Intrinsically disordered proteins (IDPs) present a functional paradox because they lack
stable tertiary structure, but nonetheless play a central role in signaling, utilizing a process …

Transcription factors and other allosteric cell signaling proteins contain a disproportionate
number of domains or segments that are intrinsically disordered (ID) under native …

Allostery is a biological phenomenon of critical importance in metabolic regulation and cell
signalling. The fundamental premise of classical models that describe allostery is that …

Increased understanding of intrinsically disordered proteins (IDPs) and protein regions has
revolutionized our view of the relationship between protein structure and function. Data now …

Intrinsically disordered proteins must compete for binding to common regulatory targets to
carry out their biological functions. Previously, we showed that the activation domains of two …

Intrinsically disordered proteins (IDPs) lack stable structures under physiological conditions
but often fold into stable structures upon specific binding. These coupled binding and folding …

Intrinsically disordered (ID) regions are disproportionately higher in cell signaling proteins
and are predicted to have much larger frequency of phosphorylation sites than ordered …

Intrinsically disordered proteins (IDPs) are enriched in signaling and regulatory functions
because disordered segments permit interaction with several proteins and hence the re-use …

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

In recent years, it has become quite evident that numerous proteins exist as an ensemble of
conformers that collectively appears to be intrinsically disordered (ID). Of particular …