The angiotensin receptor-associated protein Atrap is a stimulator of the cardiac Ca2+-ATPase SERCA2a

Cardiovascular Research

Volumn 110, Issue 3, 2016, Pages 359-370

  Mederle, Katharina ^a   Gess, Bernhard ^a   Pluteanu, Florentina ^b   Plackic, Jelena ^b   Tiefenbach, Klaus Jürgen ^a   Grill, Alexandra ^a   Kockskämper, Jens ^b   Castrop, Hayo ^a  

^a UNIVERSITY OF REGENSBURG   (Germany)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

Agtrap; Atrap; Ca ATPase; SERCA2a

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ANGIOTENSIN 1 RECEPTOR; ANGIOTENSIN II TYPE 1 RECEPTOR ASSOCIATED PROTEIN; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; UNCLASSIFIED DRUG; AGTRAP PROTEIN, MOUSE; ATP2A2 PROTEIN, MOUSE; HOMEODOMAIN PROTEIN; PROTEIN BINDING; SIGNAL TRANSDUCING ADAPTOR PROTEIN; TLX2 PROTEIN, MOUSE;

ANIMAL CELL; ARTICLE; ASSAY; CALCIUM TRANSPORT; CARDIAC MUSCLE CELL; CELL ISOLATION; CONTROLLED STUDY; GENE SEQUENCE; GENOTYPE; HEART EJECTION FRACTION; HEART LEFT VENTRICLE FUNCTION; HEART RATE; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; IN VIVO STUDY; MASS SPECTROMETRY; MEMBRANE VESICLE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; SARCOMERE; SPECTROSCOPY; SURFACE PLASMON RESONANCE; WILD TYPE; 129 MOUSE; ANIMAL; C57BL MOUSE; CALCIUM SIGNALING; DEFICIENCY; DIASTOLE; ENZYME ACTIVATION; ENZYMOLOGY; GENETIC TRANSFECTION; GENETICS; HEK293 CELL LINE; KNOCKOUT MOUSE; MATRIX-ASSISTED LASER DESORPTION-IONIZATION MASS SPECTROMETRY; METABOLISM; PROCEDURES; PROTEOMICS; SARCOPLASMIC RETICULUM;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; ANIMALS; CALCIUM SIGNALING; DIASTOLE; ENZYME ACTIVATION; HEK293 CELLS; HOMEODOMAIN PROTEINS; HUMANS; IMMUNOPRECIPITATION; MICE, 129 STRAIN; MICE, INBRED C57BL; MICE, KNOCKOUT; MYOCYTES, CARDIAC; PROTEIN BINDING; PROTEOMICS; SARCOMERES; SARCOPLASMIC RETICULUM; SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SURFACE PLASMON RESONANCE; TRANSFECTION; VENTRICULAR FUNCTION, LEFT;

EID: 84973402613     PISSN: 00086363     EISSN: 17553245     Source Type: Journal    
DOI: 10.1093/cvr/cvw064     Document Type: Article

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