Conserved Residues Lys<sup>57</sup> and Lys<sup>401</sup> of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation.

Caba, Cody; Ali Khan, Hyder; Auld, Janeen; Ushioda, Ryo; Araki, Kazutaka; Nagata, Kazuhiro; Mutus, Bulent

Conserved Residues Lys⁵⁷ and Lys⁴⁰¹ of Protein Disulfide Isomerase Maintain an Active Site Conformation for Optimal Activity: Implications for Post-Translational Regulation.

Caba, Cody; Ali Khan, Hyder; Auld, Janeen; Ushioda, Ryo; Araki, Kazutaka; Nagata, Kazuhiro; Mutus, Bulent.

Afiliação

Caba C; Department of Chemistry and Biochemistry, University of Windsor, Windsor, ON, Canada.
Ali Khan H; Department of Chemistry and Biochemistry, University of Windsor, Windsor, ON, Canada.
Auld J; Department of Chemistry and Biochemistry, University of Windsor, Windsor, ON, Canada.
Ushioda R; Laboratory of Molecular and Cellular Biochemistry, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Araki K; Molecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan.
Nagata K; Laboratory of Molecular and Cellular Biochemistry, Faculty of Life Sciences, Kyoto Sangyo University, Kyoto, Japan.
Mutus B; Department of Chemistry and Biochemistry, University of Windsor, Windsor, ON, Canada.

Front Mol Biosci ; 5: 18, 2018.

Article em En | MEDLINE | ID: mdl-29541639