YWHAQ

(redirected from protein tau)

YWHAQ

A gene on chromosome 2p25.1 that encodes an adapter protein which regulates a broad spectrum of general and specialised signalling pathways by binding to a large number of partners, usually by recognising a phosphoserine or phosphothreonine motif. YWHAQ downregulates PDPK1’s kinase activity.
References in periodicals archive ?
Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain.
MK-6240 is designed to detect brain protein tau levels by positron emission tomography scan.
Their goal is to identify the compounds that could lower levels of the protein tau in the brain, which is considered one of the most promising approaches in Alzheimer's research and could potentially lead to new drugs to treat the disease.
Glial fibrillary acid protein (GFAP), ubiquitin c-terminal hydrolase LI (UCH-L1), as well as other proteins, including microtubule-associated protein tau, amyloid beta peptide (A[beta]342), and neurofilament light (NfL), have been proposed as promising diagnostic and prognostic biomarkers in TBI.
The contract has been signed for the development, manufacture and commercialisation of an investigational preclinical antibody candidate targeting the protein tau.
It was hoped the drug--known as LMTM--would reduce the accumulation of the protein tau.
2,7,8) Created by an inversion with several superimposed deletions, dysfunction is caused by hyperphosphorylation and aggregation of the microtubule-association protein tau (MAPT) in white matter and depends upon anatomic area, cell type and specific isoform of tau deposits.
CTE is characterized by the accumulation of the protein tau in regions of the brain that control mood, cognition and motor function.
Calpain activation promoted the cleavage of the microtubule-associated protein tau, leading to its accumulation [91].
Similar behavior has been spotted for the Alzheimer's-related protein tau.
Peripheral plasma levels of the CNS protein tau are chronically elevated after traumatic brain injury and appear to correlate with the severity of postconcussive symptoms, according to a report published in JAMA Neurology.
This project s goal is therefore to understand the role of LRRK2 phosphorylation in PD by pursuing 3 specific aims: 1) elucidate the regulation of LRRK2 phosphorylation by phosphatases, 2) determine LRRK2 phosphorylation downstream phenotypes in cellular models through transcriptome profiling, protein translation profiling and protein tau related phenotypes, and 3) verify these findings from experimental models in PD biosamples.