Different prelamin A forms accumulate in human fibroblasts: a study in experimental models and progeria.

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Different prelamin A forms accumulate in human fibroblasts: a study in experimental models and progeria.

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2009 nî lūn-bûn

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2009年の論文

@ja

2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

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Different prelamin A forms acc ...... erimental models and progeria.

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Different prelamin A forms acc ...... erimental models and progeria.

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prefLabel

Different prelamin A forms acc ...... erimental models and progeria.

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P1476

Different prelamin A forms acc ...... perimental models and progeria

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C Le Dour

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C Vigouroux

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D Camozzi

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E Schena

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G Novelli

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M Auclair

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M Caron

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M Magnani

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M R D'Apice

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N M Maraldi

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P2860

Prenylated prelamin A interacts with Narf, a novel nuclear protein

Coupling of the nucleus and cytoplasm: role of the LINC complex

Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome

Farnesylated lamins, progeroid syndromes and farnesyl transferase inhibitors

Lamin A and ZMPSTE24 (FACE-1) defects cause nuclear disorganization and identify restrictive dermopathy as a lethal neonatal laminopathy

Nuclear lamins: laminopathies and their role in premature ageing.

Alterations in mitosis and cell cycle progression caused by a mutant lamin A known to accelerate human aging

Blocking protein farnesyltransferase improves nuclear blebbing in mouse fibroblasts with a targeted Hutchinson-Gilford progeria syndrome mutation.

Lamin a truncation in Hutchinson-Gilford progeria.

Compound heterozygosity for mutations in LMNA causes a progeria syndrome without prelamin A accumulation.

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scholarly article

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10.4081/EJH.2009.E6

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Giovanna Lattanzi

Cristina Capanni

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2009-03-31T00:00:00Z

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30256865

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