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anti-Human Dystrophin Antibodies:
anti-Mouse (Murine) Dystrophin Antibodies:
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Fish Monoclonal Dystrophin Primary Antibody for ICC, IF - ABIN267904
Morris, Ellis, Nguyen: A quantitative ELISA for dystrophin. in Journal of immunological methods 1993
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Human Polyclonal Dystrophin Primary Antibody for ICC, IF - ABIN4306551
Aoyama, Kawase, Bando, Monji, Murohara et al.: Dipeptidyl Peptidase 4 Inhibition Alleviates Shortage of Circulating Glucagon-Like Peptide-1 in Heart Failure and Mitigates Myocardial Remodeling and Apoptosis via the Exchange Protein Directly ... in Circulation. Heart failure 2016
Show all 3 Pubmed References
Chicken Monoclonal Dystrophin Primary Antibody for IHC (p), IHC - ABIN267033
Hosur, Kavirayani, Riefler, Carney, Lyons, Gott, Cox, Shultz: Dystrophin and dysferlin double mutant mice: a novel model for rhabdomyosarcoma. in Cancer genetics 2012
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Ordered disorder of the astrocytic dystrophin-associated protein complex in the norm and pathology.
Forced expression of embryonic dystrophin in zebrafish using an exon-skipping approach severely impairs the mobility and muscle architecture.
Spatio-temporal differences in dystrophin dynamics at mRNA and protein levels have been revealed using a novel reporter system.
Data indicate that ataluren (0.1-1 muM, 3-5 dpf) improved contractile function (~60% improvement of force at 0.5 muM) and dystrophin expression.
early expression of the short carboxyl-terminal dystrophin transcript, with expression of the full length muscle transcript occurring during myogenesis.
Data suggest that dystrophin functions in regulation of calcium signaling during early stages of slow muscle cell differentiation; calcium signaling in these cells coincide with first spontaneous contractions of embryonic trunk.
analysis of the dystrophin associated protein complex in zebrafish
Data suggest that the progressive muscle degeneration phenotype of dystrophin mutant zebrafish embryos is caused by the failure of embryonic muscle end attachments.
Dystrophin family gene expression in zebrafish is reported.
reduction of dystrophin, dystroglycan and sarcoglycan at translational level in embryos with overexpressed myostatin2
Sequence analysis of sapje-like genomic DNA identified a mutation in the donor splice junction at the end of dystrophin exon 62.
Data indicate that skeletal muscles from with a missense mutation in the dystrophin gene is associated with muscle histophatology.
This study suggested thatdystrophins are expressed in the outer plexiform layer, around blood vessels and at the inner limiting membrane as previously described in human and mouse retinae.
This study demonstrated that the DMD alterations identify a subset of progressive/high-grade meningiomas with worse outcomes.
Two fetuses harboring DMD gene deletions but without a family history of Duchenne/Becker muscular dystrophy were discovered
The data suggests hyper-activity of xanthine oxidase in Duchenne muscular dystrophy (DMD), identifies xanthine oxidase activity as a contributing factor in eccentric contraction-induced force drop of dystrophin-deficient skeletal muscle and highlights the potential of isoxanthopterin as a noninvasive biomarker in DMD.
Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids
Three novel splicing mutations were discovered at the 5' end of DMD gene in three muscular dystrophy patients with different disease phenotypes
Dp71-depleted HBE (HBE-Dp71AS) cells displayed increased DNA damage and apoptosis induced by H2O2. Reduced RAD51 mRNA and protein levels, decreased lamin B1, focal adhesion kinase (FAK), phosphorylated focal adhesion kinase (p-FAK) and phosphorylated protein kinase B (p-AKT) were also detected in the HBE-Dp71AS cells.
findings represent an important step toward eventual correction of common Duchenne muscular dystrophy mutations and provide a means of rapidly assessing the expression and function of internally truncated forms of dystrophin-lacking portions of ABD-1
In-frame Deletion in the DMD Gene is associated with Becker muscular dystrophy.
Males amenable to exon 44 (N = 74) and exon 8 skipping (N = 18) showed prolonged ambulation compared to other exon skip groups and nonsense mutations (P = 0.035 and P < 0.01, respectively). In particular, exon 45 deletions were associated with prolonged age at loss of ambulation relative to the rest of the exon 44 skip amenable cohort and other DMD mutations.
