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References from Role of ubiquitin-mediated proteolysis in the pathogenesis of neurodegenerative disorders. Local targets link to admitted publications; unresolved targets remain external evidence.
Ubiquitin: not just for proteasomes anymore
10.1016/s0955-0674(03)00010-3 · 2003 · External reference
In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome
10.1093/emboj/16.16.4826 · 1997 · External reference
Tau and ubiquitin immunoreactivity at different stages of formation of Alzheimer neurofibrillary tangles
1989 · External reference
Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer’s disease
10.1016/0006-8993(89)91396-6 · 1989 · External reference
Impairment of the ubiquitin–proteasome system by protein aggregation
10.1126/science.292.5521.1552 · 2001 · External reference
A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
10.1126/science.2538923 · 1989 · External reference
Proteasomal degradation of tau protein
10.1046/j.1471-4159.2002.01137.x · 2002 · External reference
Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
10.1016/s0092-8674(00)00126-4 · 2000 · External reference
Mutant ubiquitin expressed in Alzheimer’s disease causes neuronal death
10.1096/fj.01-0438com · 2001 · External reference
Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
10.1126/science.277.5334.1990 · 1997 · External reference
Activity level controls postsynaptic composition and signaling via the ubiquitin–proteasome system
10.1038/nn1013 · 2003 · External reference
Pathological lesions of Alzheimer’s disease and dementia with Lewy bodies brains exhibit immunoreactivity to an ATPase that is a regulatory subunit of the 26S proteasome
10.1016/s0304-3940(96)13192-x · 1996 · External reference
Neurofibrillary tangles in progressive supranuclear palsy brains exhibit immunoreactivity to frameshift mutant ubiquitin-B protein
10.1016/s0304-3940(99)00917-9 · 2000 · External reference
Identification of genes that modify ataxin-1-induced neurodegeneration
10.1038/35040584 · 2000 · External reference
Ubiquitin Lys63 is involved in ubiquitination of a yeast plasma membrane protein
10.1093/emboj/16.19.5847 · 1997 · External reference
Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions
10.1126/science.290.5493.985 · 2000 · External reference
Alzheimer’s disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
10.1016/s0006-291x(84)80190-4 · 1984 · External reference
Tau protein and the neurofibrillary pathology of Alzheimer’s disease
10.1016/0166-2236(93)90078-z · 1993 · External reference
Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
10.1038/383550a0 · 1996 · External reference
Tau mutations cause frontotemporal dementias
10.1016/s0896-6273(00)80615-7 · 1998 · External reference
Alpha-synuclein immunoreactivity in dementia with Lewy bodies: morphological staging and comparison with ubiquitin immunostaining
10.1007/s004010051135 · 2000 · External reference
Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Abeta 42 fibrils
10.1126/science.1062097 · 2001 · External reference
Amyloid beta-protein inhibits ubiquitin-dependent protein degradation in vitro
10.1074/jbc.270.34.19702 · 1995 · External reference
Phosphorylated alpha-synuclein is ubiquitinated in alpha-synucleinopathy lesions
10.1074/jbc.m208046200 · 2002 · External reference
Human recombinant NACP/alpha-synuclein is aggregated and fibrillated in vitro: relevance for Lewy body disease
10.1016/s0006-8993(98)00514-9 · 1998 · External reference
Spongiform degeneration in mahoganoid mutant mice
10.1126/science.1079694 · 2003 · External reference
Ubiquitin and the synapse
10.1038/nrn961 · 2002 · External reference
The ubiquitin system
10.1146/annurev.biochem.67.1.425 · 1998 · External reference
Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly
10.1097/00005072-199702000-00002 · 1997 · External reference
An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
10.1016/s0092-8674(01)00407-x · 2001 · External reference
Purification and characterization of Lewy bodies from the brains of patients with diffuse Lewy body disease
1996 · External reference
A proteolytic pathway that recognizes ubiquitin as a degradation signal
10.1074/jbc.270.29.17442 · 1995 · External reference
Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer’s disease
10.1046/j.1471-4159.2003.01642.x · 2003 · External reference
Impaired proteasome function in Alzheimer’s disease
10.1046/j.1471-4159.2000.0750436.x · 2000 · External reference
UBE3A/E6-AP mutations cause Angelman syndrome
10.1038/ng0197-70 · 1997 · External reference
Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice
10.1016/s0092-8674(00)81781-x · 1998 · External reference
Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson’s disease
10.1038/ng0298-106 · 1998 · External reference
Multicatalytic proteinase is present in Lewy bodies and neurofibrillary tangles in diffuse Lewy body disease brains
10.1016/0304-3940(91)90751-e · 1991 · External reference
Inhibition of the ubiquitin–proteasome system in Alzheimer’s disease
10.1073/pnas.170173897 · 2000 · External reference
A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
10.1038/416763a · 2002 · External reference
Does an inhibition of the ubiquitin/26S proteasome pathway of protein degradation underlie the pathogenesis of non-familial Alzheimer’s disease?
