Intrinsically disordered proteins (IDPs) are characterized by substantial conformational
plasticity. Given their inherent structural flexibility X-ray crystallography is not applicable to …

The current pandemic situation caused by the Betacoronavirus SARS-CoV-2 (SCoV2)
highlights the need for coordinated research to combat COVID-19. A particularly important …

Thanks to recent improvements in NMR instrumentation, pulse sequence design, and
sample preparation, a panoply of new NMR tools has become available for atomic …

The mechanisms by which intrinsically disordered proteins engage in rapid and highly
selective binding is a subject of considerable interest and represents a central paradigm to …

Liquid-liquid phase separation (LLPS) of intrinsically disordered proteins (IDPs) is involved
in both intracellular membraneless organelles and extracellular tissues. Despite growing …

Nuclear magnetic resonance (NMR) spectroscopy is a powerful high-resolution tool for
characterizing biomacromolecular structure, dynamics, and interactions. However, the …

Activated SUMOylation is a hallmark of cancer. Starting from a targeted screening for SUMO-
regulated immune evasion mechanisms, we identified an evolutionarily conserved function …

The linear ubiquitin chain assembly complex (LUBAC) regulates immune signaling, and its
function is regulated by the deubiquitinases OTULIN and CYLD, which associate with the …

Aromatic residues cluster in the core of folded proteins, where they stabilize the structure
through multiple interactions. Nuclear magnetic resonance (NMR) studies in the 1970s …

The nucleocapsid protein of severe acute respiratory syndrome coronavirus 2 encapsidates
the viral genome and is essential for viral function. The central disordered domain comprises …