Exon skipping induced by the nonsense mutation c.3340A > T in the DMD gene is associated with conversion of a splicing enhancer to a splicing silencer in Duchenne muscular dystrophy.
Systemic Duchenne muscular dystrophy gene therapy has come a long way. Progresses in the fields of virology, immunology, dystrophin biology, animal models, and large-scale clinical grade
confirmation of the reading frame hypothesis helped account for new dystrophin rearrangements in this study. We found that 81% of our Saudi patients would potentially benefit from exon skipping, of which 42.9% had a mutation amenable to skipping of exon 51
structural description of the whole dystrophin central domain we present here is a first necessary step to improve the design of microdystrophin constructs toward the goal of a successful gene therapy for DMD
Case Report: dystrophin mutation (p.1667 del Ala), resulting in Becker muscular dystrophy-associated cardiomyopathy that demonstrated the pathological features of significant fibrofatty replacement in the sub-epicardial layer of the ventricle.
DMD gene mutations involving the hinge 3 region, actin-binding domain, and exons 45-49, as well as the LTBP4 IAAM haplotype, were not associated with age of left ventricular dysfunction onset inDuchenne muscular dystrophy.
we found a new 9358-9359insA mutation of the dystrophy gene in a Chinese boy with muscular dystrophy and his mother
Mutation spectrum analysis of DMD gene causing Duchenne/Becker muscular dystrophy in 68 families in Kuwait has been reported.
Low dystrophin expression is associated with Becker and Duchenne muscular dystrophy.
This study characterize the developmental profile of dystrophin expression across human brain regions to define the temporal profile of astrocytic endfoot development.
A novel small mutation in the first exon-intron boundary splicing site of the DMD gene was found, in a patient with higher serum CK level in his family. This small mutation is responsible for X-linked dilated cardiomyopathy.
Our results provide a proof of principle that SaCas9 could be used to edit the human DMD gene and could be considered for further development of a therapy for DMD.
impaired cortical excitatory/inhibitory balance and executive dysfunctions contribute to the intellectual and behavioral disturbances associated with Dp71 deficiency in Duchenne muscular dystrophy.
It is concluded that that DeltaH2-R15 mini-dystrophin is a superior candidate gene for heart protection. This finding has important implications in the design of the mini/micro-dystrophin gene for Duchenne cardiomyopathy therapy.
The localization of Dp71 at the glial-vascular interface could be associated with supraoptic nucleus (SON) osmosensitivity, leading to an adequate oxytocin synthesis in the SON and release from the NL/HP upon plasmatic hyperosmolality
Allogenic exosomes producing dystrophin may serve as an alternative treatment for cardiomyopathy of Duchenne muscular dystrophy.
This study demonstrates the contribution of Dp427 and utrophin in male fertility, suggesting a potential pathology in DMD patients.
we demonstrated that the Dp71d group of isoforms is highly expressed in the brain, while the Dp71f group predominates in the retina, at both the cDNA and protein levels. These findings suggest that distinct Dp71 isoforms may play different roles in the brain and retina.
Dp71 loss alters cerebellar synapse function and cerebellum-dependent navigation strategies without being detrimental for motor functions.
alpha-DG hypoglycosylation, together with an increased protein instability, reduces the membrane dynamics of the beta-subunit and its clustering within the actin-rich domains, influencing cell migration and spontaneous cell movement.
Influence of full-length dystrophin on brain volumes in mouse models of Duchenne muscular dystrophy
Impaired regenerative capacity and lower revertant fibre expansion in dystrophin-deficient Duchenne muscular dystrophy mouse muscles on DBA/2 background has been reported.
these results provide new insights into the spatial distribution of dystrophin glycoprotein components and their dynamics in living mice.
it is concluded that the LVH with high LVEDWS is associated to a degradation of dystrophin and increase of myocardial stiffness. At least in a murine model these alterations were attenuated after the administration of a matrix metalloprotease inhibitor.
Dystrophin-glycoprotein complex component dystroglycan 1 (Dag1) directly binds to the Hippo pathway effector Yap to inhibit cardiomyocyte proliferation in mice
CRIPSR-mediated genome editing efficiently excised the mutant exon 23 in dystrophic mice, restoring the expression of dystrophin protein expression in dystrophic cardiac muscles to a level approaching 40% and improving myocardial contraction.
