"Solute carrier 11 cation symport requires distinct residues in transmembrane helices 1 and 6." . "Solute carrier 11 cation symport requires distinct residues in transmembrane helices 1 and 6."@en . . . "Journal of Biological Chemistry" . . . . . "395828" . "Urb\u00E1nkov\u00E1, Eva" . "Rensing, Christopher" . . "[AFB0D81695C2]" . . . . "Solute carrier 11 cation symport requires distinct residues in transmembrane helices 1 and 6."@cs . "Solute carrier 11 cation symport requires distinct residues in transmembrane helices 1 and 6." . . "RIV/00216208:11320/08:00100281" . . "6"^^ . "0021-9258" . "Solute carrier 11 cation symport requires distinct residues in transmembrane helices 1 and 6."@en . "000254671600019" . "Quick, Matthias" . "Cellier, Mathieu" . "US - Spojen\u00E9 st\u00E1ty americk\u00E9" . . "RIV/00216208:11320/08:00100281!RIV09-MSM-11320___" . "Solute; carrier; cation; symport; requires; distinct; residues; transmembrane; helices"@en . . "P(GA204/07/0558), Z(MSM0021620835)" . . "283" . "Ubiquitous solute carriers 11 (SLC11) contribute to metal-ion homeostasis by importing Me(2+) and H(+) into the cytoplasm. To identify residues mediating cation symport, Escherichia coli proton-dependent manganese transporter (MntH) was mutated at five SLC11-specific transmembrane (TM) sites; each mutant activity was compared with wild-type MntH, and the biochemical results were tested by homology threading. Cd(2+) and H(+) uptake kinetics were analyzed in whole cells as a function of pH and temperature, and right-side out membrane vesicles were used to detail energy requirements and to probe site accessibility by Cys replacement and thiol modification. This approach revealed that..."@cs . "Courville, Pascal" . . . "Chaloupka, Roman" . "2"^^ . "Ubiquitous solute carriers 11 (SLC11) contribute to metal-ion homeostasis by importing Me(2+) and H(+) into the cytoplasm. To identify residues mediating cation symport, Escherichia coli proton-dependent manganese transporter (MntH) was mutated at five SLC11-specific transmembrane (TM) sites; each mutant activity was compared with wild-type MntH, and the biochemical results were tested by homology threading. Cd(2+) and H(+) uptake kinetics were analyzed in whole cells as a function of pH and temperature, and right-side out membrane vesicles were used to detail energy requirements and to probe site accessibility by Cys replacement and thiol modification. This approach revealed that..."@en . . . "15" . "11320" . . "Ubiquitous solute carriers 11 (SLC11) contribute to metal-ion homeostasis by importing Me(2+) and H(+) into the cytoplasm. To identify residues mediating cation symport, Escherichia coli proton-dependent manganese transporter (MntH) was mutated at five SLC11-specific transmembrane (TM) sites; each mutant activity was compared with wild-type MntH, and the biochemical results were tested by homology threading. Cd(2+) and H(+) uptake kinetics were analyzed in whole cells as a function of pH and temperature, and right-side out membrane vesicles were used to detail energy requirements and to probe site accessibility by Cys replacement and thiol modification. This approach revealed that..." . . "Solute carrier 11 cation symport requires distinct residues in transmembrane helices 1 and 6."@cs . . . "8"^^ . .