RNA-binding proteins (RBPs) are typically thought of as proteins that bind RNA through one
or multiple globular RNA-binding domains (RBDs) and change the fate or function of the …

Over the past decade, we have observed a massive increase in the amount of information
describing protein sequences from a variety of organisms. 1, 2 While this may reflect the …

Transcription factors (TFs) that bind common DNA motifs in vitro occupy distinct sets of
promoters in vivo, raising the question of how binding specificity is achieved. TFs are …

Mammalian cells harbor more than a thousand RNA-binding proteins (RBPs), with half of
these employing unknown modes of RNA binding. We developed RBDmap to determine the …

The suggestion that the native state of many proteins is intrinsically disordered (or, as
originally termed, unstructured) is now integral to our general view of protein structure and …

RNA-binding proteins (RBPs) determine RNA fate from synthesis to decay. Employing two
complementary protocols for covalent UV crosslinking of RBPs to RNA, we describe a …

The ideas that proteins might possess specific functions without being uniquely folded into
rigid 3D-structures and that these floppy polypeptides might constitute a noticeable part of …

Gene-specific transcription factors (TFs) are key regulatory components of signaling
pathways, controlling, for example, cell growth, development, and stress responses. Their …

Intrinsically disordered regions, terminal tails, and flexible linkers are abundant in DNA-
binding proteins and play a crucial role by increasing the affinity and specificity of DNA …

Traditionally, specific DNA recognition is thought to rely on static contacts with the bases or
phosphates. Recent results, however, indicate that residues far outside the binding context …