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

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

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

http://www.wikidata.org/entity/Q33895774

about

The cell nucleus and aging: tantalizing clues and hopeful promises Molecular ageing in progeroid syndromes: Hutchinson-Gilford progeria syndrome as a model Hutchinson-Gilford progeria mutant lamin A primarily targets human vascular cells as detected by an anti-Lamin A G608G antibody.Progeria: a rare genetic premature ageing disorder Targeting protein prenylation in progeria 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 Model of human aging: recent findings on Werner's and Hutchinson-Gilford progeria syndromes Lamin A-dependent misregulation of adult stem cells associated with accelerated ageing Lamin A-dependent nuclear defects in human aging Molecular insights into the premature aging disease progeria Mouse models of laminopathies The nuclear envelope: an intriguing focal point for neurogenetic disease Analysis of prelamin A biogenesis reveals the nucleus to be a CaaX processing compartment Laminopathies and the long strange trip from basic cell biology to therapy Prelamin A farnesylation and progeroid syndromes Temsirolimus Partially Rescues the Hutchinson-Gilford Progeria Cellular Phenotype Embryonic senescence and laminopathies in a progeroid zebrafish model Interruption of progerin-lamin A/C binding ameliorates Hutchinson-Gilford progeria syndrome phenotype Farnesylated nuclear proteins Kugelkern and lamin Dm0 affect nuclear morphology by directly interacting with the nuclear membrane.Drug screening on Hutchinson Gilford progeria pluripotent stem cells reveals aminopyrimidines as new modulators of farnesylation.Assessing the efficacy of protein farnesyltransferase inhibitors in mouse models of progeria.Lamin A rod domain mutants target heterochromatin protein 1alpha and beta for proteasomal degradation by activation of F-box protein, FBXW10 Dynamics of lamin-A processing following precursor accumulation.Defective lamin A-Rb signaling in Hutchinson-Gilford Progeria Syndrome and reversal by farnesyltransferase inhibition.Nuclear localization signal deletion mutants of lamin A and progerin reveal insights into lamin A processing and emerin targeting Targeting protein prenylation for cancer therapy Diseases of the nuclear envelope.Abnormal development of the cerebral cortex and cerebellum in the setting of lamin B2 deficiency.Genetic studies on the functional relevance of the protein prenyltransferases in skin keratinocytes.The posttranslational processing of prelamin A and disease.A novel approach to tag and identify geranylgeranylated proteins.DNA damage and lamins Impact of farnesylation inhibitors on survival in Hutchinson-Gilford progeria syndrome.An accumulation of non-farnesylated prelamin A causes cardiomyopathy but not progeria.Metformin decreases progerin expression and alleviates pathological defects of Hutchinson-Gilford progeria syndrome cells.Blocking protein farnesyltransferase improves nuclear shape in fibroblasts from humans with progeroid syndromes Therapeutic intervention based on protein prenylation and associated modifications Direct synthesis of lamin A, bypassing prelamin a processing, causes misshapen nuclei in fibroblasts but no detectable pathology in mice.Requirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24.

P2860

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P2860

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

http://www.wikidata.org/entity/Q33895774

description

2005 nî lūn-bûn

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2005 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2005 թվականի հուլիսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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Blocking protein farnesyltrans ...... rd progeria syndrome mutation.

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Blocking protein farnesyltrans ...... rd progeria syndrome mutation.

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Blocking protein farnesyltrans ...... rd progeria syndrome mutation.

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Blocking protein farnesyltrans ...... rd progeria syndrome mutation.

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PNAS.0504641102

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

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Blocking protein farnesyltrans ...... ord progeria syndrome mutation

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Julia I Toth

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Loren G Fong

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Margarita Meta

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Martin O Bergo

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Michael H Gelb

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Pravin Bendale

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Salemiz Sandoval

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Shao H Yang

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Xin Qiao

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Yan Hu

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P2860

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

Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum

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

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

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

Heterozygosity for Lmna deficiency eliminates the progeria-like phenotypes in Zmpste24-deficient mice

Protein farnesyltransferase in embryogenesis, adult homeostasis, and tumor development

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10291-10296

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scholarly article

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10.1073/PNAS.0504641102

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29

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102

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Stephen G. Young

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2005-07-12T00:00:00Z

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7731110

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16014412

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1174929

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