Direct synthesis of lamin A, bypassing prelamin a processing, causes misshapen nuclei in fibroblasts but no detectable pathology in mice. - sprookjes - yvandenbroek - TriplyDB

Direct synthesis of lamin A, bypassing prelamin a processing, causes misshapen nuclei in fibroblasts but no detectable pathology in mice.

Direct synthesis of lamin A, bypassing prelamin a processing, causes misshapen nuclei in fibroblasts but no detectable pathology in mice.

http://www.wikidata.org/entity/Q33966782

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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 Breaching the nuclear envelope in development and disease Mouse models of laminopathies The effect of the lamin A and its mutants on nuclear structure, cell proliferation, protein stability, and mobility in embryonic cells The interaction between nesprins and sun proteins at the nuclear envelope is critical for force transmission between the nucleus and cytoskeleton.Farnesylation of lamin B1 is important for retention of nuclear chromatin during neuronal migration.Nuclear lamins and neurobiology.Chromatin remodeling, DNA damage repair and aging.Absence of progeria-like disease phenotypes in knock-in mice expressing a non-farnesylated version of progerin.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 Investigating the purpose of prelamin A processing An absence of both lamin B1 and lamin B2 in keratinocytes has no effect on cell proliferation or the development of skin and hair.Deficiencies in lamin B1 and lamin B2 cause neurodevelopmental defects and distinct nuclear shape abnormalities in neurons Regulation of prelamin A but not lamin C by miR-9, a brain-specific microRNA.Are B-type lamins essential in all mammalian cells?Understanding the roles of nuclear A- and B-type lamins in brain development.Nuclear lamins in the brain - new insights into function and regulation.Modulation of LMNA splicing as a strategy to treat prelamin A diseases.Nuclear lamin functions and disease.Myopathic lamin mutations impair nuclear stability in cells and tissue and disrupt nucleo-cytoskeletal coupling.Lamin B1 and lamin B2 are long-lived proteins with distinct functions in retinal development.Mass spectrometry captures off-target drug binding and provides mechanistic insights into the human metalloprotease ZMPSTE24.New Lmna knock-in mice provide a molecular mechanism for the 'segmental aging' in Hutchinson-Gilford progeria syndrome.Protein farnesylation and disease.Normal and aberrant splicing of LMNA.Do lamin A and lamin C have unique roles?HypE-specific nanobodies as tools to modulate HypE-mediated target AMPylation.MG132-induced progerin clearance is mediated by autophagy activation and splicing regulation.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.LMNA missense mutations causing familial partial lipodystrophy do not lead to an accumulation of prelamin A.OGT (O-GlcNAc Transferase) Selectively Modifies Multiple Residues Unique to Lamin A.The Pathogenesis and Therapies of Striated Muscle Laminopathies

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P2860

Direct synthesis of lamin A, bypassing prelamin a processing, causes misshapen nuclei in fibroblasts but no detectable pathology in mice.

http://www.wikidata.org/entity/Q33966782

description

2010 nî lūn-bûn

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2010 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2010 թվականի մայիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Direct synthesis of lamin A, b ...... detectable pathology in mice.

@ast

Direct synthesis of lamin A, b ...... detectable pathology in mice.

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type

label

Direct synthesis of lamin A, b ...... detectable pathology in mice.

@ast

Direct synthesis of lamin A, b ...... detectable pathology in mice.

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prefLabel

Direct synthesis of lamin A, b ...... detectable pathology in mice.

@ast

Direct synthesis of lamin A, b ...... detectable pathology in mice.

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JBC.M110.128835

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Journal of Biological Chemistry

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Direct synthesis of lamin A, b ...... detectable pathology in mice.

@en

P2093

Brandon S Davies

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

Catherine Coffinier

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

Chika Nobumori

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Emily A Farber

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Hea-Jin Jung

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

Jan Lammerding

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Javad N Farahani

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Laurent A Bentolila

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

Loren G Fong

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Michael M Weinstein

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P2860

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

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

Laminopathies and the long strange trip from basic cell biology to therapy

The processing pathway of prelamin A

Farnesylated lamins, progeroid syndromes and farnesyl transferase inhibitors

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

Disruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cells

Biochemical studies of Zmpste24-deficient mice

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20818-20826

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44570388

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20439468

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