PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
about
Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tetheringPhosphorylation by PINK1 releases the UBL domain and initializes the conformational opening of the E3 ubiquitin ligase ParkinSerotonin 1A Receptors on Astrocytes as a Potential Target for the Treatment of Parkinson's DiseaseStructural insights into Parkin substrate lysine targeting from minimal Miro substratesLoss of Parkinson's disease-associated protein CHCHD2 affects mitochondrial crista structure and destabilizes cytochrome cQuantitative proteomics reveal a feedforward mechanism for mitochondrial PARKIN translocation and ubiquitin chain synthesis.Mask loss-of-function rescues mitochondrial impairment and muscle degeneration of Drosophila pink1 and parkin mutantsPINK1 and Parkin control localized translation of respiratory chain component mRNAs on mitochondria outer membrane.The Parkinson's Disease-Associated Protein Kinase LRRK2 Modulates Notch Signaling through the Endosomal Pathway.(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylationUsing protein motion to read, write, and erase ubiquitin signals.The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's diseaseDrosophila clueless is involved in Parkin-dependent mitophagy by promoting VCP-mediated Marf degradation.PINK1-dependent phosphorylation of PINK1 and Parkin is essential for mitochondrial quality control.Analysis of mitochondrial structure and function in the Drosophila larval musculature.Age-related accumulation of phosphorylated mitofusin 2 protein in retinal ganglion cells correlates with glaucoma progression.Altered mitochondrial dynamics as a consequence of Venezuelan Equine encephalitis virus infection.Evidence that a mitochondrial death spiral underlies antagonistic pleiotropy.Post translational modification of Parkin.Reduced TDP-43 Expression Improves Neuronal Activities in a Drosophila Model of Perry Syndrome.Mitochondrial quality control in amyotrophic lateral sclerosis: towards a common pathway?Lysine 63-linked polyubiquitination is dispensable for Parkin-mediated mitophagy.Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis.Vps35 in cooperation with LRRK2 regulates synaptic vesicle endocytosis through the endosomal pathway in Drosophila.Monitoring Mitochondrial Changes by Alteration of the PINK1-Parkin Signaling in Drosophila.F1 -ATP synthase α-subunit: a potential target for RNAi-mediated pest management of Locusta migratoria manilensis.Evidence that phosphorylated ubiquitin signaling is involved in the etiology of Parkinson's disease.Neuronal Proteomic Analysis of the Ubiquitinated Substrates of the Disease-Linked E3 Ligases Parkin and Ube3a.
P2860
Q27311602-70559962-C073-4F28-B673-42227A3B8440Q27320529-83AD7003-61BA-4580-A731-D81B3CD61098Q28079379-DB13AF36-E0B4-4A55-94C3-D055EEE37047Q28831032-578FEF7F-ECAD-4758-8AE6-0814BF67D4E0Q30855422-106EA798-3455-4820-9AE8-814E0DB5D983Q34622632-518C32BE-B82E-432E-8381-1F45F9980D1DQ35585304-43CAC5DE-0355-450B-9A90-283F286A0CD1Q35684286-00E67E54-96AA-4F0F-B847-8798D5840849Q35768943-576AB87F-E66C-4E70-8FD5-248CC50712F8Q36078552-4598F58B-ED1F-42F5-AFD4-5E83383B75B0Q36283663-6266E883-3AC6-45E5-8885-1CF41DA4F58FQ36611426-06A6402F-04DE-4270-B66E-7495B94FCA7FQ37336130-40F8D73C-9E3A-4BFC-8360-AB93EF3DE650Q37603514-197973EF-F4CE-48F0-85AB-9A26216C5594Q38413591-2FB706F9-C11C-4CDE-88FC-ED6FA75A865CQ38661781-441AA9E5-2FD5-44AF-AE38-1B0DF52640A2Q39027481-E170CC90-A741-4D90-B273-D35BF9CBB2C6Q39129509-11574915-71D8-460B-9F50-20DF7C794563Q39145536-A2F7FFEF-FC1B-4328-BE5E-3E8F850278D9Q41040861-CD299C2E-9900-4932-BE81-9DBA323FCA0FQ41429779-885A51B2-805F-44F2-9645-9BE43FFDAE64Q42275369-17190B73-F32F-486D-B97D-0D51FCB5956DQ43215694-30D803FA-773B-4C57-A630-00941788E720Q47733442-7D5D9396-54F3-4C42-A8ED-0345D23F36D2Q48253269-5A2B11BD-2EFE-4064-AFC6-3290E860DCB6Q51649454-CA46E8C4-1825-495F-92B4-907816DFD4FFQ52093815-726DCF88-D364-47E9-A64E-80A7889506A8Q52564493-0B6C9F04-0FEE-44BF-82A1-E3BEFC54D091
P2860
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
@ast
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
@en
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
@nl
type
label
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
@ast
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
@en
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
@nl
prefLabel
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
@ast
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
@en
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
@nl
P2093
P2860
P3181
P1433
P1476
PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
@en
P2093
Kahori Shiba-Fukushima
Tsuyoshi Inoshita
Yuzuru Imai
P2860
P304
P3181
P356
10.1371/JOURNAL.PGEN.1004391
P407
P577
2014-06-01T00:00:00Z