U2 snRNP B Inhibitors

Chemical inhibitors of U2 snRNP B play a crucial role in modulating the process of RNA splicing by interacting with components of the spliceosome. Pladienolide B and its derivative E7107 can bind directly to the SF3b complex within the spliceosome, leading to the disruption of its assembly and function. This interaction prevents U2 snRNP B from performing its essential role in RNA splicing. Similarly, Meayamycin B targets the SF3b complex, leading to a compromised spliceosome and the inhibition of U2 snRNP B's contribution to RNA processing. Herboxidiene, also known by the name GEX1A, binds to the same complex, adding to the list of molecules that hinder the activity of the spliceosome and thus U2 snRNP B's role within it.

Furthermore, compounds such as Spliceostatin A, found in Pseudomonas bacteria, and FD-895 exert their inhibitory effects by binding to the spliceosome, which impedes the function of U2 snRNP B. Madrasin is another inhibitor that, by targeting the spliceosome, prevents the proper assembly and function of U2 snRNP B in RNA splicing. Isoginkgetin, a biflavonoid, disrupts the assembly process of the spliceosome, thereby limiting the capacity of U2 snRNP B to partake in splicing. Plaunotol, although its exact mechanism of action on the spliceosome is less characterized, is known to disrupt splicing, suggesting an inhibitory effect on U2 snRNP B. In addition, Tetrocarcin A affects the assembly and function of the spliceosome complex, leading to an inhibition of U2 snRNP B's function. Lastly, FR901464 is a compound that binds to the spliceosome, directly affecting the complex where U2 snRNP B operates and thus inhibiting its function in mRNA processing. Each of these chemical inhibitors, through their unique interactions with the spliceosomal components, effectively impede the RNA splicing process by targeting the activity of U2 snRNP B.