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BioID performed in HeLa cells for the TPR domain of The O-GlcNAc Transferase and eGFP (negative control). Used to determine TPR interactors and the TPR interactome in HeLa cells. Three biological replicates were performed, with each replicate having an experimental (TPR-BirA*) and negative (eGFP-Bir...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-06-24 | MSV000085626 | MassIVE
HDX-MS was used to establish that conformational-inhibition-signals extended from the TPR-domain to the U-box of CHIP. This underscores inter-domain allosteric regulation of CHIP by the core molecular chaperones. Defining the chaperone-associated TPR-domain of CHIP as a manager of inter-domain commu...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2015-07-30 | MSV000079205 | MassIVE
OGT’s tetratricopeptide(TPR) domain is important in substrate recognition, but there is little information on how changing the TPR domain impacts its cellular functions. Here, we investigate how altering OGT’s TPR domain impacts cell growth after the endogenous enzyme is deleted. We find that disrup...
ORGANISM(S): Mus musculus (Mouse) 
2024-05-06 | PXD052018 | Pride
Nucleocytoplasmic O-linked N-acetylglucosamine (O-GlcNAc) is an essential post-translational modification that is installed to thousands of protein substrates by O-GlcNAc transferase (OGT). Substrate selection by OGT and its isoforms is primarily mediated by the tetratricopeptide repeat (TPR) domain...
ORGANISM(S): Homo sapiens (Human) 
2021-11-01 | PXD028141 | Pride
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