Many proteins and protein segments cannot attain a single stable three-dimensional
structure under physiological conditions; instead, they adopt multiple interconverting …

Signaling pathways allow cells to detect and respond to a wide variety of chemical (eg Ca2+
or chemokine proteins) and physical stimuli (eg, sheer stress, light). Together, these …

The facts that many proteins with crucial biological functions do not have unique structures
and that many biological processes are compartmentalized into the liquid-like biomolecular …

Proteins with intrinsically disordered regions (IDRs) are common among eukaryotes. Many
IDRs interact with nucleic acids and proteins. Annotation of these interactions is supported …

Intrinsic disorder is instrumental for a wide range of protein functions, and its analysis, using
computational predictions from primary structures, complements secondary and tertiary …

Intrinsic disorder in proteins is relatively abundant in nature and essential for a broad
spectrum of cellular functions. While disorder can be accurately predicted from protein …

In previous work, we showed that intrinsically disordered regions (IDRs) of proteins contain
sequence-distributed molecular features that are conserved over evolution, despite little …

For years, proteasomal degradation was predominantly attributed to the ubiquitin-26S
proteasome pathway. However, it is now evident that the core 20S proteasome can …

Motivation Intrinsically disordered protein regions interact with proteins, nucleic acids and
lipids. Regions that bind lipids are implicated in a wide spectrum of cellular functions and …

One of the key features of intrinsically disordered regions (IDRs) is their ability to interact
with a broad range of partner molecules. Multiple types of interacting IDRs were identified …