He, Yantao published the artcileA potent and selective inhibitor for the UBLCP1 proteasome phosphatase, Computed Properties of 39546-32-2, the publication is Bioorganic & Medicinal Chemistry (2015), 23(12), 2798-2809, database is CAplus and MEDLINE.
The ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1) has been implicated as a neg. regulator of the proteasome, a key mediator in the ubiquitin-dependent protein degradation Small mol. inhibitors that block UBLCP1 activity would be valuable as research tools and potential therapeutics for human diseases caused by the cellular accumulation of misfold/damaged proteins. The authors report a salicylic acid fragment-based library approach aimed at targeting both the phosphatase active site and its adjacent binding pocket for enhanced affinity and selectivity. Screening of the focused libraries led to the identification of the first potent and selective UBLCP1 inhibitor I. Compound I exhibits an IC50 of 1.0 μM for UBLCP1 and greater than 5-fold selectivity against a large panel of protein phosphatases from several distinct families. Importantly, the inhibitor possesses efficacious cellular activity and is capable of inhibiting UBLCP1 function in cells, which in turn up-regulates nuclear proteasome activity. These studies set the groundwork for further developing compound I into chem. probes or potential therapeutic agents targeting the UBLCP1 phosphatase.
Bioorganic & Medicinal Chemistry published new progress about 39546-32-2. 39546-32-2 belongs to piperidines, auxiliary class Piperidine,Amine,Amide, name is Piperidine-4-carboxamide, and the molecular formula is C6H12N2O, Computed Properties of 39546-32-2.
Referemce:
https://en.wikipedia.org/wiki/Piperidine,
Piperidine | C5H11N – PubChem