We show that strong and specific expression of exogenous Dp71 in Muller cells leads to correct localization of Dp71 protein restoring all protein interactions in order to re-establish a proper functional BRB and retina homeostasis thus preventing retina from oedema.
avoiding vector genome loss after AAV injection by PPMO pre-treatment would allow efficient long-term restoration of dystrophin and the use of lower and thus safer vector doses for Duchenne patients.
To optimize a dystrophin cDNA construct for therapeutic application we designed and produced four human minidystrophins within the packaging capacity of lentiviral vectors. Two novel minidystrophins retained the centrally located neuronal nitric oxide synthase (nNOS)-anchoring domain in order to achieve sarcolemmal nNOS restoration, which is lost in most internally deleted dystrophin constructs.
Our study demonstrates for the first time that low-level dystrophin can partially preserve heart function.
Dys protein regulates tarsal joint formation in response to Notch activity during Drosophila leg development.
The findings suggest that the signaling functions of Dystrophin protein are able to ameliorate dilated cardiomyopathy, and thus might help to improve heart muscle function in micro-Dystrophin-based gene therapy approaches.
Nrk, mbl, capt and Cam genetically interact with dystrophin and/or dystroglycan in the process of axon path-finding in the eye.
only dystroglycan, but not dystrophin deficiency causes myodegeneration induced by energetic stress suggesting that dystroglycan might be a component of the low-energy pathway and act as a transducer of energetic stress in normal and dystrophic muscles
Dystrophin and the Rho GTPase crossveinless-c signaling pathway likely interact at the postsynaptic side of the NMJ to maintain synaptic homeostasis.
3 5' promoters and 3 internal promoters regulate expression of 3 full-length and 3 truncated products, respectively. The existence of this complex gene structure in such evolutionary remote organisms suggests that it has diverse important functions
Lack of the large dystrophin isoforms in the postsynaptic muscle cell leads to elevated evoked neurotransmitter release from presynaptic terminals.
Our results indicate the existence of at least two possibly separate roles of dystrophin in muscle, maintaining synaptic homeostasis and preserving the structural stability of the muscle.
The det locus encodes Drosophila dys, which acts with other components of the DAPC to influence intercellular signalling in developing wing veins.
RNAi-mediated knockdown in the mesoderm shortens lifespan. Deletion of the large isoforms increases the heart rate by widening the cardiac tube and lowering fractional shortening, a phenotype reminiscent of dilated cardiomyopathy
Possibility that Dp186 modulates other non-Gbb/Wit-dependent retrograde signaling pathways required to maintain normal synaptic physiology.
The dystrophin gene is the largest gene found in nature, measuring 2.4 Mb. The gene was identified through a positional cloning approach, targeted at the isolation of the gene responsible for Duchenne (DMD) and Becker (BMD) Muscular Dystrophies. DMD is a recessive, fatal, X-linked disorder occurring at a frequency of about 1 in 3,500 new-born males. BMD is a milder allelic form. In general, DMD patients carry mutations which cause premature translation termination (nonsense or frame shift mutations), while in BMD patients dystrophin is reduced either in molecular weight (derived from in-frame deletions) or in expression level. The dystrophin gene is highly complex, containing at least eight independent, tissue-specific promoters and two polyA-addition sites. Furthermore, dystrophin RNA is differentially spliced, producing a range of different transcripts, encoding a large set of protein isoforms. Dystrophin (as encoded by the Dp427 transcripts) is a large, rod-like cytoskeletal protein which is found at the inner surface of muscle fibers. Dystrophin is part of the dystrophin-glycoprotein complex (DGC), which bridges the inner cytoskeleton (F-actin) and the extra-cellular matrix.
dystrophin (muscular dystrophy, Duchenne and Becker types)
, Duchenne muscular dystrophy
, dystrophin isoform Dp116
, dystrophin Dp71 isoform
, X-linked muscular dystrophy
, dystrophin transcript variant Dp71e
, dystrophin, muscular dystrophy
, Dystrophin-like protein 1
, Dystrophin-like protein 186
, Dystrophin-like protein 2
, Dystrophin-like protein 3
, dystrophin Dp186