Intrinsically disordered protein regions exist in a collection of dynamic interconverting
conformations that lack a stable 3D structure. These regions are structurally heterogeneous …

Cells use membraneless compartments to organize their interiors, and recent research has
begun to uncover the molecular principles underlying their assembly. Here, we explore how …

Intrinsically disordered regions (IDRs) are critical for a wide variety of cellular functions,
many of which involve interactions with partner proteins. Molecular recognition is typically …

Intrinsically disordered protein regions (IDRs) are well established as contributors to
intermolecular interactions and the formation of biomolecular condensates. In particular …

Intrinsically disordered regions (IDRs) are critical for cellular function, yet often appear to
lack sequence conservation when assessed by multiple sequence alignments. This raises …

Intrinsically disordered protein regions (IDRs) are ubiquitous across all kingdoms of life and
play a variety of essential cellular roles. IDRs exist in a collection of structurally distinct …

Biomolecular condensation underlies the biogenesis of an expanding array of
membraneless assemblies, including stress granules (SGs), which form under a variety of …

The living cell creates a unique internal molecular environment that is challenging to
characterize. By combining single-molecule displacement/diffusivity map** (SM d M) with …

Nuclear bodies are diverse membraneless suborganelles with emerging links to
development and disease. Explaining their structure, function, regulation, and implications in …

Highlights•Single point mutations in intrinsically disordered protein regions (IDRs) are poorly
studied.•Multiple studies show that single-point mutations can change IDR structural …