Calcium-binding protein 39 facilitates molecular interaction between Ste20p proline alanine-rich kinase and oxidative stress response 1 monomers

American Journal of Physiology - Cell Physiology

Volumn 303, Issue 11, 2012, Pages

  Ponce Coria, José ^a   Gagnon, Kenneth B ^b   Delpire, Eric ^a  

^a VANDERBILT UNIVERSITY MEDICAL CENTER   (United States)

^b UNIVERSITY OF SASKATCHEWAN   (Canada)

Author keywords

Cab39; Domain swap; Kinase dimerization; Na K 2Cl cotransporter; OSR1

Indexed keywords

ALANINE; CALCIUM BINDING PROTEIN; CALCIUM BINDING PROTEIN 39; GLUTAMINE; HETERODIMER; MONOMER; MUTANT PROTEIN; OXIDATIVE STRESS RESPONSE 1 PROTEIN; PROLINE; PROLINE ALANINE RICH KINASE STE20P; PROTEIN; PROTEIN KINASE; SODIUM POTASSIUM CHLORIDE COTRANSPORTER; SODIUM POTASSIUM CHLORIDE COTRANSPORTER 1; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVATION; FEMALE; MOLECULAR INTERACTION; NONHUMAN; NUCLEOTIDE SEQUENCE; OOCYTE; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; WILD TYPE; XENOPUS LAEVIS;

AMINO ACID SEQUENCE; ANIMALS; BIOLOGICAL TRANSPORT; CALCIUM-BINDING PROTEINS; CRYSTALLOGRAPHY, X-RAY; FEMALE; GLUTAMINE; HUMANS; MOLECULAR SEQUENCE DATA; OOCYTES; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, TERTIARY; PROTEIN-SERINE-THREONINE KINASES; SODIUM-POTASSIUM-CHLORIDE SYMPORTERS; XENOPUS LAEVIS;

XENOPUS LAEVIS;

EID: 84870494488     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00284.2012     Document Type: Article

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