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References from SUMO-modifying Huntington’s disease. Local targets link to admitted publications; unresolved targets remain external evidence.
SUMOylation: implications for neurodegenerative diseases
2017 · External reference
Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
10.1038/nature02998 · 2004 · External reference
Huntingtin and the synapse
10.3389/fncel.2021.689332 · 2021 · External reference
Bioinformatics analysis of Ras homologue enriched in the striatum, a potential target for Huntington’s disease therapy
2019 · External reference
Sumoylation on its 25th anniversary: mechanisms, pathology, and emerging concepts
10.1111/febs.15319 · 2020 · External reference
Sumo: from bench to bedside
10.1152/physrev.00025.2019 · 2020 · External reference
The function of SUMOylation and its crucial roles in the development of neurological diseases
2021 · External reference
Site-specific phosphorylation of huntingtin exon 1 recombinant proteins enabled by the discovery of novel kinases
10.1002/cbic.202000508 · 2021 · External reference
Deciphering protein post-translational modifications using chemical biology tools
10.1038/s41570-020-00223-8 · 2020 · External reference
A role for autophagy in Huntington’s disease
10.1016/j.nbd.2018.08.010 · 2019 · External reference
The interrelationship of proteasome impairment and oligomeric intermediates in neurodegeneration
10.1111/acel.12359 · 2015 · External reference
SUMO on the road to neurodegeneration
10.1016/j.bbamcr.2007.03.017 · 2007 · External reference
Altered gut microbiota related to inflammatory responses in patients with Huntington’s disease
10.3389/fimmu.2020.603594 · 2021 · External reference
Small changes, big impact: posttranslational modifications and function of huntingtin in huntington disease
10.1177/1073858410390378 · 2011 · External reference
Gene targeting techniques for Huntington’s disease
2021 · External reference
Cellular maintenance of nuclear protein homeostasis
10.1007/s00018-013-1530-y · 2014 · External reference
A caspase-3-cleaved fragment of the glial glutamate transporter EAAT2 is sumoylated and targeted to promyelocytic leukemia nuclear bodies in mutant SOD1-linked amyotrophic lateral sclerosis
10.1074/jbc.m704314200 · 2007 · External reference
SUMO-regulated mitochondrial function in Parkinson’s disease
10.1111/jnc.13599 · 2016 · External reference
SENP3-mediated deSUMOylation of dynamin-related protein 1 promotes cell death following ischaemia
2013 · External reference
Regulation of mitochondrial dynamics and neurodegenerative diseases
2011 · External reference
The role of Rhes, Ras homolog enriched in striatum, in neurodegenerative processes
10.1016/j.yexcr.2013.03.033 · 2013 · External reference
Health state utility values (QALY weights) for Huntington’s disease: an analysis of data from the European Huntington’s Disease Network (EHDN)
10.1007/s10198-019-01092-9 · 2019 · External reference
Regulation of HSF1 protein stabilization: an updated review
10.1016/j.ejphar.2018.01.005 · 2018 · External reference
A chain of events: regulating target proteins by SUMO polymers
10.1016/j.tibs.2020.09.002 · 2021 · External reference
Human cystathionine β-synthase is a target for sumoylation
10.1021/bi0615644 · 2006 · External reference
Targeting SUMO signaling to wrestle cancer
10.1016/j.trecan.2020.11.009 · 2020 · External reference
Supression of protein aggregation by chaperone modification of high molecular weight complexes
10.1093/brain/aws022 · 2012 · External reference
Classification of extrapyramidal disorders
1981 · External reference
SUMO5, a novel poly-SUMO isoform, regulates PML nuclear bodies
2016 · External reference
Ubiquitin-dependent and independent roles of SUMO in proteostasis
2016 · External reference
Loss of Hap1 selectively promotes striatal degeneration in Huntington disease mice
10.1073/pnas.2002283117 · 2020 · External reference
Increased SUMO-2/3-ylation mediated by SENP3 degradation is protective against cadmium-induced caspase 3–dependent cytotoxicity
10.2131/jts.42.529 · 2017 · External reference
An overview of the possible therapeutic role of SUMOylation in the treatment of Alzheimer’s disease
10.1016/j.phrs.2017.12.023 · 2018 · External reference
Battling Alzheimer’s disease: targeting SUMOylation-mediated pathways
10.1007/s11064-015-1681-3 · 2016 · External reference
Huntington’s disease: a clinical review
10.1111/ene.13413 · 2018 · External reference
Transcriptional profiles for distinct aggregation states of mutant Huntingtin exon 1 protein unmask new Huntington’s disease pathways
10.1016/j.mcn.2017.07.004 · 2017 · External reference
PIAS1 modulates striatal transcription, DNA damage repair, and SUMOylation with relevance to Huntington’s disease
10.1073/pnas.2021836118 · 2021 · External reference
The thyroid hormone-target gene Rhes a novel crossroad for neurological and psychiatric disorders: new insights from animal models
10.1016/j.neuroscience.2018.05.027 · 2018 · External reference
SUMO-2 and PIAS1 modulate insoluble mutant huntingtin protein accumulation
10.1016/j.celrep.2013.06.034 · 2013 · External reference
PIAS1 regulates mutant huntingtin accumulation and Huntington’s disease-associated phenotypes in vivo
10.1016/j.neuron.2016.03.016 · 2016 · External reference
SUMO-targeted ubiquitin ligases (STUbLs) reduce the toxicity and abnormal transcriptional activity associated with a mutant, aggregation-prone fragment of huntingtin
10.3389/fgene.2018.00379 · 2018 · External reference
The regulation of mitochondrial morphology: intricate mechanisms and dynamic machinery
10.1016/j.cellsig.2011.05.021 · 2011 · External reference
Neuropsychiatric burden in Huntington’s disease
10.3390/brainsci7060067 · 2017 · External reference
Biological markers of cognition in prodromal Huntington’s disease: a review
10.1016/j.bandc.2011.07.009 · 2011 · External reference
Protein aggregation and misfolding: good or evil?
