IndraLab

Statements


| 7 2

sparser
"Todi et al. [94] identified Lys-117 as the primary site of ubiquitination in wild-type and pathogenic ataxin-3 and showed that ubiquitin-dependent activation of ataxin-3 at Lys-117 is important for re[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Further studies indicate that ubiquitin-dependent activation of ataxin-3 at Lys-117 is important for its ability to reduce high molecular weight ubiquitinated species in cells."

reach
"To exclude the possibility that conjugated ubiquitin (Ub) may interact with Atx3 and cause coaggregation of the PQE protein with Atx3 [55], we applied a mutant of Htt -N90 (3KR, three Lys residues replaced by Arg) for the experiment as described previously [51]."

reach
"Todi et al. [94] identified Lys-117 as the primary site of ubiquitination in wild-type and pathogenic ataxin-3 and showed that ubiquitin-dependent activation of ataxin-3 at Lys-117 is important for re[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"For SCA 3, it is known that both normal and polyQ expanded ataxin-3 localize to mitochondria [XREF_BIBR] and that degradation of polyQ expanded ataxin-3 via the UPS is promoted by an ubiquitin ligase in the outer mitochondrial membrane called MITOL [XREF_BIBR]."

reach
"Further studies indicate that ubiquitin dependent activation of ataxin-3 at Lys 117 is important for its ability to reduce high molecular weight ubiquitinated species in cells."

reach
"Cytoplasmic Ubiquitin Specific Protease 19 (USP19) Modulates Aggregation of Polyglutamine Expanded Ataxin-3 and Huntingtin through the HSP90 Chaperone."

reach
"AT3 is composed of a structured globular N-terminal domain, the Josephin domain (JD), which displays ubiquitin hydrolase activity, followed by a disordered C-terminal tail containing two ubiquitin interacting motifs (UIMs) and the polyQ stretch of variable length, whose expansion beyond a certain threshold triggers SCA3 [XREF_BIBR, XREF_BIBR]."

reach
"The pattern of ubiquitin linkages on both forms of ataxin-3 are also reportedly similar, suggesting that toxicity and aggregation of polyQ-expanded ataxin-3 is unlikely to be caused by differences in ubiquitin linkage types [77]."