Ontology highlight
ABSTRACT:
SUBMITTER: Caraveo G
PROVIDER: S-EPMC5748183 | biostudies-literature | 2017 Dec
REPOSITORIES: biostudies-literature
Caraveo Gabriela G Soste Martin M Cappelleti Valentina V Fanning Saranna S van Rossum Damian B DB Whitesell Luke L Huang Yanmei Y Chung Chee Yeun CY Baru Valeriya V Zaichick Sofia S Picotti Paola P Lindquist Susan S
Proceedings of the National Academy of Sciences of the United States of America 20171211 52
Calcineurin is an essential Ca<sup>2+</sup>-dependent phosphatase. Increased calcineurin activity is associated with α-synuclein (α-syn) toxicity, a protein implicated in Parkinson's Disease (PD) and other neurodegenerative diseases. Calcineurin can be inhibited with Tacrolimus through the recruitment and inhibition of the 12-kDa <i>cis-trans</i> proline isomerase FK506-binding protein (FKBP12). Whether calcineurin/FKBP12 represents a native physiologically relevant assembly that occurs in the a ...[more]