The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity

Journal of Virology

Volumn 80, Issue 7, 2006, Pages 3322-3331

  Pérez Vargas, Jimena ^a   Romero, Pedro ^a   López, Susana ^a   Arias, Carlos F ^a  

^a INSTITUTO DE BIOTECNOLOGÍA   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; COMPLEMENTARY DNA; HEAT SHOCK COGNATE PROTEIN 70; MONOCLONAL ANTIBODY; POLYCLONAL ANTIBODY; RECOMBINANT PROTEIN;

ANIMAL CELL; ANTIBODY DETECTION; ARTICLE; DIARRHEA; ENZYME LINKED IMMUNOSORBENT ASSAY; IMMUNOBLOTTING; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN BINDING; ROTAVIRUS; TEMPERATURE SENSITIVITY; VIRUS CELL INTERACTION; VIRUS INFECTION; VIRUS PARTICLE;

ADENOSINE TRIPHOSPHATASES; ANIMALS; CELL LINE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME-LINKED IMMUNOSORBENT ASSAY; HSC70 HEAT-SHOCK PROTEINS; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; IMMUNOBLOTTING; LIGANDS; LUCIFERASES; PERMEABILITY; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; ROTAVIRUS; ROTAVIRUS INFECTIONS; SOLUTIONS;

ANIMALIA; ROTAVIRUS;

EID: 33645212832     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.80.7.3322-3331.2006     Document Type: Article

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