10.1054/mehy.2000.1198 · 2001 · External reference
The ubiquitin protein catabolic disorders
10.1046/j.1365-2990.2001.00335.x · 2001 · External reference
Characterization of cytoplasmic alpha-synuclein aggregates. Fibril formation is tightly linked to the inclusion-forming process in cells
10.1074/jbc.m208192200 · 2002 · External reference
Neurodegenerative tauopathies
10.1146/annurev.neuro.24.1.1121 · 2001 · External reference
The ubiquitin pathway in Parkinson’s disease
10.1038/26652 · 1998 · External reference
Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
10.1126/science.1058189 · 2001 · External reference
Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation
10.1083/jcb.200111034 · 2002 · External reference
The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson’s disease susceptibility
10.1016/s0092-8674(02)01012-7 · 2002 · External reference
Endoproteolytic activity of the proteasome
10.1126/science.1079293 · 2003 · External reference
Defective ubiquitination of cerebral proteins in Alzheimer’s disease
10.1002/1097-4547(20001015)62:2<302::aid-jnr15>3.0.co;2-l · 2000 · External reference
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
10.1002/path.1711550105 · 1988 · External reference
A filamentous inclusion body within anterior horn neurones in motor neurone disease defined by immunocytochemical localisation of ubiquitin
10.1016/0304-3940(88)90296-0 · 1988 · External reference
Quality control of mRNA function
10.1016/s0092-8674(01)00202-1 · 2001 · External reference
Proteasomal-dependent aggregate reversal and absence of cell death in a conditional mouse model of Huntington’s disease
10.1523/jneurosci.21-22-08772.2001 · 2001 · External reference
De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome
10.1038/ng0197-74 · 1997 · External reference
Alpha-synuclein-enhanced green fluorescent protein fusion proteins form proteasome sensitive inclusions in primary neurons
10.1016/s0306-4522(01)00113-0 · 2001 · External reference
Proteasomal function is impaired in substantia nigra in Parkinson’s disease
10.1016/s0304-3940(00)01701-8 · 2001 · External reference
Selective loss of 20S proteasome alpha-subunits in the substantia nigra pars compacta in Parkinson’s disease
10.1016/s0304-3940(02)00296-3 · 2002 · External reference
Impairment of the ubiquitin–proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures
10.1046/j.1471-4159.2002.00821.x · 2002 · External reference
Altered proteasomal function in sporadic Parkinson’s disease
10.1006/exnr.2002.8050 · 2003 · External reference
Ubiquitin is a component of paired helical filaments in Alzheimer’s disease
10.1126/science.3029875 · 1987 · External reference
Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments
10.1016/0896-6273(93)90063-w · 1993 · External reference
How the ubiquitin–proteasome system controls transcription
10.1038/nrm1049 · 2003 · External reference
Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
10.1016/s1097-2765(01)00407-5 · 2001 · External reference
Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons
10.1016/s0896-6273(02)01125-x · 2002 · External reference
Mutation in the alpha-synuclein gene identified in families with Parkinson’s disease
10.1126/science.276.5321.2045 · 1997 · External reference
Proteasomal inhibition leads to formation of ubiquitin/alpha-synuclein-immunoreactive inclusions in PC12 cells
10.1046/j.1471-4159.2001.00474.x · 2001 · External reference
Intragenic deletions in the gene encoding ubiquitin carboxyl-terminal hydrolase in gad mice
10.1038/12647 · 1999 · External reference
Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
10.1016/s0092-8674(00)81782-1 · 1998 · External reference
Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure
10.1016/s0021-9258(19)51080-8 · 1994 · External reference
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
10.1038/12647 · 1999 · External reference
Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson’s disease
10.1126/science.1060627 · 2001 · External reference
Aggregated and monomeric alpha-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function
10.1074/jbc.m208641200 · 2003 · External reference
A ubiquitin mutant with specific defects in DNA repair and multiubiquitination
10.1128/mcb.15.3.1265 · 1995 · External reference
Alpha-synuclein in Lewy bodies
10.1038/42166 · 1997 · External reference
Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson’s disease and dementia with Lewy bodies
10.1016/s0304-3940(98)00504-7 · 1998 · External reference
Expression of mutant alpha-synuclein causes increased susceptibility to dopamine toxicity
10.1093/hmg/9.18.2683 · 2000 · External reference
Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis
10.1093/hmg/10.9.919 · 2001 · External reference
Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein
10.1093/hmg/ddg074 · 2003 · External reference
Recognition of the polyubiquitin proteolytic signal
10.1093/emboj/19.1.94 · 2000 · External reference
Alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
10.1016/s0014-5793(01)03115-5 · 2001 · External reference
10.1074/jbc.m212235200
10.1074/jbc.m212235200 · External reference
Clinical and pathologic abnormalities in a family with parkinsonism and parkin gene mutations
10.1212/wnl.56.4.555 · 2001 · External reference
Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer’s and Down’s syndrome patients
10.1126/science.279.5348.242 · 1998 · External reference
+1 Proteins and aging
10.1016/s1357-2725(02)00043-2 · 2002 · External reference
Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome
10.1006/scdb.2000.0164 · 2000 · External reference
Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease
10.1038/ng1006 · 2002 · External reference
Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila
10.1016/s0896-6273(03)00143-0 · 2003 · External reference
