Reductive activation of type 2 ribosome-inactivating proteins is promoted by transmembrane thioredoxin-related protein

Journal of Biological Chemistry

Volumn 287, Issue 10, 2012, Pages 7367-7373

  Pasetto, Matteo ^a   Barison, Erika ^a   Castagna, Monica ^a   Della Cristina, Pietro ^a   Anselmi, Cristina ^a   Colombatti, Marco ^a  

^a UNIVERSITY OF VERONA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

A549 CELLS; AFTER-TREATMENT; BINDING DOMAIN; CELL FRACTION; CELL LINES; CONTROL-CELL; CYTOTOXINS; DISULFIDE BONDS; ENDOPLASMIC RETICULUM; EUKARYOTIC CELLS; OXIDOREDUCTASES; POLYPEPTIDE CHAIN; PROTEIN DISULFIDE ISOMERASES; PSEUDOMONAS EXOTOXIN A; REDUCTIVE ACTIVATION; REDUCTIVE PROCESS; RIBOSOME-INACTIVATING PROTEIN; SAPORIN; TRANSMEMBRANES;

BACTERIA; CELL CULTURE; CELL MEMBRANES; COVALENT BONDS; ENZYME ACTIVITY;

PROTEINS;

ABRIN; GLUTATHIONE; MEMBRANE PROTEIN; PROTEIN DISULFIDE ISOMERASE; PSEUDOMONAS EXOTOXIN; PSEUDOMONAS EXOTOXIN A; RIBOSOME INACTIVATING PROTEIN 2; RICIN; SAPORIN; THIOREDOXIN LIKE TRANSMEMBRANE PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; CELL FRACTIONATION; CELL MEDIATED CYTOTOXICITY; CONTROLLED STUDY; DEGRADATION KINETICS; DISULFIDE BOND; HUMAN; HUMAN CELL; IN VITRO STUDY; INTERMETHOD COMPARISON; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEPLETION; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN METABOLISM; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SENSITIVITY ANALYSIS; WESTERN BLOTTING;

ABRIN; ADP RIBOSE TRANSFERASES; BACTERIAL TOXINS; CHEMICAL WARFARE AGENTS; ENDOPLASMIC RETICULUM; EXOTOXINS; HUMANS; JURKAT CELLS; MEMBRANE PROTEINS; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASES; PROTEIN SYNTHESIS INHIBITORS; RIBOSOME INACTIVATING PROTEINS, TYPE 1; RICIN; THIOREDOXINS; VIRULENCE FACTORS;

EUKARYOTA; PSEUDOMONAS EXOTOXIN;

EID: 84857746992     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.316828     Document Type: Article

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