about
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65Efficient genetic encoding of phosphoserine and its nonhydrolyzable analogPhosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity.Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation.The pyridoxal 5'-phosphate (PLP)-dependent enzyme serine palmitoyltransferase (SPT): effects of the small subunits and insights from bacterial mimics of human hLCB2a HSAN1 mutations
P50
description
investigador
@es
researcher
@en
wetenschapper
@nl
name
Agne Kazlauskaite
@en
Agne Kazlauskaite
@nl
type
label
Agne Kazlauskaite
@en
Agne Kazlauskaite
@nl
prefLabel
Agne Kazlauskaite
@en
Agne Kazlauskaite
@nl
P31
P496
0000-0001-9145-8479