A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
about
Guidelines for the use and interpretation of assays for monitoring autophagyNix is a selective autophagy receptor for mitochondrial clearanceGuidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)A comprehensive glossary of autophagy-related molecules and processes (2nd edition)Structural determinants in GABARAP required for the selective binding and recruitment of ALFY to LC3B-positive structuresThe E3-ubiquitin ligase TRIM50 interacts with HDAC6 and p62, and promotes the sequestration and clearance of ubiquitinated proteins into the aggresomeOATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturationBinding of the Atg1/ULK1 kinase to the ubiquitin-like protein Atg8 regulates autophagyFYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transportNBR1 is a new PB1 signalling adapter in Th2 differentiation and allergic airway inflammation in vivop62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for bothTRIM proteins regulate autophagy and can target autophagic substrates by direct recognitionPhosphorylation of the autophagy receptor optineurin restricts Salmonella growthRab GTPase-activating proteins in autophagy: regulation of endocytic and autophagy pathways by direct binding to human ATG8 modifiersThe selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein AlfyRAB3GAP1 and RAB3GAP2 modulate basal and rapamycin-induced autophagyInteractions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnoverp62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcriptionDOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family encoding dual regulators of autophagy and transcriptionTMEM59 defines a novel ATG16L1-binding motif that promotes local activation of LC3Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagyNetwork organization of the human autophagy systemSpred2 interaction with the late endosomal protein NBR1 down-regulates fibroblast growth factor receptor signalingPeroxisomal Atg37 binds Atg30 or palmitoyl-CoA to regulate phagophore formation during pexophagyAutophagy promotes primary ciliogenesis by removing OFD1 from centriolar satellitesSVIP induces localization of p97/VCP to the plasma and lysosomal membranes and regulates autophagyRegulation of endoplasmic reticulum turnover by selective autophagyExtracellular M. tuberculosis DNA targets bacteria for autophagy by activating the host DNA-sensing pathwayAutophagy, mitochondria and oxidative stress: cross-talk and redox signallingThe Cvt pathway as a model for selective autophagyp62 and NDP52 proteins target intracytosolic Shigella and Listeria to different autophagy pathwaysDistinct mechanisms of ferritin delivery to lysosomes in iron-depleted and iron-replete cellsAutophagic degradation of peroxisomes in mammalsAutophagy signal transduction by ATG proteins: from hierarchies to networksDirect and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein ToxicityAutophagy and the regulation of the immune responseThe atypical PKCs in inflammation: NF-κB and beyondMechanisms for quality control of misfolded transmembrane proteinsParticle-rich cytoplasmic structure (PaCS): identification, natural history, role in cell biology and pathologyPAMPs and DAMPs: signal 0s that spur autophagy and immunity
P2860
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
P248
Q21996341-EFCEF633-8EF6-4CDE-BDF5-EEB1229A97DFQ22001532-21B623FF-EE1B-4F63-82F4-EE8E973F9D1BQ22676705-801CD0B2-2572-49F4-80BF-44D0D1F65650Q23757242-F17EA2E8-AABD-43B8-812D-1F9D03098C08Q24292981-B4C87765-2485-40E9-8FB2-3A37A6054AE4Q24293114-1E6A8874-5CFF-46FE-9EE7-097DE85FD334Q24295224-D52E829B-911E-41A6-9D43-442D617ABA42Q24295813-17B2DC89-94E3-4B0F-8D65-5EC3FAC510CCQ24297378-27432481-9D89-4098-B285-6AA6137D6534Q24298214-580FF6D5-3242-43DB-A478-F237F457D526Q24301629-2F11FFA7-0219-4A4D-8C1A-6131D2B1B379Q24302068-536B7499-91E6-4CE4-A4FC-49180815DA2FQ24304447-E2EF558E-63E1-4125-AA49-DE6B4E021EC5Q24305592-2C39DCCC-81A8-4BD9-9DA7-E8909D97F5D4Q24307759-4CB9B19A-393D-4E9A-828C-CCF3E9B2DF93Q24309113-766B85D5-E160-46C8-978E-602F3BAD8F95Q24309203-E95CAB96-28BF-4BDC-B1AD-00A9CF470BDDQ24310885-02152DFF-3952-4D2B-BE81-503614520960Q24311383-D9CB8F13-4BCC-45DC-80F9-D261CCF85A72Q24313405-560B45C7-34A6-4FD9-A08D-1A77C2A96D5EQ24314391-F8492788-9BCF-42DA-B251-E2C5409A041EQ24324004-24D43249-F8EF-498F-AD25-9A4FE82647C0Q24324825-120863CD-06DF-46C9-A118-F68B0460AC51Q24337501-41EF5D13-E16B-49CF-A420-0AC5D2001B92Q24337670-8968DD69-0EB4-4FBA-B6DB-E30FAA673F55Q24337684-848341FC-C3DB-43B2-88D4-550F0DE5EC6CQ24337913-509825F3-C711-4A6C-ADD9-60FC762A403AQ24601311-B3283D3C-59B6-4DCC-BAE1-505BE95C84CCQ24608960-AF062C43-644C-407E-808F-4E4BDC767D04Q24617191-2D4D2877-20F9-41C7-A1B5-95192AE498A0Q24629208-E9402B84-C963-4ED0-9D63-6DEBA5122D40Q24634199-A7E4AC3D-0091-4D2A-8636-144F556B6D45Q26749227-E72C5DC8-F5D8-4DC4-BC1E-9140A0BFA7B1Q26782670-2D60B01D-4DF7-4B49-93AD-BE57817F6D2CQ26799306-9091C70F-03CC-4A45-99C5-7798346AE7F9Q26822919-67B1F290-126B-4209-BDA5-9BA421B50237Q26829823-EFC88226-987D-4935-9202-847A39FBE92BQ26830475-B4976544-E8F5-414E-B64C-CD71623CFC5FQ26998855-9C4DF0CC-0691-4F22-91E8-38B987648787Q27004190-E796EF88-4A9B-4D7B-ABE0-714F23500A10
P2860
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
description
2009 nî lūn-bûn
@nan
2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@ast
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@en
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@en-gb
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@nl
type
label
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@ast
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@en
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@en-gb
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@nl
prefLabel
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@ast
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@en
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@en-gb
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@nl
P2093
P50
P921
P3181
P1433
P1476
A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
@en
P2093
Aud Øvervatn
Ivana Bilusic
Jennifer L Nunn
Philipp Wild
Terje H Clausen
Tetsuro Ishii
Trond Lamark
Vladimir Kirkin
Yu-Shin Sou
P304
P3181
P356
10.1016/J.MOLCEL.2009.01.020
P407
P50
P577
2009-02-27T00:00:00Z