Chaperoning heat shock proteins: proteomic analysis and relevance for normal and dystrophin-deficient muscle.
about
The biochemical and mass spectrometric profiling of the dystrophin complexome from skeletal muscleThe Human Skeletal Muscle Proteome Project: a reappraisal of the current literatureSize dependent classification of heat shock proteins: a mini-review204th ENMC International Workshop on Biomarkers in Duchenne Muscular Dystrophy 24-26 January 2014, Naarden, The NetherlandsAbsence of Dystrophin Disrupts Skeletal Muscle Signaling: Roles of Ca2+, Reactive Oxygen Species, and Nitric Oxide in the Development of Muscular Dystrophy.Concurrent Label-Free Mass Spectrometric Analysis of Dystrophin Isoform Dp427 and the Myofibrosis Marker Collagen in Crude Extracts from mdx-4cv Skeletal Muscles.Pathoproteomic profiling of the skeletal muscle matrisome in dystrophinopathy associated myofibrosis.Expression times for hsp27 and hsp70 as an indicator of thermal stress during death due to fire.Understanding the molecular consequences of inherited muscular dystrophies: advancements through proteomic experimentation.Label-free mass spectrometric analysis of the mdx-4cv diaphragm identifies the matricellular protein periostin as a potential factor involved in dystrophinopathy-related fibrosis.Comparative mass spectrometric and immunoassay-based proteome analysis in serum of Duchenne muscular dystrophy patients.Translocation of molecular chaperones to the titin springs is common in skeletal myopathy patients and affects sarcomere function.Modulation of Protein Quality Control and Proteasome to Autophagy Switch in Immortalized Myoblasts from Duchenne Muscular Dystrophy Patients.Proteomic profiling of the dystrophin complex and membrane fraction from dystrophic mdx muscle reveals decreases in the cytolinker desmoglein and increases in the extracellular matrix stabilizers biglycan and fibronectin.The Work of Titin Protein Folding as a Major Driver in Muscle Contraction.Comparative Label-Free Mass Spectrometric Analysis of Mildly versus Severely Affected mdx Mouse Skeletal Muscles Identifies Annexin, Lamin, and Vimentin as Universal Dystrophic Markers.
P2860
Q26770343-CF2D9EE7-0184-4157-9305-595BD7CB8607Q28068399-DFAE34A6-7ED0-4FA0-9B07-05F16E5E7A1AQ28079450-AE8BC325-F594-4DD4-B936-36385746AD7CQ28611318-94B50C8E-EBF0-4E57-BAA7-CBCC486F5FEBQ36422465-CCAE4718-FB4C-4A1A-94AB-5C373968E5D4Q37566483-E3EC6623-CD53-4192-B3D6-2B7F709FAF15Q38563300-EF47AF00-6538-4579-B0E6-907515DB3A32Q38753837-45BF9073-C773-4760-BD48-38C0F2FC136EQ38850056-15FE0AFF-215D-4E22-A4D1-8BEC07F75ACDQ39033229-AF557C70-62F4-454E-9993-1D7237557A97Q40198410-FE28A5B3-3393-4DFC-89CC-DD657D5507EDQ41710937-310977AD-AB7B-4AFE-8764-B0A45F6717AFQ47216956-7C734B31-E53B-4C0C-A4C2-3E7C6B98884CQ47959546-066F248C-9F07-49BB-86B9-2BA24436C3A9Q50058195-F9A71556-37AD-4BE4-B41C-5646EC259140Q53457776-422CBE89-58BD-456C-8094-0D8D9313C8A4
P2860
Chaperoning heat shock proteins: proteomic analysis and relevance for normal and dystrophin-deficient muscle.
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Chaperoning heat shock protein ...... d dystrophin-deficient muscle.
@en
type
label
Chaperoning heat shock protein ...... d dystrophin-deficient muscle.
@en
prefLabel
Chaperoning heat shock protein ...... d dystrophin-deficient muscle.
@en
P2860
P356
P1476
Chaperoning heat shock protein ...... nd dystrophin-deficient muscle
@en
P2093
Heinrich Brinkmeier
P2860
P304
P356
10.1002/PRCA.201400015
P577
2014-08-28T00:00:00Z