed with the substrate and affinity label pyridoxal-5'-phosphate (PLP). Acting from outside, this probe labels two chymotryptic fragments of 65 and 35 kD of AEP but only the 35-kD fragment is protected from labeling by reversibly ...
S, Bar-Noy, Z I, Cabantchik
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Life Sciences, 2000
The organic anion transporter 3 (rOAT3) is a multispecific OAT localized at the basolateral membrane of the proximal tubule. The purpose of this study was to elucidate the role of protein kinase C (PKC) in the regulation of organic anion transport driven by rOAT3 and its mechanism of action.
M, Takeda, T, Sekine, H, Endou
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The organic anion transporter 3 (rOAT3) is a multispecific OAT localized at the basolateral membrane of the proximal tubule. The purpose of this study was to elucidate the role of protein kinase C (PKC) in the regulation of organic anion transport driven by rOAT3 and its mechanism of action.
M, Takeda, T, Sekine, H, Endou
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Fluorescent stilbene (BADS) binding proteins in anion-transporting epithelia
American Journal of Physiology-Cell Physiology, 1990Chloride transport occurs at the interface between the internal and external environments of a cell where chloride uptake or efflux is regulated through a variety of mechanisms that involve cotransport of cations, exchange mechanism with anions, or movement through channels.
S F, Pearce, J A, Zadunaisky
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Catabolism of the anion transport protein in human erythrocytes
Biochemistry, 1985We identified the catabolic products of protein 3 in human erythrocytes. Protein 3, the major protein of the erythrocyte membrane, functions in anion transport and reacts covalently with tritiated 4,4'-diisothiocyano-1,2-diphenylethane-2,2'-disulfonic acid ([3H]DIDS), a very selective inhibitor of anion transport.
M, Morrison +4 more
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The erythrocyte anion transport protein is cotranslationally inserted into microsomes
Cell, 1982The biosynthesis of the erythrocyte anion transport protein, Band III (molecular weight 100,000), is of interest, as its NH2-terminal half is hydrophilic and faces the cytoplasmic surface, and its COOH-terminal half spans the phospholipid bilayer several times.
W A, Braell, H F, Lodish
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Association Of An Integral Membrane Protein With Glucose Transport And With Anion Transport
Journal of Cell Science, 1984ABSTRACT A monoclonal antibody that recognizes a cell-surface glycoprotein associated with glucose transport was reported previously. Additional information about the function and intracellular distribution of the antigen recognized by this antibody is presented.
M R, Banyard, M K, White
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The Journal of Pharmacology and Experimental Therapeutics, 1999
Transport characteristics of 17beta-estradiol 17beta-D-glucuronide (E217betaG), a dual substrate of the transporters for cellular uptake (organic anion-transporting polypeptide 1 or oatp1) and cellular excretion (multidrug resistance-associated protein 1or MRP1), in the rat choroid plexus were studied in vivo and in vitro.
J, Nishino +6 more
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Transport characteristics of 17beta-estradiol 17beta-D-glucuronide (E217betaG), a dual substrate of the transporters for cellular uptake (organic anion-transporting polypeptide 1 or oatp1) and cellular excretion (multidrug resistance-associated protein 1or MRP1), in the rat choroid plexus were studied in vivo and in vitro.
J, Nishino +6 more
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