Immunoreactivity to Lys63-linked polyubiquitin is a feature of neurodegeneration

Molecular Pathways of Neurodegeneration in Parkinson's Disease

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Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease, and Alzheimer's disease, as well as Rosenthal fibres in cerebellar astrocytomas, cytoplasmic bodies in muscle, and mallory bodies in alcoholic liver disease

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Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases

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Certain Pairs of Ubiquitin-conjugating Enzymes (E2s) and Ubiquitin-Protein Ligases (E3s) Synthesize Nondegradable Forked Ubiquitin Chains Containing All Possible Isopeptide Linkages

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Inhibition of Proteolysis and Cell Cycle Progression in a Multiubiquitination-Deficient Yeast Mutant

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

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Depletion of 26S Proteasomes in Mouse Brain Neurons Causes Neurodegeneration and Lewy-Like Inclusions Resembling Human Pale Bodies

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Inhibition of the ubiquitin-proteasome system in Alzheimer's disease

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Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation

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Alzheimer Disease-specific Conformation of Hyperphosphorylated Paired Helical Filament-Tau Is Polyubiquitinated through Lys-48, Lys-11, and Lys-6 Ubiquitin Conjugation

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Lysine 63‐linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome

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Ubiquitin is associated with abnormal cytoplasmic filaments characteristic of neurodegenerative diseases.

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Analysis of nondegradative protein ubiquitylation with a monoclonal antibody specific for lysine-63-linked polyubiquitin

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Assembly of Lysine 63-linked Ubiquitin Conjugates by Phosphorylated α-Synuclein Implies Lewy Body Biogenesis

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Shortfalls in the peptidyl-prolyl cis–trans isomerase protein Pin1 in neurons are associated with frontotemporal dementias

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Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease

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Ubiquitin-like protein conjugation and the ubiquitin–proteasome system as drug targets

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Tau degradation: The ubiquitin–proteasome system versus the autophagy-lysosome system

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Assembly, structure, and function of the 26S proteasome

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Versatile Roles of K63-Linked Ubiquitin Chains in Trafficking

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The Ubiquitin-Proteasome System and the Autophagic-Lysosomal System in Alzheimer Disease

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Polyubiquitin Linkage Profiles in Three Models of Proteolytic Stress Suggest the Etiology of Alzheimer Disease

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Comparative Proteomic Analysis Identifies a Role for SUMO in Protein Quality Control

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Mutations in the ubiquitin-binding domain of OPTN/optineurin interfere with autophagy-mediated degradation of misfolded proteins by a dominant-negative mechanism

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The ubiquitin proteasome system in neurodegenerative diseases: Culprit, accomplice or victim?

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Tau interactome mapping based identification of Otub1 as Tau deubiquitinase involved in accumulation of pathological Tau forms in vitro and in vivo

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Ubiquitin signaling in neurodegenerative diseases: an autophagy and proteasome perspective

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Role of ubiquitin–proteasome-mediated proteolysis in nervous system disease

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K63-linked ubiquitination and neurodegeneration

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Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies

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Of the atypical PKCs, Par-4 and p62: recent understandings of the biology and pathology of a PB1-dominated complex

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Role of Post‐translational Modifications in Alzheimer's Disease

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Lysine 63-linked ubiquitination of tau oligomers contributes to the pathogenesis of Alzheimer’s disease

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Degradation or aggregation: the ramifications of post-translational modifications on tau

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Mutant ubiquitin decreases amyloid β plaque formation in a transgenic mouse model of Alzheimer’s disease

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Review: The ubiquitin-proteasome system: contributions to cell death or survival in neurodegeneration

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Proteasome Inhibition Promotes Parkin-Ubc13 Interaction and Lysine 63-Linked Ubiquitination

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Diverse polyubiquitin chains accumulate following 26S proteasomal dysfunction in mammalian neurones

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Identification of linear polyubiquitin chain immunoreactivity in tau pathology of Alzheimer’s disease

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Dangerous Liaisons: Tau Interaction with Muscarinic Receptors

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Altered Proteostasis in Neurodegenerative Tauopathies

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Suppressing UBE2N ameliorates Alzheimer's disease pathology through the clearance of amyloid beta

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Misframed Proteins and Neurodegeneration: A Novel View on Alzheimer’s and Parkinson’s Diseases

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Role of frameshift ubiquitin B protein in Alzheimer's disease

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Heterozygosity for the proteasomal Psmc1 ATPase is insufficient to cause neuropathology in mouse brain, but causes cell cycle defects in mouse embryonic fibroblasts

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Post-translational modifications as a regulatory code for tau function in health and disease

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The HEK293T cells manage overload by the overexpressed full-length Htt variants via proteasome activation

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Huntingtin, the Major Factor in Huntington’s Disease Development. Main Functions and Intracellular Proteolysis

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Neuronal cell line expressing full-length mutant huntingtin displays alteration of proteasome activityPreprint

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MARINESCO BODIES: INTRANUCLEAR INCLUSION-BODIESOF DOPAMINERGIC NEURONS

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Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases

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K63-linked ubiquitination and neurodegeneration

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