Regulation, recognition and cell signaling involve the coordinated actions of many players.
To achieve this coordination, each participant must have a valid identification (ID) that is …

The last general review of the aspartic peptidase family was by David R. Davies in 1990. 1
Since then, several reviews on selected aspects of the structure and function of aspartic …

Intrinsically unstructured proteins (IUPs) are devoid of extensive structural order but often
display signs of local and limited residual structure. To explain their effective functioning, we …

Intrinsically disordered proteins (IDPs) or intrinsically disordered regions do not have a fixed
tertiary structure but play key roles in signal regulation, molecule recognition, and drug …

Calpains are non-lysosomal calcium-dependent cysteine proteinases that selectively cleave
proteins in response to calcium signals and thereby control cellular functions such as …

Among proteases or proteinases, the endopeptidases account for a significant proportion (∼
2%) of the human genome with over 550 defined members and a further 100 or so predicted …

Serine proteases and their natural protein inhibitors are among the most intensively studied
protein complexes. About 20 structurally diverse inhibitor families have been identified …

Traditionally, molecular disorder has been viewed as local or global instability. Molecules or
regions displaying disorder have been considered inherently unstructured. The term has …

Cleavage of amyloid precursor protein (APP) by the Alzheimer's β-secretase (BACE1) is a
key step in generating amyloid β-peptide, the main component of amyloid plaques. Here we …

The interaction of proteinase inhibitors produced, in most cases, by host organisms and the
invasive proteinases of pathogens or parasites or the dietary proteinases of predators …