Cross Currents in Protein Misfolding Disorders: Interactions and Therapy
Open accessAbstract
Protein Misfolding Disorders (PMDs) are a group of diseases characterized by the accumulation of abnormally folded proteins. Despite the wide range of proteins and tissues involved, PMDs share similar molecular and pathogenic mechanisms. Several epidemiological, clinical and experimental reports have described the co-existence of PMDs, suggesting a possible cross-talk between them. A better knowledge of the molecular basis of PMDs could have important implications for understanding the mechanism by which these diseases appear and progress and ultimately to develop novel strategies for treatment. Due to their similar molecular mechanisms, common therapeutic strategies could be applied for the diseases in this group.
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TDP-43 binds to many cellular transcripts including tau and alpha synuclein, and its dysregulation may underlie some of the pathologies seen with these proteins; TDP-43 may influence tau isoform expression.
“TDP-43 binds to many cellular transcripts including tau and alpha synuclein, and its dysregulation may underlie some of the pathologies seen with these proteins [162]. In particular, TDP-43 may influence tau iso-form expression [136].”
From The neuropathology of sport (2014) · cites this paper as [136]
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References 82 · Cited by 72
Research works printed but not linked: 3
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- Authors
- Morales, R., Green, K., & Soto, C.
- Affiliations
- The University of Texas Health Science Center at Houston (US)
- Venue
- CNS & Neurological Disorders - Drug Targets
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2009-11-01
- Volume
- 8
- Issue
- 5
- Pages
- 363-371
- ISSN
- 1568-007X (ISSN-L)
- 1871-5273
- PMC
- PMC2804467
- OpenAlex
- W2141412231
- Cited by
- 72
- References
- 82
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 4 · 2023: 4 · 2022: 2 · 2021: 3 · 2020: 8 · 2019: 3 · 2018: 5 · 2017: 2 · 2016: 7 · 2015: 7 · 2014: 6 · 2013: 9 · 2012: 6
- FWCI
- 1.21
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- CNS & Neurological Disorders - Drug Targets (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Commons-TMC (Texas Medical Center) (submittedVersion)
- Funders
- National Institute on Aging (R01AG028821)
- National Institute of Neurological Disorders and Stroke (R01NS050349)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- proteinopathies, protein aggregation, protein folding, pathophysiological mechanisms, treatment options, neurodegenerative diseases
- MeSH terms
- Protein Conformation, Prion Diseases, Protein Folding, Proteostasis Deficiencies
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