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 …

Many intrinsically disordered proteins (IDPs) are involved in complex signalling networks
inside the cell. Their particular binding modes elicit different types of responses that can be …

The intrinsically disordered transactivation domains of HIF-1α and CITED2 compete for
binding of the TAZ1 domain of the CREB-binding protein by a unidirectional allosteric …

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 …

Proteins form the molecular scaffolding of life and are essential to catalyzing the chemical
reactions that sustain living systems. These characteristics have led us to think that proteins …

Intrinsically disordered proteins (IDPs) are common in eukaryotes. However, relatively few
experimental studies have addressed the nature of the rate-limiting transition state for the …

The cellular response to hypoxia is critical for cell survival and is fine-tuned to allow cells to
recover from hypoxic stress and adapt to heterogeneous or fluctuating oxygen levels,. The …

Many intrinsically disordered proteins (IDPs) attain a well-defined structure in a coupled
folding and binding reaction with another protein. Such reactions may involve early to late …

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

Proteins that contain long disordered regions are prevalent in the proteome and frequently
associated with diseases. However, the mechanisms by which such intrinsically disordered …