Name
Abstract | ||
|---|---|---|
Structural modules that specifically recognize--or read--methylated or acetylated lysine residues on histone peptides are important components of chromatin-mediated signaling and epigenetic regulation of gene expression. Deregulation of epigenetic mechanisms is associated with disease conditions, and antagonists of acetyl-lysine binding bromodomains are efficacious in animal models of cancer and inflammation, but little is known regarding the druggability of methyl-lysine binding modules. We conducted a systematic structural analysis of readers of methyl marks and derived a predictive druggability landscape of methyl-lysine binding modules. We show that these target classes are generally less druggable than bromodomains, but that some proteins stand as notable exceptions. |
Year | DOI | Venue |
|---|---|---|
2011 | 10.1007/s10822-011-9505-2 | Journal of computer-aided molecular design |
Keywords | Field | DocType |
Druggability,Binding pocket,Methyl-lysine,Inhibitors,Epigenetics | Druggability,Bromodomain,Binding site,Histone,Biochemistry,Chemistry,Gene expression,Bioinformatics,Lysine,Acetylation,Epigenetics | Journal |
Volume | Issue | ISSN |
25 | 12 | 1573-4951 |
Citations | PageRank | References |
1 | 0.36 | 3 |
Authors | ||
3 | ||
Name | Order | Citations | PageRank |
|---|---|---|---|
| Calvin Santiago | 1 | 1 | 0.36 |
| Kong T. Nguyen | 2 | 11 | 1.63 |
| Matthieu Schapira | 3 | 21 | 4.41 |