Investigating the purpose of prelamin A processing - sprookjes - yvandenbroek - TriplyDB

Investigating the purpose of prelamin A processing

Investigating the purpose of prelamin A processing

http://www.wikidata.org/entity/Q35015891

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When lamins go bad: nuclear structure and disease Nuclear lamins and neurobiology.Rapamycin treatment of Mandibuloacral dysplasia cells rescues localization of chromatin-associated proteins and cell cycle dynamics An absence of nuclear lamins in keratinocytes leads to ichthyosis, defective epidermal barrier function, and intrusion of nuclear membranes and endoplasmic reticulum into the nuclear chromatin LMNA cardiomyopathy: cell biology and genetics meet clinical medicine.Mitogen-activated protein kinase inhibitor regulation of heart function and fibrosis in cardiomyopathy caused by lamin A/C gene mutation.Lamins at a glance.Altered chromatin organization and SUN2 localization in mandibuloacral dysplasia are rescued by drug treatment.Nuclear lamins in the brain - new insights into function and regulation.Calcium causes a conformational change in lamin A tail domain that promotes farnesyl-mediated membrane association.Detection of mesenchymal stem cells senescence by prelamin A accumulation at the nuclear level.Progeroid syndrome patients with ZMPSTE24 deficiency could benefit when treated with rapamycin and dimethylsulfoxide Broken nuclei--lamins, nuclear mechanics, and disease.Nuclear lamina at the crossroads of the cytoplasm and nucleus.Lamina-associated polypeptide (LAP)2α and nucleoplasmic lamins in adult stem cell regulation and disease.Diverse lamin-dependent mechanisms interact to control chromatin dynamics. Focus on laminopathies Disruption of PCNA-lamins A/C interactions by prelamin A induces DNA replication fork stalling.A truncated lamin A in the Lmna -/- mouse line: implications for the understanding of laminopathies.Blocking farnesylation of the prelamin A variant in Hutchinson-Gilford progeria syndrome alters the distribution of A-type lamins.Aberrant Compartment Formation by HSPB2 Mislocalizes Lamin A and Compromises Nuclear Integrity and Function.Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model.Prelamin A impairs 53BP1 nuclear entry by mislocalizing NUP153 and disrupting the Ran gradient Exploring the Crosstalk Between and Splicing Machinery Gene Mutations in Dilated Cardiomyopathy Comparative proteomic analysis of malignant pleural mesothelioma evidences an altered expression of nuclear lamin and filament-related proteins

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Investigating the purpose of prelamin A processing

http://www.wikidata.org/entity/Q35015891

description

2011 nî lūn-bûn

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2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2011 թվականի հունվարին հրատարակված գիտական հոդված

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2011年の論文

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年学术文章

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2011年學術文章

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name

Investigating the purpose of prelamin A processing

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Investigating the purpose of prelamin A processing

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Investigating the purpose of prelamin A processing

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Investigating the purpose of prelamin A processing

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Investigating the purpose of prelamin A processing

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Investigating the purpose of prelamin A processing

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Brandon Sj Davies

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

Catherine Coffinier

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Hea-Jin Jung

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Loren G Fong

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Richard H Barnes

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Shao H Yang

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

Stephen G Young

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Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy

Structural organization of the human gene encoding nuclear lamin A and nuclear lamin C

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

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

Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy

Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)

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

The A-type lamins: nuclear structural proteins as a focus for muscular dystrophy and cardiovascular diseases

Life at the edge: the nuclear envelope and human disease

The processing pathway of prelamin A

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4-9

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scholarly article

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10.4161/NUCL.13723

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1

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2

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2011-01-01T00:00:00Z

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21647293

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3104803

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