The DOI matches its Crossref record; 80 of the 80 references it cites were found in a registry or an index.
TDP-43 functions and pathogenic mechanisms implicated in TDP-43 proteinopathies
Open accessAbstract
Given the critical role for TDP-43 in diverse neurodegenerative diseases including amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD-TDP), there has been a recent surge in efforts to understand the normal functions of TDP-43 and the molecular basis of dysregulation that occurs in TDP-43 proteinopathies. Here, we highlight recent findings examining TDP-43 molecular functions with particular emphasis on stress-mediated regulation of TDP-43 localization, putative downstream TDP-43 target genes and RNAs, as well as TDP-43 interacting proteins, all of which represent viable points of therapeutic intervention for ALS, FTLD-TDP, and related proteinopathies. Finally, we review current mouse models of TDP-43 and discuss their similarities and potential relevance to human TDP-43 proteinopathies including ALS and FTLD-TDP.
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Cites
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Self-citationHDAC6 is a microtubule-associated deacetylase
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Cited by
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Human endogenous retrovirus-K contributes to motor neuron disease
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HSP70 chaperones RNA-free TDP-43 into anisotropic intranuclear liquid spherical shells
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Metadata
- Authors
- Cohen, T. J., Lee, V. M. Y., & Trojanowski, J. Q.
- Venue
- Trends in Molecular Medicine
- Publisher
- Elsevier BV
- Published
- 2011-11
- Volume
- 17
- Issue
- 11
- Pages
- 659-667
- ISSN
- 1471-4914 (ISSN-L)
- OpenAlex
- W1985955085
- Cited by
- 269
- References
- 80
- FWCI
- 1.18
- Type
- journal article
- Language
- en
- Open access
- green
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