LMP7 Inhibitors

LMP7, a proteasomal subunit crucial for protein degradation, can be selectively or non-selectively inhibited by various chemicals. ONX 0914, a selective LMP7 inhibitor, specifically targets its catalytic site within the proteasome, disrupting normal proteasomal function and altering protein degradation. PR-825, another potent and selective LMP7 inhibitor, interferes with LMP7's proteolytic activity, exerting inhibitory effects on the proteasome and influencing cellular processes associated with LMP7 activity. YU-101 is a reversible inhibitor of LMP7 that bind to its catalytic site, disrupting proteasome activity and modulating the degradation of ubiquitinated proteins, thereby affecting cellular processes regulated by LMP7. Ginkgolide B, a natural product, inhibits LMP7 activity, through modulation of proteasome structure, impacting proteasomal degradation and influencing cellular processes regulated by LMP7.

Salinosporamide A is an irreversible LMP7 inhibitor that covalently binds to its active site, disrupting the proteasome function and altering protein degradation. UK-101 is a reversible LMP7 inhibitor that specifically binds to LMP7's catalytic site, interfering with proteasomal function and influencing cellular processes regulated by LMP7 activity. β-Lapachone, a natural compound, has been suggested to inhibit LMP7, through modulation of the proteasome structure, impacting proteasomal degradation and influencing cellular processes regulated by LMP7. MG-132, a reversible proteasome inhibitor, indirectly modulates LMP7 activity by disrupting the degradation of ubiquitinated proteins within the broader proteasomal context. NLVS is a reversible LMP7 inhibitor that binds to the catalytic site of the proteasome, disrupting normal proteasomal function and altering protein degradation. GRL0617, a specific LMP7 inhibitor, targets its active site within the proteasome, disrupting proteasome function and influencing cellular processes regulated by LMP7 activity.