Accessorizing and anchoring the LINC complex for multifunctionality. - Wikidata - awgldk - TriplyDB

Accessorizing and anchoring the LINC complex for multifunctionality.

Accessorizing and anchoring the LINC complex for multifunctionality.

http://www.wikidata.org/entity/Q34825870

about

Under Pressure: Mechanical Stress Management in the Nucleus Emery-Dreifuss muscular dystrophy: a test case for precision medicine.GIP Contributions to the Regulation of Centromere at the Interface Between the Nuclear Envelope and the Nucleoplasm Nuclear migration events throughout development Implications and Assessment of the Elastic Behavior of Lamins in Laminopathies Nuclear envelope: positioning nuclei and organizing synapses 53BP1 and the LINC Complex Promote Microtubule-Dependent DSB Mobility and DNA Repair Samp1, a RanGTP binding transmembrane protein in the inner nuclear membrane.The Soft- and Hard-Heartedness of Cardiac Fibroblasts: Mechanotransduction Signaling Pathways in Fibrosis of the Heart.Nuclear membrane diversity: underlying tissue-specific pathologies in disease?Cell Microharpooning to Study Nucleo-Cytoskeletal Coupling.The C-Terminal SynMuv/DdDUF926 Domain Regulates the Function of the N-Terminal Domain of DdNKAP.Data on the association of the nuclear envelope protein Sun1 with nucleoli.PML isoform II plays a critical role in nuclear lipid droplet formation.Forces, fluctuations, and self-organization in the nucleus SUN2 Overexpression Deforms Nuclear Shape and Inhibits HIV.Targeting Mitogen-Activated Protein Kinase Signaling in Mouse Models of Cardiomyopathy Caused by Lamin A/C Gene Mutations Squish and squeeze-the nucleus as a physical barrier during migration in confined environments.Nuclear Envelope Retention of LINC Complexes Is Promoted by SUN-1 Oligomerization in the Caenorhabditis elegans Germ Line.Nuclear envelope rupture: Actin fibers are putting the squeeze on the nucleus.Lamin-B1 contributes to the proper timing of epicardial cell migration and function during embryonic heart development.Opposing roles for distinct LINC complexes in regulation of the small GTPase RhoA.Shared mechanisms in physiological and pathological nucleoplasmic reticulum formation Nuclear morphologies: their diversity and functional relevance.Dynamic, mechanical integration between nucleus and cell- where physics meets biology Outer nuclear membrane protein Kuduk modulates the LINC complex and nuclear envelope architecture.Quantitative Brightness Analysis of Protein Oligomerization in the Nuclear Envelope.TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement.Multiple Isoforms of Nesprin1 Are Integral Components of Ciliary Rootlets.The nucleus is a conserved mechanosensation and mechanoresponse organelle.The Malleable Nature of the Budding Yeast Nuclear Envelope: Flares, Fusion, and Fenestrations.Fascin Regulates Nuclear Movement and Deformation in Migrating Cells.An unresolved LINC in the nuclear envelope.Inner nuclear envelope protein SUN1 plays a prominent role in mammalian mRNA export.Cytoskeletal Integrators: The Spectrin Superfamily.Spatial organization of the Schizosaccharomyces pombe genome within the nucleus.The Nuclear Option: Evidence Implicating the Cell Nucleus in Mechanotransduction.Bursting the Bubble - Nuclear Envelope Rupture as a Path to Genomic Instability?Pathways Involved in Formation of Mammary Organoid Architecture Have Keys to Understanding Drug Resistance and to Discovery of Druggable Targets.UNC-84: "LINC-ing" chromosome movement and double strand break repair.

P2860

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P2860

Accessorizing and anchoring the LINC complex for multifunctionality.

http://www.wikidata.org/entity/Q34825870

description

2015 nî lūn-bûn

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2015 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի հունվարին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

@zh-hant

2015年論文

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2015年論文

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2015年論文

@zh-tw

2015年论文

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name

Accessorizing and anchoring the LINC complex for multifunctionality.

@ast

Accessorizing and anchoring the LINC complex for multifunctionality.

@en

Accessorizing and anchoring the LINC complex for multifunctionality.

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type

label

Accessorizing and anchoring the LINC complex for multifunctionality.

@ast

Accessorizing and anchoring the LINC complex for multifunctionality.

@en

Accessorizing and anchoring the LINC complex for multifunctionality.

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prefLabel

Accessorizing and anchoring the LINC complex for multifunctionality.

@ast

Accessorizing and anchoring the LINC complex for multifunctionality.

@en

Accessorizing and anchoring the LINC complex for multifunctionality.

@nl

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Journal of Cell Biology

P1476

Accessorizing and anchoring the LINC complex for multifunctionality.

@en

P2093

Gregg G Gundersen

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

Howard J Worman

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

Wakam Chang

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

P2860

Multiple novel nesprin-1 and nesprin-2 variants act as versatile tissue-specific intracellular scaffolds

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

Syne-1, a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction

Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues

Nesprin-2 is a multi-isomeric protein that binds lamin and emerin at the nuclear envelope and forms a subcellular network in skeletal muscle

Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement.

The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus

Coupling of the nucleus and cytoplasm: role of the LINC complex

Nesprin-1alpha self-associates and binds directly to emerin and lamin A in vitro

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

P304

11-22

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scholarly article

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10.1083/JCB.201409047

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1

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208

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270652706

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25559183

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macromolecular substances

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4284225

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