Subcellular localization of SREBP1 depends on its interaction with the C-terminal region of wild-type and disease related A-type lamins - Wikidata - wikimedia - TriplyDB

Subcellular localization of SREBP1 depends on its interaction with the C-terminal region of wild-type and disease related A-type lamins

Subcellular localization of SREBP1 depends on its interaction with the C-terminal region of wild-type and disease related A-type lamins

http://www.wikidata.org/entity/Q35549134

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Defects of Lipid Synthesis Are Linked to the Age-Dependent Demyelination Caused by Lamin B1 Overexpression N-acetyl-L-cysteine prevents stress-induced desmin aggregation in cellular models of desminopathy Comparative proteome analysis of abdominal adipose tissues between fat and lean broilers.Distinct features of lamin A-interacting chromatin domains mapped by ChIP-sequencing from sonicated or micrococcal nuclease-digested chromatin A Novel Lamin A Mutant Responsible for Congenital Muscular Dystrophy Causes Distinct Abnormalities of the Cell Nucleus.Lamin A tail modification by SUMO1 is disrupted by familial partial lipodystrophy-causing mutations Muscular Dystrophy Mutations Impair the Nuclear Envelope Emerin Self-assembly Properties Partial lipodystrophy with severe insulin resistance and adult progeria Werner syndrome.Role of the nuclear envelope in the pathogenesis of age-related bone loss and osteoporosis.Lamin A/C-promoter interactions specify chromatin state-dependent transcription outcomes.Chrom3D: three-dimensional genome modeling from Hi-C and nuclear lamin-genome contacts.Hutchinson-Gilford progeria syndrome through the lens of transcription.Hutchinson-Gilford Progeria Syndrome: A premature aging disease caused by LMNA gene mutations.Lamin B1 mediated demyelination: Linking Lamins, Lipids and Leukodystrophies.The p.R482W substitution in A-type lamins deregulates SREBP1 activity in Dunnigan-type familial partial lipodystrophy.Itm2a silencing rescues lamin A mediated inhibition of 3T3-L1 adipocyte differentiation.A lipodystrophy-causing lamin A mutant alters conformation and epigenetic regulation of the anti-adipogenic MIR335 locus.Lipodystrophic syndromes due to LMNA mutations: recent developments on biomolecular aspects, pathophysiological hypotheses and therapeutic perspectives.

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Subcellular localization of SREBP1 depends on its interaction with the C-terminal region of wild-type and disease related A-type lamins

http://www.wikidata.org/entity/Q35549134

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2011 nî lūn-bûn

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2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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Subcellular localization of SR ...... disease related A-type lamins

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Subcellular localization of SR ...... disease related A-type lamins

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Subcellular localization of SR ...... disease related A-type lamins

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Subcellular localization of SR ...... disease related A-type lamins

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Subcellular localization of SR ...... disease related A-type lamins

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Subcellular localization of SR ...... disease related A-type lamins

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J.YEXCR.2011.09.012

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Experimental Cell Research

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Subcellular localization of SR ...... disease related A-type lamins

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Aurélie Gombault

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Brigitte Buendia

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Carine Tellier-Lebègue

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Cecilia Ostlund

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Constantin T Craescu

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Emilie Kondé

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Howard J Worman

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Isabelle Duband-Goulet

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Nathalie Vadrot

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Pascal Roussel

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P2860

Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells

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

Loss of a DNA binding site within the tail of prelamin A contributes to altered heterochromatin anchorage by progerin

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

Phenotype and course of Hutchinson-Gilford progeria syndrome

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Structure of the globular tail of nuclear lamin

The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy

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

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2800-2813

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10.1016/J.YEXCR.2011.09.012

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