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anti-Human DMPK Antibodies:
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Cow (Bovine) Polyclonal DMPK Primary Antibody for IHC, WB - ABIN2775281
Ramasamy, Ren, Mench, Regan: Impact of initial biofilm growth on the anode impedance of microbial fuel cells. in Biotechnology and bioengineering 2008
Show all 2 Pubmed References
Variant repeats might explain a part of the phenotypic variability in a small percent of myotonic dystrophy type 1 patients and likely display a stabilizing effect on the meiotic instability of DMPK expanded alleles
Haplotype analysis using various polymorphic-markers in proximity to DMPK gene indicates that a single founder mutation originates myotonic dystrophy type 1 in Mexico; however, Y-STR (show STATH Antibodies) haplogroups data and the presence of pre-mutated and large normal alleles in Amerindians support the hypothesis that both European and Amerindian ancestral chromosomes might have introduced the disease to the Mexican population.
Patients with myotonic dystrophy type 1 (DM1) may have a slight decrease in renal function that cannot be explained by a higher occurrence of risk factors for renal failure such as diabetes, hypertension or age. In addition, there was no correlation between CTG repeats, a marker of disease severity, and renal function.
Interruptions within the DMPK expanded alleles could also interfere with the chromatin structure, the transcriptional activity of the Myotonic dystrophy type 1 (DM1) locus and the interaction with RNA CUG-binding proteins
A second point is that DM mutations, although located in noncoding regions, may reduce the expression of mutant alleles, raising questions whether loss-of-function may contribute to the phenotype, or possibly impose a safety limit on knockdown therapies that create or aggravate a DMPK or CNBP (show CNBP Antibodies) deficiency state
The patients with DM1 nucleotide expansion (CTG) mutation showed widespread abnormalities of all DTI parameters in the white matter, which were associated with reduced gray matter volume in all brain lobes and thinning in parieto-temporo-occipital cortices.
Our work suggests that DM1 patients are at risk for Fuchs' endothelial corneal dystrophy (FECD (show COL8a2 Antibodies)). DMPK mutations contribute to the genetic burden of FECD (show COL8a2 Antibodies) but are uncommon. We establish a connection between two repeat expansion disorders converging upon RNA-MBNL1 (show MBNL1 Antibodies) foci and FECD (show COL8a2 Antibodies).
findings thus suggest that nuclear retention may be a common feature of regulation of DMPK RNA expression. The typical forced nuclear residence of expanded DMPK transcripts affects this regulation in tissues of DM1 patients, but not through hyperadenylation.
Data, including data from studies on synthetic RNA modeling RNA repeat expansions found in patients with Huntington's disease (mRNA for exon 1 of Huntingtin (show HTT Antibodies) protein) and myotonic dystrophy type 1 (mRNA for 3prime untranslated region of dystrophia myotonica-protein kinase), suggest internal loops of r(3xCAG) are stabilized by one-hydrogen bond AA pairs, while those of r(3xCUG) prefer one- or two-hydrogen bond UU pairs.
Analysis of five intergenerational transmissions revealed a substantial intrafamilial stability of the DM1 mutation among relatives.
Our results support the feasibility and safety of using antisense oligonucleotides for post-transcriptional silencing of DMPK in muscle and heart.
Sense DMPK RNA foci clearly co-localize with MBNL1 (show MBNL1 Antibodies) and MBNL2 (show MBNL2 Antibodies) proteins and accumulate in myotonic dystrophy 1 tissues during development.
The data of this study demonstrated that DMPK knockout mice present altered beta-agonist-induced responses and suggest that this is due, at least in part, to a reduced density of beta(1)-adrenergic receptors in cardiac plasma membranes.
Cytosolic DMPK participates in remodeling of the actomyosin cytoskeleton in developing skeletal muscle cells.
Muscleblind1, but not Dmpk or Six5, contributes to a complex phenotype of muscular and motivational deficits in mouse models of myotonic dystrophy
a tail-anchored myotonic dystrophy protein kinase isoform induces perinuclear clustering of mitochondria, autophagy, and apoptosis
Dmpk deficiency results in a sodium (Na) channel abnormality comprising frequent, long bursts of Na channel reopenings during sustained depolarization resulting in a plateau of non-inactivating late Na current.
DMPK has a modulatory role in the control of intracellular Ca2 (show CA2 Antibodies)+ concentration in mouse ventricular cardiomyocytes, loss of which contributes to cardiac dysfunction in myotonic dystrophy.
role for DMPK in synaptic plasticity that could be relevant to the cognitive dysfunction associated with myotonic dystrophy
DMPK isoforms have cell-type and location dependent substrate specificities with a role in organellar and cytoarchitectural dynamics
The protein encoded by this gene is a serine-threonine kinase that is closely related to other kinases that interact with members of the Rho family of small GTPases. Substrates for this enzyme include myogenin, the beta-subunit of the L-type calcium channels, and phospholemman. The 3' untranslated region of this gene contains 5-37 copies of a CTG trinucleotide repeat. Expansion of this unstable motif to 50-5,000 copies causes myotonic dystrophy type I, which increases in severity with increasing repeat element copy number. Repeat expansion is associated with condensation of local chromatin structure that disrupts the expression of genes in this region. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.
dystrophia myotonica-protein kinase
, myotonic dystrophy protein kinase
, myotonin-protein kinase-like
, DM protein kinase
, DM1 protein kinase
, myotonic dystrophy associated protein kinase
, myotonin protein kinase A
, myotonin-protein kinase
, thymopoietin homolog
, dystrophia myotonica kinase, B15