Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation

Mechanisms Underlying Ubiquitination

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Impaired Proteasome Function in Alzheimer's Disease

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Aβ Immunotherapy Leads to Clearance of Early, but Not Late, Hyperphosphorylated Tau Aggregates via the Proteasome

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CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

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Sequestosome 1/p62 Is a Polyubiquitin Chain Binding Protein Involved in Ubiquitin Proteasome Degradation

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Global Impairment of the Ubiquitin-Proteasome System by Nuclear or Cytoplasmic Protein Aggregates Precedes Inclusion Body Formation

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Tau filament formation in transgenic mice expressing P301L tau

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CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival

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Proteasome subunit Rpn1 binds ubiquitin-like protein domains

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Aggresomes Formed by α-Synuclein and Synphilin-1 Are Cytoprotective

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Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies

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Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments

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Proteasomal degradation of tau protein

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The Atypical PKC-Interacting Protein p62 Is an Important Mediator of RANK-Activated Osteoclastogenesis

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p62, a Phosphotyrosine-independent Ligand of the SH2 Domain of p56 , Belongs to a New Class of Ubiquitin-binding Proteins

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In Vitro Assembly and Recognition of Lys-63 Polyubiquitin Chains

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Mass Spectrometric and Mutational Analyses Reveal Lys-6-linked Polyubiquitin Chains Catalyzed by BRCA1-BARD1 Ubiquitin Ligase

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Amyloid β-Protein Inhibits Ubiquitin-dependent Protein Degradation in Vitro

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Localization of Atypical Protein Kinase C Isoforms into Lysosome-Targeted Endosomes through Interaction with p62

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Structure and functional properties of the ubiquitin binding protein p62

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Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease: possible role in tangle formation

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Ubiquitylation of synphilin-1 and α-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease

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The Atypical Protein Kinase C-interacting Protein p62 Is a Scaffold for NF-κB Activation by Nerve Growth Factor

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Characterization of Cytoplasmic α-Synuclein Aggregates

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P62 and the sequestosome, a novel mechanism for protein metabolism

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Microtubule-associated Protein 1B Is a Component of Cortical Lewy Bodies and Binds α-Synuclein Filaments

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Structure of the Ubiquitin-associated Domain of p62 (SQSTM1) and Implications for Mutations That Cause Paget's Disease of Bone

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The p38 MAP kinase signaling pathway in Alzheimer's disease

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The Ubiquitin-Associated (UBA) Domain: On the Path from Prudence to Prurience

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NEDD8 protein is involved in ubiquitinated inclusion bodies

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The PB1 domain and the PC motif‐containing region are structurally similar protein binding modules

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Ubiquitinated inclusions and neuronal cell death.

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A method to identify p62’s UBA domain interacting proteins

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PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1

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Genetic inactivation of p62 leads to accumulation of hyperphosphorylated tau and neurodegeneration

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Sequestosome 1/p62 links familial ALS mutant SOD1 to LC3 via an ubiquitin‐independent mechanism

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