about
Ubiquitylation of autophagy receptor Optineurin by HACE1 activates selective autophagy for tumor suppressionAutophagy-Related Deubiquitinating Enzymes Involved in Health and DiseaseEmerging strategies to effectively target autophagy in cancerVaricella-Zoster Virus Infectious Cycle: ER Stress, Autophagic Flux, and Amphisome-Mediated TraffickingEvidence for a common biological pathway linking three Parkinson's disease-causing genes: parkin, PINK1 and DJ-1E3 Ubiquitin Ligases Neurobiological Mechanisms: Development to DegenerationApolipoprotein B100 quality control and the regulation of hepatic very low density lipoprotein secretion.Versatile roles of k63-linked ubiquitin chains in trafficking.UPR, autophagy, and mitochondria crosstalk underlies the ER stress responseThe functional and pathologic relevance of autophagy proteases.Posttranslational modification of autophagy-related proteins in macroautophagyMuRF2 regulates PPARγ1 activity to protect against diabetic cardiomyopathy and enhance weight gain induced by a high fat diet.ULK1 cycling: The ups and downs of the autophagy response.RNF166 Determines Recruitment of Adaptor Proteins during Antibacterial Autophagy.E3 Ubiquitin Ligase Nedd4 Promotes Japanese Encephalitis Virus Replication by Suppressing Autophagy in Human Neuroblastoma CellsRegulation of autophagy by protein post-translational modification.How to control self-digestion: transcriptional, post-transcriptional, and post-translational regulation of autophagy.Ubiquitin-dependent proteolysis in yeast cells expressing neurotoxic proteins.Recent advances in quantitative and chemical proteomics for autophagy studies.Insights into links between autophagy and the ubiquitin system from the structure of LC3B bound to the LIR motif from the E3 ligase NEDD4.Characterization of the mammalian family of DCN-type NEDD8 E3 ligases.Cardiac ubiquitin ligases: Their role in cardiac metabolism, autophagy, cardioprotection and therapeutic potential.Ischaemia-induced autophagy leads to degradation of gap junction protein connexin43 in cardiomyocytes.Ubiquitin ligase ITCH recruitment suppresses the aggregation and cellular toxicity of cytoplasmic misfolded proteins.Fine-tuning of ULK1 mRNA and protein levels is required for autophagy oscillation.Ubiquitin Ligases and Posttranslational Regulation of Energy in the Heart: The Hand that Feeds.Regulation of autophagic flux by CHIP.The E3 ubiquitin ligase seven in absentia homolog 1 may be a potential new therapeutic target for Parkinson's disease.Gp78 E3 Ubiquitin Ligase: Essential Functions and Contributions in Proteostasis.Autophagy plays a WASHing game.Autophagy regulation: RNF2 targets AMBRA1.Regulation of the Tumor-Suppressor BECLIN 1 by Distinct Ubiquitination Cascades.Glucose starvation induces LKB1-AMPK-mediated MMP-9 expression in cancer cells.Contribution of Mitophagy to Cell-Mediated Mineralization: Revisiting a 50-Year-Old ConundrumDeubiquitinating Enzymes Related to Autophagy: New Therapeutic Opportunities?
P2860
Q24300797-59894913-1BE0-479D-B425-9E40C82CA829Q26786631-649DE61E-24B7-4635-95DB-D263D1C221CDQ27009194-68B42814-81FC-4881-9B92-47A42999FAACQ28076761-413DEE95-ED0D-45F4-AADE-2831E2D5E9FFQ28258696-760B72D5-2F2E-4438-AED1-C1FE2947DDABQ33705444-B35E326E-01E0-43C9-BA4D-A26BB8F5319DQ33858526-38AE4F38-F2B6-43D9-98AE-879C666B22E7Q34774715-C1EF6874-B203-4EE5-8C45-01F534362E9CQ35122358-7A12DB12-E83A-46E8-995A-4265F0697996Q35242420-ABD6D440-52C3-45D3-AD47-76C883D6A5A0Q35852919-8399C401-BF38-4823-8967-737CA26881FBQ35920226-CB5B9075-04F0-4395-B508-A002FBBA7F25Q37513998-06FE137F-A9DF-4F95-BB94-9234300F9BBFQ37539697-2D12751A-F4F8-4C4F-A31E-D7B55949723AQ37724320-81B41956-4EDA-4155-93F4-3E0464157DCBQ38264531-9ABA2218-CAD5-4987-B114-F2CDB01B9DFFQ38373179-559AD16A-FA51-4694-AF68-4DAC17F48D3CQ38393072-348DA4D8-4BC3-4EED-9176-763C7DA6B9D3Q38640396-40D478C1-DCCE-4A42-95D7-65C09496D7C5Q38704902-1494ACE3-688D-44DC-A5E1-25C5FA15AA8BQ38791699-2D247ED3-79CD-4C16-983E-E9E2C060DD7BQ38898242-388FCDB2-E57E-4A97-9A45-1DAE673AAE2FQ38918153-601DE60B-3ACD-4AB6-AB30-9E3254228E14Q38991141-3D461A76-21C4-44A1-821E-B3B9462780D9Q39312592-5F0C1968-DFCE-4884-BE0A-F53DB6D71AC1Q39390991-A0DD8CA9-70AF-4D93-B96C-723FFF3EA818Q40685914-CCD29BCE-B696-4F5B-8D4F-E81B64E2EA3EQ41521020-AB2574C4-AE5F-4DD1-98CC-6F6CF088D68EQ41551065-A3CD7122-EC92-4C34-AC10-A06DEEC9B7B8Q42696555-C09A5D27-4593-468F-8C38-46D2C3CA044FQ42858025-44E4838C-DB78-4441-AD27-E454D7A31BC6Q47171904-8F4F9581-B9F4-46F7-B6DA-699036AC284FQ55712083-6D072F0F-B536-468E-8F3C-B2A2BA25B30EQ57824734-0EC3296D-1EC3-41EC-ACBC-1AFA98BF1C91Q58766259-DB4D3B1C-F2A3-4117-ACA2-BA8672A6878E
P2860
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Emerging roles of E3 ubiquitin ligases in autophagy.
@en
type
label
Emerging roles of E3 ubiquitin ligases in autophagy.
@en
prefLabel
Emerging roles of E3 ubiquitin ligases in autophagy.
@en
P2860
P1476
Emerging roles of E3 ubiquitin ligases in autophagy.
@en
P2093
Ersheng Kuang
Jianfei Qi
P2860
P304
P356
10.1016/J.TIBS.2013.06.008
P50
P577
2013-07-16T00:00:00Z