Chaperone-assisted E3 ligase CHIP: A double agent in cancer - ScienceDirect
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The E3 ubiquitin ligase CHIP in normal cell function and in disease conditions - Wang - 2020 - Annals of the New York Academy of Sciences - Wiley Online Library
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CHIP Is a U-box-dependent E3 Ubiquitin Ligase: IDENTIFICATION OF Hsc70 AS A TARGET FOR UBIQUITYLATION - ScienceDirect
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Specificity for latent C termini links the E3 ubiquitin ligase CHIP to caspases | Nature Chemical Biology
CHIP E3 ligase mediates proteasomal degradation of the proliferation regulatory protein ALDH1L1 during the transition of NIH3T3 fibroblasts from G0/G1 to S-phase | PLOS ONE
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Chaperone-assisted E3 ligase CHIP: A double agent in cancer - ScienceDirect
The E3 Ubiquitin Ligase CHIP and the Molecular Chaperone Hsc70 Form a Dynamic, Tethered Complex | Biochemistry