2012 · External reference
SUMO-1 marks the nuclear inclusions in familial neuronal intranuclear inclusion disease
10.1016/j.expneurol.2003.07.004 · 2003 · External reference
SUMOylation in neurodegenerative diseases
10.1159/000502142 · 2020 · External reference
Evaluation of post-translational modifications in histone proteins: a review on histone modification defects in developmental and neurological disorders
10.1007/s12038-020-00099-2 · 2020 · External reference
Post-translational modifications in proteins: resources, tools and prediction methods
10.1093/database/baab012 · 2021 · External reference
Overview of Huntington’s disease models: neuropathological, molecular, and behavioral differences
10.1002/cpns.47 · 2018 · External reference
Dynamin-related protein 1 and mitochondrial fragmentation in neurodegenerative diseases
10.1016/j.brainresrev.2010.11.004 · 2011 · External reference
Generation of native, untagged huntingtin exon1 monomer and fibrils using a SUMO fusion strategy
2018 · External reference
Huntington disease: pathogenesis, biomarkers, and approaches to experimental therapeutics
10.1016/s1353-8020(09)70800-4 · 2009 · External reference
SUMO and its role in human diseases
10.1016/b978-0-12-386041-5.00004-2 · 2011 · External reference
Do post-translational modifications influence protein aggregation in neurodegenerative diseases: a systematic review
10.3390/brainsci10040232 · 2020 · External reference
SUMOylation prevents huntingtin fibrillization and localization onto lipid membranes
10.1021/acschemneuro.9b00509 · 2020 · External reference
Involvement of the protein ras homolog enriched in the striatum, rhes, in dopaminergic neurons’ degeneration: link to Parkinson’s disease
10.3390/ijms22105326 · 2021 · External reference
Rhes travels from cell to cell and transports Huntington disease protein via TNT-like protrusion
10.1083/jcb.201807068 · 2019 · External reference
SUMO proteins in the cardiovascular system: friend or foe?
10.1186/s12929-020-00689-0 · 2020 · External reference
Mutant huntingtin’s interaction with mitochondrial protein Drp1 impairs mitochondrial biogenesis and causes defective axonal transport and synaptic degeneration in Huntington’ s disease
10.1093/hmg/ddr475 · 2012 · External reference
Does huntingtin play a role in selective macroautophagy?
10.4161/cc.9.17.12718 · 2010 · External reference
SUMO modification of huntingtin and Huntington’s disease pathology
10.1126/science.1092194 · 2004 · External reference
Rhes, a physiologic regulator of sumoylation, enhances cross-sumoylation between the basic sumoylation enzymes E1 and Ubc9
10.1074/jbc.c110.127191 · 2010 · External reference
Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity
10.1126/science.1172871 · 2009 · External reference
Huntington’s disease is a disorder of the corpus striatum: focus on Rhes (Ras homologue enriched in the striatum)
10.1016/j.neuropharm.2010.10.025 · 2011 · External reference
Ectopic expression of the striatal-enriched GTPase Rhes elicits cerebellar degeneration and an ataxia phenotype in Huntington’s disease
10.1016/j.nbd.2015.05.011 · 2015 · External reference
Huntington disease: new insights into molecular pathogenesis and therapeutic opportunities
10.1038/s41582-020-0389-4 · 2020 · External reference
SUMO-1 co-localized with mutant atrophin-I with expanded polyglutamines accelerates intranuclear aggregation and cell death
10.1097/00001756-200212030-00038 · 2002 · External reference
Huntington disease: a quarter century of progress since the gene discovery
10.1016/j.jns.2018.09.022 · 2019 · External reference
IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
10.1083/jcb.200909067 · 2009 · External reference
Enhanced SUMOylation in polyglutamine diseases
10.1016/s0006-291x(02)00211-5 · 2002 · External reference
Inflammation in Huntington’s disease: a few new twists on an old tale
10.1016/j.jneuroim.2020.577380 · 2020 · External reference
Beyond the brain: widespread pathology in Huntington’s disease
10.1016/s1474-4422(09)70178-4 · 2009 · External reference
Body weight is a robust predictor of clinical progression in Huntington disease
10.1002/ana.25007 · 2017 · External reference
Molecular mechanisms in SUMO conjugation
10.1042/bst20190357 · 2020 · External reference
SUMOylation and deSUMOylation at a glance
10.1242/jcs.050542 · 2009 · External reference
The role of post-translational modifications of huntingtin in the pathogenesis of Huntington’s disease
10.1007/s12264-010-1118-6 · 2010 · External reference
Introduction to sumoylation
2017 · External reference
SUMO-1 is associated with a subset of lysosomes in glial protein aggregate diseases
10.1007/s12640-012-9358-z · 2013 · External reference
mTOR signaling pathway and mTOR inhibitors in cancer: progress and challenges
2020 · External reference