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Chemical Inhibition of NAT10 Corrects Defects of Laminopathic Cells
Open accessAbstract
Remodelin Nuclear Defects: Deregulation of A-type lamin proteins leads to disorganization of chromatin structure and misshapen nuclei, which are believed to underlie the pathologies of various human diseases, including the premature aging disorder Hutchinson Gilford progeria syndrome (HGPS) and various cancers. Larrieu et al. (p. 527 ) developed a small molecule, Remodelin, that not only improved nuclear shape defects of human lamin A/C–depleted cells, HGPS cells, and aged normal cells, but also decreased the levels of a DNA damage marker and improved global cellular fitness.
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“Remodelin, a small molecule that inhibits the acetyl-transferase protein NAT10 (Larrieu et al., 2014).”
From The Aging Epigenome (2016) · cites this paper as Larrieu et al., 2014
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“when cells derived from patients with the progeria disease HGPS were treated with the drug Remodelin, the cells had improved nuclear architecture and increased chromatin compaction, consistent with a gain of heterochromatin (Larrieu et al., 2014).”
From The Aging Epigenome (2016) · cites this paper as Larrieu et al., 2014
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Metadata
- Authors
- Larrieu, D., Britton, S., Demir, M., Rodriguez, R., & Jackson, S. P.
- Affiliations
- University of Cambridge (GB)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Britton, Sébastien
- Rodriguez, Raphaël
- Jackson, Stephen P.
- Venue
- Science
- Published
- 2014-05-02
- Volume
- 344
- Issue
- 6183
- Pages
- 527-532
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC4246063
- OpenAlex
- W2008052894
- Cited by
- 431
- References
- 27
- Citations by year
- 2026: 51 · 2025: 64 · 2024: 45 · 2023: 45 · 2022: 39 · 2021: 32 · 2020: 22 · 2019: 31 · 2018: 28 · 2017: 26 · 2016: 24 · 2015: 14 · 2014: 10
- FWCI
- 10.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- HAL (submittedVersion)
- Apollo (University of Cambridge) (submittedVersion)
- Apollo
- Funders
- Wellcome Trust (092096/Z/10/Z, WT092096, 092096)
- Cancer Research UK (18796, C6/A11224, C6946 /A14492, 11224, A11224)
- Medical Research Council (MR/L019116/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Skin and Cellular Biology Research
- Keywords
- NAT10, lamin A/C, laminopathies, Hutchinson-Gilford progeria syndrome, Remodelin, nuclear organization, chromatin organization, microtubule reorganization, DNA damage, premature aging, histone acetylation
- MeSH terms
- Cell Nucleus, Chromatin, Enzyme Inhibitors, Humans, Hydrazones, Microtubules, Progeria, Thiazoles, Nocodazole, Protein Structure, Tertiary, RNA, Small Interfering, Lamin Type A, Cell Line, Tumor, N-Terminal Acetyltransferases, N-Terminal Acetyltransferase E
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