Biologically active but floppy proteins represent a new reality of modern protein science.
These intrinsically disordered proteins (IDPs) and hybrid proteins containing ordered and …

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 discovery that endoplasmic reticulum (ER) luminal chaperones such as GRP78/BiP can
escape to the cell surface upon ER stress where they regulate cell signaling, proliferation …

Intrinsically disordered proteins (IDPs) are abundant in eukaryotic proteomes, play a major
role in cell signaling, and are associated with human diseases. To understand IDP function it …

Intrinsically disordered regions (IDRs) make up ca. 30% of the proteome of most eukaryotes,
and are involved in a diverse set of functions. Conventional sequence alignment tools …

In addition to the “traditional” proteins characterized by the unique crystal-like structures
needed for unique functions, it is increasingly recognized that many proteins or protein …

Molecular recognition features (MoRFs) are short protein-binding regions that undergo
disorder-to-order transitions (induced folding) upon binding protein partners. These regions …

Current efforts in design and characterization of drugs often rely on the structure of their
protein targets. However, a large fraction of proteins lack unique 3-D structures and exist as …

Idiopathic pulmonary fibrosis (IPF) is characterized by lung remodeling arising from
epithelial injury, aberrant fibroblast growth, and excessive deposition of extracellular matrix …

Therapeutic activity of a significant majority of drugs is determined by their interactions with
proteins. Databases of drug-protein interactions (DPIs) primarily focus on the therapeutic …