Ontology highlight
ABSTRACT:
SUBMITTER: Rosenberg GM
PROVIDER: S-EPMC9108986 | biostudies-literature | 2022 May
REPOSITORIES: biostudies-literature
Rosenberg Gregory M GM Murray Kevin A KA Salwinski Lukasz L Hughes Michael P MP Abskharon Romany R Eisenberg David S DS
The Journal of biological chemistry 20220409 5
Low-complexity domains (LCDs) of proteins have been shown to self-associate, and pathogenic mutations within these domains often drive the proteins into amyloid aggregation associated with disease. These domains may be especially susceptible to amyloidogenic mutations because they are commonly intrinsically disordered and function in self-association. The question therefore arises whether a search for pathogenic mutations in LCDs of the human proteome can lead to identification of other proteins ...[more]