Absence of progeria-like disease phenotypes in knock-in mice expressing a non-farnesylated version of progerin.
about
Targeting protein prenylation in progeriaHuman ZMPSTE24 disease mutations: residual proteolytic activity correlates with disease severityMolecular insights into the premature aging disease progeriaWhen lamins go bad: nuclear structure and diseaseMouse models of laminopathiesPotential therapeutic approaches for modulating expression and accumulation of defective lamin A in laminopathies and age-related diseasesNuclear localization signal deletion mutants of lamin A and progerin reveal insights into lamin A processing and emerin targetingHP1α mediates defective heterochromatin repair and accelerates senescence in Zmpste24-deficient cells.DNA-damage accumulation and replicative arrest in Hutchinson-Gilford progeria syndromeInner nuclear membrane proteins: impact on human disease.Preventing farnesylation of the dynein adaptor Spindly contributes to the mitotic defects caused by farnesyltransferase inhibitors.iTRAQ-based analysis of progerin expression reveals mitochondrial dysfunction, reactive oxygen species accumulation and altered proteostasis.Understanding the roles of nuclear A- and B-type lamins in brain development.Neonatal progeria: increased ratio of progerin to lamin A leads to progeria of the newbornMutant lamin A links prophase to a p53 independent senescence program.Nuclear lamin functions and disease.Efficient use of exogenous isoprenols for protein isoprenylation by MDA-MB-231 cells is regulated independently of the mevalonate pathwayExpression of progerin does not result in an increased mutation rate.Blocking farnesylation of the prelamin A variant in Hutchinson-Gilford progeria syndrome alters the distribution of A-type lamins.Mitotic Dysfunction Associated with Aging Hallmarks.Disruption of lamin B1 and lamin B2 processing and localization by farnesyltransferase inhibitors.Farnesyltransferase inhibitor treatment restores chromosome territory positions and active chromosome dynamics in Hutchinson-Gilford progeria syndrome cells.Identification of novel RNA isoforms of LMNA.Structure and stability of the lamin A tail domain and HGPS mutant.Depleting the methyltransferase Suv39h1 improves DNA repair and extends lifespan in a progeria mouse model.An encouraging progress report on the treatment of progeria and its implications for atherogenesis.LMNA missense mutations causing familial partial lipodystrophy do not lead to an accumulation of prelamin A.
P2860
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P2860
Absence of progeria-like disease phenotypes in knock-in mice expressing a non-farnesylated version of progerin.
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Absence of progeria-like disea ...... nesylated version of progerin.
@ast
Absence of progeria-like disea ...... nesylated version of progerin.
@en
Absence of progeria-like disea ...... nesylated version of progerin.
@nl
type
label
Absence of progeria-like disea ...... nesylated version of progerin.
@ast
Absence of progeria-like disea ...... nesylated version of progerin.
@en
Absence of progeria-like disea ...... nesylated version of progerin.
@nl
prefLabel
Absence of progeria-like disea ...... nesylated version of progerin.
@ast
Absence of progeria-like disea ...... nesylated version of progerin.
@en
Absence of progeria-like disea ...... nesylated version of progerin.
@nl
P2093
P2860
P356
P1476
Absence of progeria-like disea ...... nesylated version of progerin.
@en
P2093
Douglas A Andres
H Peter Spielmann
Loren G Fong
Sandy Y Chang
Shao H Yang
Shuxun Ren
P2860
P304
P356
10.1093/HMG/DDQ490
P577
2010-11-18T00:00:00Z