Phosphorylated ubiquitin chain is the genuine Parkin receptor.
about
Ubiquitin modificationsMyosins, Actin and AutophagyMetabolic regulation of mitochondrial dynamicsUbiquitin phosphorylation in Parkinson's disease: Implications for pathogenesis and treatmentExpanding the ubiquitin code through post-translational modificationThe three 'P's of mitophagy: PARKIN, PINK1, and post-translational modificationsLRRK2 at the interface of autophagosomes, endosomes and lysosomesAutophagy in the liver: cell's cannibalism and beyondProbes of ubiquitin E3 ligases enable systematic dissection of parkin activationStructural insights into Parkin substrate lysine targeting from minimal Miro substratesSite-specific Interaction Mapping of Phosphorylated Ubiquitin to Uncover Parkin Activation.Structure-guided mutagenesis reveals a hierarchical mechanism of Parkin activation.The PINK1 p.I368N mutation affects protein stability and ubiquitin kinase activity(Patho-)physiological relevance of PINK1-dependent ubiquitin phosphorylationA Ubl/ubiquitin switch in the activation of ParkinThe ubiquitin signal and autophagy: an orchestrated dance leading to mitochondrial degradationMetabolism and the UPR(mt).Autophagy in acute kidney injuryThe ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy.PINK1, Parkin, and Mitochondrial Quality Control: What can we Learn about Parkinson's Disease Pathobiology?Heterozygous PINK1 p.G411S increases risk of Parkinson's disease via a dominant-negative mechanism.Mitochondrial dysfunction and Parkinson disease: a Parkin-AMPK alliance in neuroprotection.Genes associated with Parkinson's disease: regulation of autophagy and beyond.Targeting the Autophagy/Lysosomal Degradation Pathway in Parkinson's Disease.Pro- and Antioxidant Functions of the Peroxisome-Mitochondria Connection and Its Impact on Aging and DiseaseHydrophobic Patch of Ubiquitin is Important for its Optimal Activation by Ubiquitin Activating Enzyme E1.Phospho-ubiquitin: upending the PINK-Parkin-ubiquitin cascadeParkin and PINK1 functions in oxidative stress and neurodegeneration.Integration of cellular ubiquitin and membrane traffic systems: focus on deubiquitylases.Post translational modification of Parkin.Mitochondrial Quality Control and Disease: Insights into Ischemia-Reperfusion Injury.Twenty years since the discovery of the parkin gene.Mitochondrial quality control in amyotrophic lateral sclerosis: towards a common pathway?How phosphoubiquitin activates Parkin.Binding to serine 65-phosphorylated ubiquitin primes Parkin for optimal PINK1-dependent phosphorylation and activation.Mechanism of phospho-ubiquitin-induced PARKIN activation.Dual Function of Phosphoubiquitin in E3 Activation of Parkin.Hydrogen Sulphide modulating mitochondrial morphology to promote mitophagy in endothelial cells under high-glucose and high-palmitate.Phospho-ubiquitin-PARK2 complex as a marker for mitophagy defects.Superoxide drives progression of Parkin/PINK1-dependent mitophagy following translocation of Parkin to mitochondria.
P2860
Q26751380-7694054B-2F51-4113-8E1C-6D56E1FDB9A2Q26752776-B8BEDFDE-A680-4AB1-BFF7-CE4179F44A13Q26768130-A4F9CD8F-6302-445A-902D-1FF4A19FB02BQ26770342-14503897-35DF-4635-9844-A37AA89CF173Q26798369-EC328DEA-D170-45EF-910C-040AD4D8B44BQ26853492-1B566D5E-E1E2-4FFE-9CA1-26D303F41657Q28078248-008227FF-9080-478C-BEAF-6EFE22519263Q28388115-722C1DD3-14C9-45FE-BD3F-6B241077A95BQ28830194-5833B977-5B02-49DF-82EC-F1799E977220Q28831032-B36C396A-F85A-4893-B8A8-415EA87EC4B0Q30677261-D3149E23-B524-4D7E-BAC0-2EE52FAD1F9AQ30841625-062B2467-C003-4901-BEA3-C4156D077550Q30846938-0ABD7FA9-4535-490A-A9DB-6C2FA846D22AQ36078552-40770F9B-3B15-4226-BAD5-88C72D6623EDQ36172257-B47FE419-F442-45AB-8A9E-6D5C91AF4979Q36636158-AE560265-E670-44BB-A24C-BB57D38D29ECQ36654198-6638AA37-1B20-4400-B02E-F83433A52DF9Q36712027-35B5EBAB-66CE-4068-A1CB-5AEAAA45D76CQ37246125-66F22232-2651-4AC6-B2DD-E9520750776EQ37635610-FE2DA690-6AAD-46EF-AEE3-135BE89E5A45Q37736984-4D1DA316-A718-4624-B41D-E705E6C26271Q38539848-9F2D4E71-FEF3-4EFC-B8D4-772C4687F74EQ38557027-8DB7FA63-6ED8-4D80-B5BA-522A88C6FDF9Q38620227-DDF82990-F2B6-490A-9A7C-A6A1ED268942Q38641954-D07461B4-BCE7-4392-AC42-4F1D3E6DAAFDQ38689249-5F94EECF-6D3F-49FF-BFEC-515D12DE9A5AQ38721233-26ED4361-AE4B-455F-AAC7-031E4F5882CCQ39054548-9993ACBC-7F09-49E3-872D-33428C830685Q39074161-21CDF7FA-89C7-43E7-B042-B3A10978CDADQ39145536-D6ABF31E-2CE3-43FA-A57A-925D0C005130Q39236962-BAABB57D-4E52-41B0-B171-AECD77136A40Q39377582-A0898883-3103-4319-A556-0B0960662D34Q41429779-A3AE87F6-A9C9-4DD4-830B-FD8F02C5718CQ42058770-21978907-D0EF-4F58-811E-13D3D503AFBAQ42071947-F3FC8E28-72D6-4302-9EAC-BD8734FAEB3BQ42356433-C202AC47-AA65-49A9-ADCD-F9AB7665BED2Q42380097-1A34D6FB-B6D5-4332-8AEB-D778DAFDF4D0Q42426457-98E08F8E-59CB-40A0-8EAF-517323DE1695Q43273832-A82D9613-F5CF-4C79-84A6-79A42B532FA2Q46288367-457EC284-3E78-4C35-A016-53AF1E258DDB
P2860
Phosphorylated ubiquitin chain is the genuine Parkin receptor.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Phosphorylated ubiquitin chain is the genuine Parkin receptor.
@en
Phosphorylated ubiquitin chain is the genuine Parkin receptor.
@nl
type
label
Phosphorylated ubiquitin chain is the genuine Parkin receptor.
@en
Phosphorylated ubiquitin chain is the genuine Parkin receptor.
@nl
prefLabel
Phosphorylated ubiquitin chain is the genuine Parkin receptor.
@en
Phosphorylated ubiquitin chain is the genuine Parkin receptor.
@nl
P2093
P2860
P356
P1476
Phosphorylated ubiquitin chain is the genuine Parkin receptor
@en
P2093
Fumika Koyano
Hidetaka Kosako
Kei Okatsu
Keiji Tanaka
Mayumi Kimura
Yasushi Saeki
P2860
P304
P356
10.1083/JCB.201410050
P407
P577
2015-04-06T00:00:00Z