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This topic has appeared in the trending rankings 1 time(s) in the past year. While it does not trend frequently, its appearance suggests a renewed or concentrated surge of public interest.
Based on Wikipedia pageviews and search interest, this topic gained significant attention on the selected date.
Bromodomain entered the ranking for the first time today at position #. This is its highest position ever recorded.
This topic has appeared in the English Wikipedia rankings 1 time. It first appeared on 2026-04-15 and was most recently seen on 2026-04-15.
A bromodomain is an approximately 110 amino acid protein domain that recognizes acetylated lysine residues, such as those on the N-terminal tails of histones. Bromodomains, as the "readers" of lysine acetylation, are responsible in transducing the signal carried by acetylated lysine residues and translating it into various normal or abnormal phenotypes. Their affinity is higher for regions where multiple acetylation sites exist in proximity. This recognition is often a prerequisite for protein-histone association and chromatin remodeling. The domain itself adopts an all-α protein fold, a bundle of four alpha helices each separated by loop regions of variable lengths that form a hydrophobic pocket that recognizes the acetyl lysine.
Read more on Wikipedia →This topic has recently gained attention due to increased public interest. Search activity and Wikipedia pageviews suggest growing global engagement.
Search interest data over the past 12 months indicates that this topic periodically attracts global attention. Sudden spikes often correlate with major news events, public statements, or geopolitical developments.