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References from Monitoring the ubiquitin/proteasome system in conformational diseases. Local targets link to admitted publications; unresolved targets remain external evidence.
In vivo half-life of a protein is a function of its amino-terminal residue
10.1126/science.3018930 · 1986 · External reference
The recognition component of the N-end rule pathway
10.1002/j.1460-2075.1990.tb07516.x · 1990 · External reference
The proteasome: paradigm of a self-compartmentalizing protease
10.1016/s0092-8674(00)80929-0 · 1998 · External reference
Impairment of the ubiquitin-proteasome system by protein aggregation
10.1126/science.292.5521.1552 · 2001 · External reference
The N-end rule pathway controls the import of peptides through degradation of a transcriptional repressor
10.1093/emboj/17.1.269 · 1998 · External reference
Conformational disease
10.1016/s0140-6736(97)02073-4 · 1997 · External reference
Deubiquitinating enzymes: their diversity and emerging roles
10.1006/bbrc.1999.1880 · 1999 · External reference
Parkin ubiquitinates the α-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease
10.1038/nm1001-1144 · 2001 · External reference
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
10.1038/35050618 · 2001 · External reference
Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
10.1038/502 · 1998 · External reference
Stabilisation signals: a novel regulatory mechanism in the ubiquitin/proteasome system
10.1016/s0014-5793(02)03252-0 · 2002 · External reference
Inhibition of proteasomal degradation by the Gly-Ala repeat of Epstein-Barr virus is influenced by the length of the repeat and the strength of the degradation signal
10.1073/pnas.140217397 · 2000 · External reference
Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells
10.1038/75406 · 2000 · External reference
Rare genetic mutations shed light on the pathogenesis of Parkinson disease
10.1172/jci200317575 · 2003 · External reference
Mallory bodies revisited
10.1016/s0168-8278(00)80233-0 · 2000 · External reference
Mutant ubiquitin expressed in Alzheimer’s disease causes neuronal death
10.1096/fj.01-0438com · 2001 · External reference
Parkin. A multipurpose neuroprotective agent?
10.1016/s0896-6273(03)00201-0 · 2003 · 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
The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
10.1016/0092-8674(87)90711-2 · 1987 · External reference
Intranuclear inclusions and the ubiquitin-proteasome pathway: digestion of a red herring?
10.1016/s0896-6273(00)81022-3 · 1999 · External reference
Aggresome formation in liver cells in response to different toxic mechanisms: role of the ubiquitin-proteasome pathway and the frameshift mutant of ubiquitin
10.1006/exmp.2001.2401 · 2001 · External reference
Characterization and dynamics of aggresome formation by a cytosolic GFP-chimera
10.1083/jcb.146.6.1239 · 1999 · External reference
Parkin and the molecular pathways of Parkinson’s disease
10.1016/s0896-6273(01)00439-1 · 2001 · External reference
Degradation signals recognized by the Ubc6p-Ubc7p ubiquitin-conjugation enzyme pair
10.1128/mcb.20.19.7214-7219.2000 · 2000 · External reference
Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae
10.1093/emboj/17.10.2759 · 1998 · External reference
The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics
10.1126/science.1072994 · 2002 · External reference
Models of amyloid seeding in Alzheimer’s disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
10.1146/annurev.biochem.66.1.385 · 1997 · External reference
Phosphorylated α-synuclein is ubiquitinated in α-synucleinopathy lesions
10.1074/jbc.m208046200 · 2002 · External reference
The ubiquitin system
10.1146/annurev.biochem.67.1.425 · 1998 · External reference
ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
10.1126/science.273.5282.1725 · 1996 · External reference
A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin proteasome system
10.1074/jbc.m204955200 · 2002 · External reference
Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
10.1074/jbc.c000447200 · 2000 · 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
CHIP is associated with Parkin, a gene responsible for familial Parkinson’s disease, and enhances its ubiquitin ligase activity
10.1016/s1097-2765(02)00583-x · 2002 · External reference
A proteolytic pathway that recognises ubiquitin as a degradation signal
10.1074/jbc.270.29.17442 · 1995 · External reference
Aggresomes: a cellular response to misfolded proteins
10.1083/jcb.143.7.1883 · 1998 · External reference
Impaired proteasome function in Alzheimer’s disease
10.1046/j.1471-4159.2000.0750436.x · 2000 · External reference
Pathways accessory to proteasomal proteolysis are less efficient in major histocompatibility complex class I antigen production
10.1074/jbc.m211221200 · 2003 · External reference
Mutations in the parkin gene cause autosomal recessive juvenile Parkinsonism
10.1038/33416 · 1998 · External reference
A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
10.1016/s0092-8674(00)80574-7 · 1999 · External reference
