Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle - Wikidata - wikimedia - TriplyDB

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

http://www.wikidata.org/entity/Q24615708

about

Calpain 3 is a rapid-action, unidirectional proteolytic switch central to muscle remodeling Ahnak1 abnormally localizes in muscular dystrophies and contributes to muscle vesicle release Ferlins: regulators of vesicle fusion for auditory neurotransmission, receptor trafficking and membrane repair Novel protein-protein interactions inferred from literature context Down-regulation of MyoD by calpain 3 promotes generation of reserve cells in C2C12 myoblasts Comparison of dysferlin expression in human skeletal muscle with that in monocytes for the diagnosis of dysferlin myopathy.Gene expression profiling in limb-girdle muscular dystrophy 2A Calcium-dependent plasma membrane repair requires m- or mu-calpain, but not calpain-3, the proteasome, or caspases.Dysferlin interacts with tubulin and microtubules in mouse skeletal muscle.Proteomic analysis of the dysferlin protein complex unveils its importance for sarcolemmal maintenance and integrity Calpain 3 is important for muscle regeneration: evidence from patients with limb girdle muscular dystrophies.Dystrophin and dysferlin double mutant mice: a novel model for rhabdomyosarcoma Dysferlin and animal models for dysferlinopathy Plasma Membrane Repair: A Central Process for Maintaining Cellular Homeostasis.Impaired regeneration in LGMD2A supported by increased PAX7-positive satellite cell content and muscle-specific microrna dysregulation.Animal models of muscular dystrophy Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance.Attenuated muscle regeneration is a key factor in dysferlin-deficient muscular dystrophy.Mitochondrial abnormalities, energy deficit and oxidative stress are features of calpain 3 deficiency in skeletal muscle Fast-twitch sarcomeric and glycolytic enzyme protein loss in inclusion body myositis.Translational research and therapeutic perspectives in dysferlinopathies.Ferlin proteins in myoblast fusion and muscle growth.Coupling of excitation to Ca2+ release is modulated by dysferlin.Calpain-14 and its association with eosinophilic esophagitis.MicroRNA signatures predict dysregulated vitamin D receptor and calcium pathways status in limb girdle muscle dystrophies (LGMD) 2A/2B.Along signal paths: an empirical gene set approach exploiting pathway topology.AHNAK2 Participates in the Stress-Induced Nonclassical FGF1 Secretion Pathway.Interactions with M-band titin and calpain 3 link myospryn (CMYA5) to tibial and limb-girdle muscular dystrophies Presynaptic calcium channels and α3-integrins are complexed with synaptic cleft laminins, cytoskeletal elements and active zone components.Giant scaffolding protein AHNAK1 interacts with β-dystroglycan and controls motility and mechanical properties of Schwann cells.Calpain activation by hepatitis C virus proteins inhibits the extrinsic apoptotic signaling pathway.Left ventricular deformation abnormalities in a patient with calpainopathy-a case from the three-dimensional speckle-tracking echocardiographic MAGYAR-Path Study.A heterozygous 21-bp deletion in CAPN3 causes dominantly inherited limb girdle muscular dystrophy.Autosomal dominant calpainopathy due to heterozygous CAPN3 c.643_663del21.

P2860

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P2860

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

http://www.wikidata.org/entity/Q24615708

description

2008 nî lūn-bûn

@nan

2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

@ast

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

@en

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

@nl

type

label

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

@ast

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

@en

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

@nl

prefLabel

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

@ast

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

@en

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

@nl

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P1433

Human Molecular Genetics

P1476

Calpain 3 is a modulator of the dysferlin protein complex in skeletal muscle

@en

P2093

Alexandra van Remoortere

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

Antoine de Morrée

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

Johan T den Dunnen

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

Kate Bushby

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

Rune R Frants

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

Yanchao Huang

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

P2860

Myoferlin, a candidate gene and potential modifier of muscular dystrophy

A human gene (AHNAK) encoding an unusually large protein with a 1.2-microns polyionic rod structure

Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A

AHNAK, a novel component of the dysferlin protein complex, redistributes to the cytoplasm with dysferlin during skeletal muscle regeneration

The calpain system

Distal anterior compartment myopathy: a dysferlin mutation causing a new muscular dystrophy phenotype

Defective membrane repair in dysferlin-deficient muscular dystrophy

Calpain 3 cleaves filamin C and regulates its ability to interact with gamma- and delta-sarcoglycans

Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy

A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B

P304

1855-66

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P31

scholarly article

P356

10.1093/HMG/DDN081

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P407

P433

12

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

P478

17

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P50

Silvère M van der Maarel

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2008-06-15T00:00:00Z

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P5875

5516895

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P698

18334579

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P932

2900895

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