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Brian C. Capell

Researcher at University of Pennsylvania

Publications -  61
Citations -  4478

Brian C. Capell is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Biology & Epigenetics. The author has an hindex of 21, co-authored 44 publications receiving 3614 citations. Previous affiliations of Brian C. Capell include New York University & University of North Carolina at Chapel Hill.

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Cytoplasmic chromatin triggers inflammation in senescence and cancer

TL;DR: It is shown that cytoplasmic chromatin activates the innate immunity cytosolic DNA-sensing cGAS–STING (cyclic GMP–AMP synthase linked to stimulator of interferon genes) pathway, leading both to short-term inflammation to restrain activated oncogenes and to chronic inflammation that associates with tissue destruction and cancer.
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Human laminopathies: nuclei gone genetically awry.

TL;DR: The study of LMNA, its products and the phenotypes that result from its mutation have provided important insights into subjects ranging from transcriptional regulation, the cell biology of the nuclear lamina and mechanisms of ageing.
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Autophagy mediates degradation of nuclear lamina

TL;DR: The study suggests that this new function of autophagy acts as a guarding mechanism protecting cells from tumorigenesis, and prevents activated RAS-induced lamin B1 loss and attenuates oncogene-induced senescence in primary human cells.
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Lamin B1 depletion in senescent cells triggers large-scale changes in gene expression and the chromatin landscape

TL;DR: Comparing genome-wide Lys4 trimethylation on histone H3 and H3K27me3 distributions between proliferating and senescent human cells found dramatic differences in senescence, suggesting that pre-malignant senescent chromatin changes foreshadow epigenetic cancer changes.
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Inhibiting farnesylation of progerin prevents the characteristic nuclear blebbing of Hutchinson-Gilford progeria syndrome

TL;DR: The results suggest that treatment with FTIs represents a potential therapy for patients with HGPS, and hypothesized that retention of the farnesyl group causes progerin to become permanently anchored in the nuclear membrane, disrupting proper nuclear scaffolding and causing the characteristic nuclear blebbing seen in HGPS cells.