Tau post-translational modifications: dynamic transformers of tau function, degradation, and aggregation
C Alquezar, S Arya, AW Kao - Frontiers in neurology, 2021 - frontiersin.org
Post-translational modifications (PTMs) on tau have long been recognized as affecting
protein function and contributing to neurodegeneration. The explosion of information on …
protein function and contributing to neurodegeneration. The explosion of information on …
Tau in physiology and pathology
Y Wang, E Mandelkow - Nature reviews neuroscience, 2016 - nature.com
Tau is a microtubule-associated protein that has a role in stabilizing neuronal microtubules
and thus in promoting axonal outgrowth. Structurally, tau is a natively unfolded protein, is …
and thus in promoting axonal outgrowth. Structurally, tau is a natively unfolded protein, is …
Expansion of human-specific GGC repeat in neuronal intranuclear inclusion disease-related disorders
Y Tian, JL Wang, W Huang, S Zeng, B Jiao, Z Liu… - The American Journal of …, 2019 - cell.com
Neuronal intranuclear inclusion disease (NIID) is a slowly progressing neurodegenerative
disease characterized by eosinophilic intranuclear inclusions in the nervous system and …
disease characterized by eosinophilic intranuclear inclusions in the nervous system and …
[HTML][HTML] Translation of GGC repeat expansions into a toxic polyglycine protein in NIID defines a novel class of human genetic disorders: the polyG diseases
M Boivin, J Deng, V Pfister, E Grandgirard… - Neuron, 2021 - cell.com
Neuronal intranuclear inclusion disease (NIID) is a neurodegenerative disease
characterized by the presence of intranuclear inclusions of unknown origin. NIID is caused …
characterized by the presence of intranuclear inclusions of unknown origin. NIID is caused …
SUMO modification of Huntingtin and Huntington's disease pathology
JS Steffan, N Agrawal, J Pallos, E Rockabrand… - Science, 2004 - science.org
Huntington's disease (HD) is characterized by the accumulation of a pathogenic protein,
Huntingtin (Htt), that contains an abnormal polyglutamine expansion. Here, we report that a …
Huntingtin (Htt), that contains an abnormal polyglutamine expansion. Here, we report that a …
SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?
G Gill - Genes & development, 2004 - genesdev.cshlp.org
The small ubiquitin-related modifier SUMO posttranslationally modifies many proteins with
roles in diverse processes including regulation of transcription, chromatin structure, and …
roles in diverse processes including regulation of transcription, chromatin structure, and …
SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination
HB Luo, YY Xia, XJ Shu, ZC Liu… - Proceedings of the …, 2014 - National Acad Sciences
Intracellular accumulation of the abnormally modified tau is hallmark pathology of
Alzheimer's disease (AD), but the mechanism leading to tau aggregation is not fully …
Alzheimer's disease (AD), but the mechanism leading to tau aggregation is not fully …
Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and α-synuclein
V Dorval, PE Fraser - Journal of Biological Chemistry, 2006 - ASBMB
Sumoylation is an important post-translational modification that provides a rapid and
reversible means for controlling the activity, subcellular localization, and stability of target …
reversible means for controlling the activity, subcellular localization, and stability of target …
Neuronal SUMOylation: mechanisms, physiology, and roles in neuronal dysfunction
JM Henley, TJ Craig, KA Wilkinson - Physiological reviews, 2014 - journals.physiology.org
Protein SUMOylation is a critically important posttranslational protein modification that
participates in nearly all aspects of cellular physiology. In the nearly 20 years since its …
participates in nearly all aspects of cellular physiology. In the nearly 20 years since its …
[HTML][HTML] SUMO protein modification
RJ Dohmen - Biochimica et Biophysica Acta (BBA)-Molecular Cell …, 2004 - Elsevier
SUMO (small ubiquitin-related modifier) family proteins are not only structurally but also
mechanistically related to ubiquitin in that they are posttranslationally attached to other …
mechanistically related to ubiquitin in that they are posttranslationally attached to other …