Protein-protein interactions modulate the docking-dependent E3-ubiquitin ligase activity of carboxy-terminus of Hsc70-interacting protein (CHIP)

• Main Authors: Narayan, V, Landré, V, Ning, J, Hernychova, L, Muller, P, Verma, C, Walkinshaw, M.D, Blackburn, E.A, Ball, K.L
• Other Authors: BIOLOGY (NU)
• Format: Article
• Published: 2020
• Subjects: carboxyl terminus of hsc70 interacting protein; chaperone; heat shock protein 70; interferon regulatory factor 1; protein p53; regulator protein; tetratricopeptide repeat protein; ubiquitin protein ligase E3; unclassified drug; proteasome; protein binding; STUB1 protein, human; ubiquitin protein ligase; allosterism; Article; binding affinity; binding site; biochemical analysis; carboxy terminal sequence; conformational transition; controlled study; deuterium hydrogen exchange; enzyme activity; enzyme specificity; human; mass spectrometry; molecular docking; molecular dynamics; mouse; mutation; nonhuman; priority journal; protein conformation; protein function; protein protein interaction; protein structure; regulatory mechanism; tetratricopeptide repeat; u box activity; ubiquitination; chemistry; cytology; gene expression; genetics; kinetics; lymphocyte; metabolism; molecular model; protein analysis; protein secondary structure; protein tertiary structure; tumor cell line; Allosteric Regulation; Binding Sites; Cell Line, Tumor; Gene Expression; HSP70 Heat-Shock Proteins; Humans; Interferon Regulatory Factor-1; Kinetics; Lymphocytes; Models, Molecular; Proteasome Endopeptidase Complex; Protein Binding; Protein Interaction Mapping; Protein Structure, Secondary; Protein Structure, Tertiary; Tumor Suppressor Protein p53; Ubiquitin-Protein Ligases; Ubiquitination
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/181422
• Institution: National University of Singapore

10.1074/mcp.M115.051169