Novel structural features drive DNA binding properties of Cmr, a CRP family protein in TB complex mycobacteriaNUCLEIC ACIDS RESEARCHIF13.12017-11-206OAAI
Structures of paraoxon-inhibited human acetylcholinesterase reveal perturbations of the acyl loop and the dimer interfacePROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICSIF2.82016-06-0374PREAI
Structural insights into mis-regulation of protein kinase A in human tumorsPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICAIF9.12015-01-2091OAAI
Conformational ensemble of the sodium-coupled aspartate transporterNATURE STRUCTURAL & MOLECULAR BIOLOGYIF10.12013-01-20120OAAI
The iodide-transport-defect-causing mutation R124H: a δ-amino group at position 124 is critical for maturation and trafficking of the Na+/I- symporterJOURNAL OF CELL SCIENCEIF3.62013-01-0128OAAI
Molecular characterization of V59E NIS, a Na+/I- symporter mutant that causes congenital I- transport defectENDOCRINOLOGYIF3.32008-08-1333OAAI
Amino acid residues in transmembrane segment IX of the Na+/I- symporter play a role in its Na+ dependence and are critical for transport activityJOURNAL OF BIOLOGICAL CHEMISTRYIF3.92007-08-0159OAAI
The Q267E mutation in the sodium/iodide symporter (NIS) causes congenital iodide transport defect (ITD) by decreasing the NIS turnover numberJOURNAL OF CELL SCIENCEIF3.62004-02-1553OAAI
Journey of the iodide transporter NIS:: from its molecular identification to its clinical role in cancerTRENDS IN BIOCHEMICAL SCIENCESIF112001-08-0161PREAI
N-linked glycosylation of the thyroid Na+/I- symporter (NIS) -: Implications for its secondary structure modelJOURNAL OF BIOLOGICAL CHEMISTRYIF3.91998-08-01179OAAI
Identification of a structural requirement for thyroid Na+/I- symporter (NIS) function from analysis of a mutation that causes human congenital hypothyroidismFEBS LETTERSIF31998-06-2572OA
Characterization of the thyroid Na+/I- symporter with an anti-COOH terminus antibodyPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICAIF9.11997-05-27218OAAI
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