Quantitative proteomic analysis of dystrophic dog muscle.
about
The biochemical and mass spectrometric profiling of the dystrophin complexome from skeletal muscleDifferential Gene Expression Profiling of Dystrophic Dog Muscle after MuStem Cell TransplantationNovel approach to meta-analysis of microarray datasets reveals muscle remodeling-related drug targets and biomarkers in Duchenne muscular dystrophyApplication of fluorescence two-dimensional difference in-gel electrophoresis as a proteomic biomarker discovery tool in muscular dystrophy researchAffinity proteomics within rare diseases: a BIO-NMD study for blood biomarkers of muscular dystrophiesPharmacologic management of Duchenne muscular dystrophy: target identification and preclinical trialsExploration of lipid metabolism in relation with plasma membrane properties of Duchenne muscular dystrophy cells: influence of L-carnitineQuantitative analysis of proteins of metabolism by reverse phase protein microarrays identifies potential biomarkers of rare neuromuscular diseases.Quantitative proteomic analysis reveals metabolic alterations, calcium dysregulation, and increased expression of extracellular matrix proteins in laminin α2 chain-deficient muscle.Simultaneous Pathoproteomic Evaluation of the Dystrophin-Glycoprotein Complex and Secondary Changes in the mdx-4cv Mouse Model of Duchenne Muscular DystrophyIdentification in GRMD dog muscle of critical miRNAs involved in pathophysiology and effects associated with MuStem cell transplantation.Multi-level omics analysis in a murine model of dystrophin loss and therapeutic restoration.Profiling of age-related changes in the tibialis anterior muscle proteome of the mdx mouse model of dystrophinopathyMetabolic remodeling agents show beneficial effects in the dystrophin-deficient mdx mouse modelSparing of the dystrophin-deficient cranial sartorius muscle is associated with classical and novel hypertrophy pathways in GRMD dogsConcurrent Label-Free Mass Spectrometric Analysis of Dystrophin Isoform Dp427 and the Myofibrosis Marker Collagen in Crude Extracts from mdx-4cv Skeletal Muscles.Circulating Biomarkers for Duchenne Muscular Dystrophy.Proteomic identification of biomarkers of skeletal muscle disorders.Proteomic profiling of the contractile apparatus from skeletal muscle.ROS and RNS signaling in skeletal muscle: critical signals and therapeutic targets.Chaperoning heat shock proteins: proteomic analysis and relevance for normal and dystrophin-deficient muscle.Quantitative proteome profiling of dystrophic dog skeletal muscle reveals a stabilized muscular architecture and protection against oxidative stress after systemic delivery of MuStem cells.Pathoproteomic profiling of the skeletal muscle matrisome in dystrophinopathy associated myofibrosis.Mass spectrometry-based protein analysis to unravel the tissue pathophysiology in Duchenne muscular dystrophy.Progressive muscle proteome changes in a clinically relevant pig model of Duchenne muscular dystrophy.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.Post-natal induction of PGC-1α protects against severe muscle dystrophy independently of utrophin.Elastase levels and activity are increased in dystrophic muscle and impair myoblast cell survival, proliferation and differentiation.Gene expression in mdx mouse muscle in relation to age and exercise: aberrant mechanical-metabolic coupling and implications for pre-clinical studies in Duchenne muscular dystrophy.Proteomic Profiling of the Dystrophin-Deficient Brain.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.Proteomic profiling of muscle fibre type shifting in neuromuscular diseases.Comparative Label-Free Mass Spectrometric Analysis of Mildly versus Severely Affected mdx Mouse Skeletal Muscles Identifies Annexin, Lamin, and Vimentin as Universal Dystrophic Markers.The Isotope-Coded Affinity Tag Method for Quantitative Protein Profile Comparison and Relative Quantitation of Cysteine Redox Modifications.Changes in Muscle Metabolism are Associated with Phenotypic Variability in Golden Retriever Muscular Dystrophy.
P2860
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P2860
Quantitative proteomic analysis of dystrophic dog muscle.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年学术文章
@wuu
2011年学术文章
@zh-cn
2011年学术文章
@zh-hans
2011年学术文章
@zh-my
2011年学术文章
@zh-sg
2011年學術文章
@yue
2011年學術文章
@zh
2011年學術文章
@zh-hant
name
Quantitative proteomic analysis of dystrophic dog muscle.
@en
Quantitative proteomic analysis of dystrophic dog muscle.
@nl
type
label
Quantitative proteomic analysis of dystrophic dog muscle.
@en
Quantitative proteomic analysis of dystrophic dog muscle.
@nl
prefLabel
Quantitative proteomic analysis of dystrophic dog muscle.
@en
Quantitative proteomic analysis of dystrophic dog muscle.
@nl
P2093
P356
P1476
Quantitative proteomic analysis of dystrophic dog muscle
@en
P2093
Carolina Perez-Iratxeta
Jessie R Lavoie
Karl Rouger
Laurence Dubreil
Marie Feron
Marjorie Brand
Sophie Talon
P304
P356
10.1021/PR2001385
P577
2011-03-29T00:00:00Z