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DES encodes a muscle-specific class III intermediate filament. Additionally we are shipping Desmin Antibodies (393) and Desmin Kits (54) and many more products for this protein.
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Desmin intermediate filaments are required for normal active force generation.
Desmin distribution during muscle maturation changes from dispersed aggregates to a perinuclear concentration to striated (show NSDHL Proteins) afterwards.
Increasing desmin abnormalities were correlated with diastolic dysfunction progression.
expression level of mutant versus wild-type desmin in mouse model as well as in skeletal muscle specimens derived from human R350P desminopathies; findings demonstrate missense-mutant desmin inflicts changes of the subcellular localization and turnover of desmin itself and of direct desmin-binding partners
Results propose that the mutations affect desmin structure and cause its aberrant folding and subsequent aggregation, triggering disruption of myofibrils organization.
identified disruption of the desmin system in gastrocnemius myofibers as an index of the myopathy and limitation of muscle function in patients with peripheral artery disease.
The desmin intermediate filament network plays a major role in striated (show NSDHL Proteins) muscle development and maintenance by integrating and coordinating most cellular components necessary for proper mechanochemical signaling, organelle cross-talk, energy production and trafficking processes required for proper tissue homeostasis. [Review]
Data suggest that loss of the desmin-p. A120D filament localization at the intercalated disk indicates its clinical arrhythmogenic potential.
we describe a new mutation located in the coiled 1B domain of desmin and associated with a predominant cardiac involvement and a high degree of cardiac sudden death in a large Indian pedigree with 12 affected members
Perfomed proteomic analysis on a transgenic mouse model of severe cardiac hypertrophy; compared data to dataset of heart failure found MYH7 (show MYH7 Proteins), IGFBP7 (show IGFBP7 Proteins), ANXA2 (show ANXA2 Proteins), and DESM to be biomarker candidates for heart failure.
autosomal recessive mutations in DES cause LGMD2 (show CAPN3 Proteins) phenotype without features of myofibrillar myopathy.
Data suggest that for some filament-forming desmin mutants, the molecular etiology of desminopathy results from subtle deficiencies in their association with nebulin, a major actin-binding filament protein of striated (show NSDHL Proteins) muscle.
E413K mutation induces desmin network disorganization, desmin aggregate formation and alters the traction forces generation of single myoblasts.
This study identifies desmin as a new Asb2b target for proteasomal degradation in cardiomyocytes and suggests that accumulation of desmin could contribute to UPS impairment in Hypertrophic cardiomyopathy mice and patients
found that inhibition of the Rac1 pathway (a G protein signaling pathway involved in diverse cellular processes), antioxidant treatment, and stimulation of macroautophagy reduced desmin aggregation by up to 75% in this model
This demonstration of biomechanical integration by the desmin intermediate filament system suggests that it plays an active biological role in muscle in addition to its accepted structural role
Disruption of both nesprin 1 and desmin results in decreased lifespan, body weight and muscle strength.
Desmin content and transversal stiffness of the left ventricle mouse cardiomyocytes and skeletal muscle fibers after a 30-day space flight on board "BION-M1" biosatellite
the observed decline in [Ca(2 (show CA2 Proteins)+)]mit was due to desmin aggregate accumulation resulting in the loss of desmin mitochondria interactions
During fasting, desmin phosphorylation increases and enhances Trim32 (show TRIM32 Proteins)-mediated degradation of the desmin cytoskeleton, which appears to facilitate the breakdown of Z-bands and thin filaments.
Results show that expression of desmin increased during the late fattening stage of of hanwoo steers and it contributes to the muscle contractile apparatus.
This gene encodes a muscle-specific class III intermediate filament. Homopolymers of this protein form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. Mutations in this gene are associated with desmin-related myopathy, a familial cardiac and skeletal myopathy (CSM), and with distal myopathies.
, desmin, gene 1
, intermediate filament protein
, muscle-specific intermediate filament desmin