Hutchinson-Gilford progeria mutant lamin A primarily targets human vascular cells as detected by an anti-Lamin A G608G antibody. - Test2 - elhamkhani - TriplyDB

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

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

http://www.wikidata.org/entity/Q24541467

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The mutant form of lamin A that causes Hutchinson-Gilford progeria is a biomarker of cellular aging in human skin Blocking protein farnesylation improves nuclear shape abnormalities in keratinocytes of mice expressing the prelamin A variant in Hutchinson-Gilford progeria syndrome Progerin and telomere dysfunction collaborate to trigger cellular senescence in normal human fibroblasts Skeletal Muscle Laminopathies: A Review of Clinical and Molecular Features Nuclear lamins and oxidative stress in cell proliferation and longevity Autophagy: an adaptive physiological countermeasure to cellular senescence and ischaemia/reperfusion-associated cardiac arrhythmias Temsirolimus Partially Rescues the Hutchinson-Gilford Progeria Cellular Phenotype A progeria mutation reveals functions for lamin A in nuclear assembly, architecture, and chromosome organization.Nuclear export of the rate-limiting enzyme in phosphatidylcholine synthesis is mediated by its membrane binding domain.Defective lamin A-Rb signaling in Hutchinson-Gilford Progeria Syndrome and reversal by farnesyltransferase inhibition.Identification of new autoantibody specificities directed at proteins involved in the transforming growth factor β pathway in patients with systemic sclerosis Conserved cysteine residues in the mammalian lamin A tail are essential for cellular responses to ROS generation.Clinical trial of a farnesyltransferase inhibitor in children with Hutchinson-Gilford progeria syndrome.Nuclear lamins.Functional coupling between the extracellular matrix and nuclear lamina by Wnt signaling in progeria.Maintenance of a functional higher order chromatin structure: The role of the nuclear matrix in normal and disease states.Cardiovascular pathology in Hutchinson-Gilford progeria: correlation with the vascular pathology of aging.A prospective study of radiographic manifestations in Hutchinson-Gilford progeria syndrome The role of chromatin structure in cell migration Mutant nuclear lamin A leads to progressive alterations of epigenetic control in premature aging.Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin Recapitulation of premature ageing with iPSCs from Hutchinson-Gilford progeria syndrome Sulforaphane enhances progerin clearance in Hutchinson-Gilford progeria fibroblasts.Identification of target antigens of anti-endothelial cell and anti-vascular smooth muscle cell antibodies in patients with giant cell arteritis: a proteomic approach Mechanisms of premature vascular aging in children with Hutchinson-Gilford progeria syndrome.The role of nuclear lamin B1 in cell proliferation and senescence.A lamin A protein isoform overexpressed in Hutchinson-Gilford progeria syndrome interferes with mitosis in progeria and normal cells.Mislocalization of prelamin A Tyr646Phe mutant to the nuclear pore complex in human embryonic kidney 293 cells.Proliferation of progeria cells is enhanced by lamina-associated polypeptide 2α (LAP2α) through expression of extracellular matrix proteins Mutant lamin A links prophase to a p53 independent senescence program.Loss of H3K9me3 Correlates with ATM Activation and Histone H2AX Phosphorylation Deficiencies in Hutchinson-Gilford Progeria Syndrome Telomerase Therapy to Reverse Cardiovascular Senescence.Structural organization of nuclear lamins A, C, B1, and B2 revealed by superresolution microscopy.Permanent farnesylation of lamin A mutants linked to progeria impairs its phosphorylation at serine 22 during interphase Truncated prelamin A expression in HGPS-like patients: a transcriptional study.Hypercholesterolemia potentiates aortic endothelial response to inhaled diesel exhaust Increased mechanosensitivity and nuclear stiffness in Hutchinson-Gilford progeria cells: effects of farnesyltransferase inhibitors Redistribution of the Lamin B1 genomic binding profile affects rearrangement of heterochromatic domains and SAHF formation during senescence.Management of multicellular senescence and oxidative stress.Adult stem cell maintenance and tissue regeneration in the ageing context: the role for A-type lamins as intrinsic modulators of ageing in adult stem cells and their niches.

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P2860

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

http://www.wikidata.org/entity/Q24541467

description

2006 nî lūn-bûn

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2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի փետրվարին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Hutchinson-Gilford progeria mu ...... an anti-Lamin A G608G antibody

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Hutchinson-Gilford progeria mu ...... n anti-Lamin A G608G antibody.

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Hutchinson-Gilford progeria mu ...... n anti-Lamin A G608G antibody.

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type

label

Hutchinson-Gilford progeria mu ...... an anti-Lamin A G608G antibody

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Hutchinson-Gilford progeria mu ...... n anti-Lamin A G608G antibody.

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Hutchinson-Gilford progeria mu ...... n anti-Lamin A G608G antibody.

@en

prefLabel

Hutchinson-Gilford progeria mu ...... an anti-Lamin A G608G antibody

@nl

Hutchinson-Gilford progeria mu ...... n anti-Lamin A G608G antibody.

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Hutchinson-Gilford progeria mu ...... n anti-Lamin A G608G antibody.

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P1433

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PNAS.0511133103

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Proceedings of the National Academy of Sciences of the United States of America

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Hutchinson-Gilford progeria mu ...... n anti-Lamin A G608G antibody.

@en

P2093

Dayle McClintock

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Karima Djabali

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Leslie B Gordon

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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

Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy

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

Reversal of the cellular phenotype in the premature aging disease Hutchinson-Gilford progeria syndrome

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

A biomarker that identifies senescent human cells in culture and in aging skin in vivo

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

Life at the edge: the nuclear envelope and human disease

Intermediate filaments: structure, dynamics, function, and disease

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

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2154-2159

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scholarly article

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1725017

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10.1073/PNAS.0511133103

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103

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7312224

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16461887

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1413759

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