Inhibition of the ubiquitin-proteasome system in Alzheimer’s disease
10.1073/pnas.170173897 · 2000 · External reference
Substrate targeting in the ubiquitin system
10.1016/s0092-8674(00)80752-7 · 1999 · External reference
Proteasome inhibitors: valuable new tools for cell biologists
10.1016/s0962-8924(98)01346-4 · 1998 · External reference
The ubiquitin pathway in Parkinson’s disease
10.1038/26652 · 1998 · External reference
A transgenic mouse model of the ubiquitin/proteasome system
10.1038/nbt851 · 2003 · 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 α-synuclein degradation and Parkinson’s disease susceptibility
10.1016/s0092-8674(02)01012-7 · 2002 · External reference
The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
10.1074/jbc.275.7.4613 · 2000 · External reference
Proteasomal function is impaired in substantia nigra in Parkinson’s disease
10.1016/s0304-3940(00)01701-8 · 2001 · External reference
Molecular misreading of the ubiquitin B gene and hepatic mallory body formation
10.1053/gast.2002.33629 · 2002 · External reference
10.1093/embo-reports/kve246 · 2001 · Admitted local publication
Lack of proteasome active site allostery as revealed by subunit-specific inhibitors
10.1016/s1097-2765(01)00188-5 · 2001 · 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
The human immunodeficiency virus (HIV)-1 protease inhibitor saquinavir inhibits proteasome function and causes apoptosis and radiosensitization in non-HIV-associated human cancer cells
2002 · External reference
Parkin protects against the toxicity associated with mutant α-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons
10.1016/s0896-6273(02)01125-x · 2002 · External reference
Mechanisms underlying ubiquitination
10.1146/annurev.biochem.70.1.503 · 2001 · External reference
Retrograde protein translocation: eradication of secretory proteins in health and disease
10.1016/s0968-0004(99)01420-6 · 1999 · External reference
Mutation in the α-synuclein gene identified in families with Parkinson’s disease
10.1126/science.276.5321.2045 · 1997 · External reference
Quantitating protein synthesis, degradation, and endogenous antigen processing
10.1016/s1074-7613(03)00051-7 · 2003 · External reference
Prion protein biology
10.1016/s0092-8674(00)81163-0 · 1998 · External reference
Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability
10.1038/35073627 · 2001 · External reference
The major substrates for TAP in vivo are derived from newly synthesised proteins
10.1038/35008103 · 2000 · External reference
Lessons from animal models of Huntington’s disease
10.1016/s0168-9525(01)02625-7 · 2002 · External reference
Rapid degradation of a large fraction of newly synthesised proteins by proteasomes
10.1038/35004754 · 2000 · External reference
Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases
10.1016/s0896-6273(01)00177-5 · 2001 · External reference
Ubiquitination of a new form of α-synuclein by parkin from human brain: implications for Parkinson’s disease
10.1126/science.1060627 · 2001 · External reference
A ubiquitin-based tagging system for controlled modulation of protein stability
10.1038/82422 · 2000 · External reference
Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components
10.1038/ncb859 · 2002 · External reference
Mallory body—a disease-associated type of sequestosome
10.1053/jhep.2002.32674 · 2002 · External reference
Degradation signals in lysine-asparagine sequence space
10.1093/emboj/18.21.6017 · 1999 · External reference
Parkin is linked to the ubiquitin pathway
10.1007/s001090100242 · 2001 · External reference
Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein
10.1093/hmg/ddg074 · 2003 · External reference
Mutations in RNA: a first example of molecular misreading in Alzheimer’s disease
10.1016/s0166-2236(98)01280-6 · 1998 · External reference
Frameshift mutants of β amyloid precursor protein and ubiquitin-B in Alzheimer’s and Down patients
10.1126/science.279.5348.242 · 1998 · External reference
The N-end rule
10.1101/sqb.1995.060.01.051 · 1995 · External reference
Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
10.1093/hmg/11.22.2689 · 2002 · External reference
Functional association of the parkin gene promoter with idiopathic Parkinson’s disease
10.1093/hmg/11.22.2787 · 2002 · External reference
Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome
10.1006/scdb.2000.0164 · 2000 · External reference
Ubiquitin-mediated proteolysis centres in HeLa cells: indication from studies of an inhibitor of the chymotrypsin-like activity of the proteasome
1996 · External reference
Genetically engineered mouse models of neurodegenerative diseases
10.1038/nn0702-633 · 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
PI31 is a modulator of proteasome formation and antigen processing
10.1073/pnas.212257299 · 2002 · External reference
Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
10.1073/pnas.240347797 · 2000 · External reference
Creating new fluorescent probes for cell biology
10.1038/nrm976 · 2002 · External reference
Glutamine repeats and neurodegeneration
10.1146/annurev.neuro.23.1.217 · 2000 · External reference