Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides.

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Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年学术文章

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2018年學術文章

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Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides.

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Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides.

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Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides.

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Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides.

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Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides.

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Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides.

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P1476

Autophagic Removal of Farnesylated Carboxy-Terminal Lamin Peptides

@en

P2093

Karima Djabali

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P2860

Dermal fibroblasts in Hutchinson-Gilford progeria syndrome with the lamin A G608G mutation have dysmorphic nuclei and are hypersensitive to heat stress

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

LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins

Inhibiting farnesylation of progerin prevents the characteristic nuclear blebbing of Hutchinson-Gilford progeria syndrome

Hutchinson-Gilford progeria mutant lamin A primarily targets human vascular cells as detected by an anti-Lamin A G608G antibody.

Mutation in a heterochromatin-specific chromosomal protein is associated with suppression of position-effect variegation in Drosophila melanogaster

Accumulation of mutant lamin A causes progressive changes in nuclear architecture in Hutchinson-Gilford progeria syndrome

LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing

The nuclear envelope

Molecular insights into the premature aging disease progeria

P31

scholarly article

P356

10.3390/CELLS7040033

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Xiang Lu

P577

2018-04-23T00:00:00Z

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P698

29690642

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P932

5946110

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