Related Experiment Video
Updated: Apr 6, 2026
10:34
A High-content Assay for Monitoring AMPA Receptor Trafficking
Published on: January 28, 2019
8.2K
Battling Alzheimer's Disease: Targeting SUMOylation-Mediated Pathways
Wagner Carbolin Martins1, Carla Inês Tasca1, Helena Cimarosti2
1Departamento de Bioquímica, Centro de Ciências Biológicas, Universidade Federal de Santa Catarina (UFSC), Campus Trindade, Florianópolis, SC, 88040-900, Brazil.
Neurochemical Research
|August 1, 2015
Summary
Small ubiquitin-like modifier (SUMO) conjugation regulates hundreds of proteins. SUMOylation is increasingly linked to Alzheimer
Area of Science:
- Biochemistry
- Molecular Biology
- Neuroscience
Background:
- SUMOylation is a crucial post-translational modification regulating protein function in eukaryotic cells.
- Its role in Alzheimer's disease (AD) pathophysiology is an emerging area of research.
Purpose of the Study:
- To review the current literature on SUMOylation's involvement in Alzheimer's disease.
- To provide an overview of potential SUMOylation targets and pathways implicated in AD pathogenesis.
Main Methods:
- Literature review of studies investigating SUMOylation in Alzheimer's disease.
Main Results:
- SUMOylation affects key AD-associated proteins like amyloid precursor protein, amyloid β, and tau.
- SUMOylation also regulates critical AD-related processes including inflammation, mitochondrial dynamics, and synaptic plasticity.
Conclusions:
- SUMOylation plays a significant role in the complex mechanisms underlying Alzheimer's disease.
- Further research into SUMOylation targets and pathways could reveal novel therapeutic strategies for AD.
More Related Videos
08:33Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models
Published on: March 24, 2019
8.0K
06:41Quantitative Analysis of Mitochondria-Associated Endoplasmic Reticulum Membrane (MAM) Stabilization in a Neural Model of Alzheimer's Disease (AD)
Published on: January 10, 2025
1.3K
Related Concept Videos
01:26Alzheimer's Disease: Overview
2.0K
Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
The clinical diagnosis of AD hinges on the presence of memory and other cognitive impairments. Biomarkers, such as changes in Aβ...
The clinical diagnosis of AD hinges on the presence of memory and other cognitive impairments. Biomarkers, such as changes in Aβ...
2.0K
01:22Alzheimer's Disease: Treatment
1.2K
Alzheimer's Disease (AD), a neurodegenerative disorder, is pathologically identified by amyloid plaques and neurofibrillary tangles composed of tau protein. AD pharmacotherapy aims to manage cognitive symptoms, delay disease progression, and treat behavioral symptoms. The treatment is primarily symptomatic and palliative, with no definitive disease-modifying therapy available. Cholinesterase inhibitors, including donepezil (Aricept), rivastigmine (Exelon), and galantamine (Razadyne), are...
1.2K
01:13The Proteasome
2.0K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
2.0K
02:18The Proteasome
10.6K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
10.6K
03:03Amyloid Fibrils
13.0K
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
13.0K
01:15Parkinson's Disease: Overview
2.4K
Neurodegenerative disorders are progressive diseases that cause irreversible damage and loss to neurons in specific brain areas. Examples of these disorders include Parkinson's disease, Alzheimer's disease, Multiple Sclerosis (MS), and Amyotrophic Lateral Sclerosis (ALS). These disorders share characteristics such as proteinopathies, selective neuronal vulnerability, and a complex interplay between genetic and environmental factors. The primary therapeutic goal for these conditions is...
2.4K