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Alteration of Epithelial Structure and Function Associated with PtdIns(4,5)P2 Degradation by a Bacterial Phosphatase

David Mason,Gustavo V. Mallo,Mauricio R. Terebiznik,Bernard Payrastre,B. Brett Finlay,John H. Brumell,Lucia Rameh,Sergio Grinstein
View Articletitled, Alteration of Epithelial Structure and Function Associated with PtdIns(4,5)P<sub>2</sub> Degradation by a Bacterial Phosphatase

G551D and G1349D, Two CF-associated Mutations in the Signature Sequences of CFTR, Exhibit Distinct Gating Defects

Silvia G. Bompadre,Yoshiro Sohma,Min Li,Tzyh-Chang Hwang
View Articletitled, G551D and G1349D, Two CF-associated Mutations in the Signature Sequences of CFTR, Exhibit Distinct Gating Defects

Structural Determinants of the Closed KCa3.1 Channel Pore in Relation to Channel Gating: Results from a Substituted Cysteine Accessibility Analysis

Hélène Klein,Line Garneau,Umberto Banderali,Manuel Simoes,Lucie Parent,Rémy Sauvé
View Articletitled, Structural Determinants of the Closed KCa3.1 Channel Pore in Relation to Channel Gating: Results from a Substituted Cysteine Accessibility Analysis

Uncoupling and Turnover in a Cl−/H+ Exchange Transporter

Michael Walden,Alessio Accardi,Fang Wu,Chen Xu,Carole Williams,Christopher Miller
View Articletitled, Uncoupling and Turnover in a Cl<sup>−</sup>/H<sup>+</sup> Exchange Transporter

Cooperation of the Conserved Aspartate 439 and Bound Amino Acid Substrate Is Important for High-Affinity Na+ Binding to the Glutamate Transporter EAAC1

Zhen Tao,Christof Grewer
View Articletitled, Cooperation of the Conserved Aspartate 439 and Bound Amino Acid Substrate Is Important for High-Affinity Na<sup>+</sup> Binding to the Glutamate Transporter EAAC1

Communication

A Conformation Change in the Extracellular Domain that Accompanies Desensitization of Acid-sensing Ion Channel (ASIC) 3

Kenneth A. Cushman,Josephine Marsh-Haffner,John P. Adelman,Edwin W. McCleskey
View Articletitled, A Conformation Change in the Extracellular Domain that Accompanies Desensitization of Acid-sensing Ion Channel (ASIC) 3