IndraLab

Statements


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sparser
"However, it is possible that the interaction between SREBP2 and USP28 is indirect and involves additional, unknown proteins."

sparser
"It has also been demonstrated that USP28 binds to mature SREBP2, leading to its deubiquitination and stabilization."

sparser
"While both proteins localise to and interact in the nucleus, we did observe some level of interaction of SREBP2 and USP28 also in the cytoplasm."

sparser
"Moreover, mature SREBP2 binds to USP28, leading to deubiquitination and stabilization, as well as regulation of the mevalonate pathway (MVP), which drives the synthesis of cholesterol, thus driving tu[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Notably, it is unclear whether the interaction between SREBP2 and USP28 is direct or whether it involves additional proteins."

reach
"However, it is possible that the interaction between SREBP2 and USP28 is indirect and involves additional, unknown proteins."

reach
"While both proteins localise to and interact in the nucleus, we did observe some level of interaction of SREBP2 and USP28 also in the cytoplasm."

reach
"Notably, it is unclear whether the interaction between SREBP2 and USP28 is direct or whether it involves additional proteins.USP28 is highly upregulated in LSCC, where it stabilises the transcription factor ΔNP63 that is essential for the maintenance of the squamous lineage [16]."

reach
"Moreover, mature SREBP2 binds to USP28, leading to deubiquitination and stabilization, as well as regulation of the mevalonate pathway (MVP), which drives the synthesis of cholesterol, thus driving tu[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"We also show that USP28 binds to mature SREBP2, leading to its deubiquitination and stabilisation."

sparser
"Studies have discovered an interaction between SREBP2 and USP28, with both co-localizing in the nucleus of LSCC cells."