Over the past decade, we have observed a massive increase in the amount of information
describing protein sequences from a variety of organisms. 1, 2 While this may reflect the …

This review describes the family of intrinsically disordered proteins, members of which fail to
form rigid 3-D structures under physiological conditions, either along their entire lengths or …

Motivation: Many biological processes are guided by receptor interactions with linear
ligands of variable length. One such receptor is the MHC class I molecule. The length …

Studies on the DNA-binding properties of transcription factors are important in searching for
the downstream genes regulated by these factors. In the present study, we report on the …

The suggestion that the native state of many proteins is intrinsically disordered (or, as
originally termed, unstructured) is now integral to our general view of protein structure and …

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

Traditionally, protein–protein interactions were thought to be mediated by large, structured
domains. However, it has become clear that the interactome comprises a wide range of …

The Phospho. ELM resource (http://phospho. elm. eu. org) is a relational database designed
to store in vivo and in vitro phosphorylation data extracted from the scientific literature and …

Transient interactions, which involve protein interactions that are formed and broken easily,
are important in many aspects of cellular function. Here we describe structural and functional …

Highly sophisticated mechanisms that modulate protein structure and function, which involve
synthesis and degradation, have evolved to maintain cellular homeostasis. Perturbations in …