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Different Dvl (show DVL2 Proteins) proteins (Dvl1, Dvl2 (show DVL2 Proteins), Dvl3 (show DVL3 Proteins)) and the composition of dishevelled (show DVL2 Proteins)-beta-arrestin protein complexes contribute to the specific activation of individual branches of Wnt (show WNT2 Proteins) signaling in Xenopus gastrulation.
Authors conclude that the planar cell polarity (PCP (show PRCP Proteins)) pathway contributes significantly to the motility and hence the invasiveness of glioblastoma multiforme (GBM) cells, and that Nrdp1 (show RNF41 Proteins) acts as a negative regulator of PCP (show PRCP Proteins) signaling by inhibiting Dvl (show DVL2 Proteins) through a novel polyubiquitination mechanism.
The DEP domain of Dishevelled (show DVL2 Proteins) undergoes a conformational switch, from monomeric to swapped dimer, to trigger DIX domain-dependent polymerization and signaling to beta-catenin (show CTNNB1 Proteins).
two mutually exclusive functions of the DEP domain in Wnt (show WNT2 Proteins) signal transduction - binding to Frizzled to recruit Dishevelled (show DVL2 Proteins) to the receptor complex, is reported.
we show that Wnt5a (show WNT5A Proteins) rapidly represses rDNA gene transcription in breast cancer cells and generates a chromatin state with reduced transcription of rDNA by RNA polymerase I (show POLR1C Proteins) (Pol I). These effects were specifically dependent on Dishevelled1 (DVL1), which accumulates in nucleolar organizer regions (NORs) and binds to rDNA regions of the chromosome.
Data show that dishevelled (show DVL2 Proteins) proteins DVL1, 2 and 3 were exclusively expressed in chronic lymphatic leukaemia (CLL) cells as compared to normal peripheral blood mononuclear cells (PBMCs).
The secreted frizzled-related protein (show SFRP2 Proteins) and disheveled protein family members appear to be actively involved in the pathogenesis of primary testicular germ cell tumors.
Data show that receptor for activated C kinase 1 (RACK1 (show GNB2L1 Proteins)) interacts with Dishevelled (Dvl (show DVL2 Proteins)) proteins and promotes their lysosomal degradation, and this effect is enhanced by autophagy induction.
TMEM88 stimulated triple negative breast cancer cell invasion by interacting with DVLl.
Specific -1 frameshift variants in the penultimate exon of DVL1 cause autosomal-dominant Robinow syndrome.
Results show that coexpression of IQGAP1 and Dvl (show DVL2 Proteins) in the cytoplasm and nucleus was correlated with the lymph nodal metastase and poor prognosis of non-small cell lung cancer.
Data show that the peptide binding pocket of the Dishevelled 1 (Dvl1) PDZ domain is stabilized upon CXXC finger 5 protein (CXXC5 (show CXXC5 Proteins)) binding.
Here we show that the peptide-binding pocket of the Dvl PDZ domain can be occupied by Dvl's own highly conserved C-terminus, inducing a closed conformation.
The interaction of Dvl1 with Syt-1 (show SYT1 Proteins), which is regulated by Wnts, modulates neurotransmitter release.
findings indicate that Dvl-1 may be an underlying participant of oxidative stress induced (show SQSTM1 Proteins) by selenium deficiency
These results support a novel cell-autonomous postsynaptic role for Dact1 (show DACT1 Proteins), in cooperation with Dishevelled-1 and possibly Disrupted in Schizophrenia-1 (show DISC1 Proteins), in the formation of synapses on cortical interneuron dendrites.
we show that Dvl-1 expression is restricted to OSNs in the dorsal recess of the nasal cavity, and labels a unique subpopulation of glomeruli. Dvl-2 (show DVL2 Proteins) and Dvl-3 (show DVL3 Proteins) have a widespread distribution in both the olfactory epithelium and olfactory bulb .
Fuzzy appears to control subcellular localization of the core PCP (show BMP1 Proteins) protein Dishevelled (show DVL2 Proteins), recruiting it to Rab8 (show RAB8A Proteins)-positive vesicles and to the basal body and cilium. We show that loss of Fuzzy results in inhibition of PCP (show BMP1 Proteins) signaling
A Wnt5a--> Dvl PCP signaling cascade may regulate actin polymerization and protrusive cell behavior in the caudal splanchnic mesoderm to promote second heart field deployment, outflow tract lengthening and cardiac looping.
Findings indicate that Daple interacts with Dishevelled (show DVL2 Proteins) to direct the Dishevelled (show DVL2 Proteins)/protein kinase (show CDK7 Proteins) lambda protein complex to activate Rac (show AKT1 Proteins), which in turn mediates the non-canonical Wnt (show WNT2 Proteins) signalling pathway required for cell migration.
The antagonistic functions of Vangl2 (show VANGL2 Proteins) and Dvl1 allow sharpening of planar cell polarity signaling locally on the tips of the filopodia to sense directional cues, Wnts, eventually causing turning of growth cones.
DVL1, the human homolog of the Drosophila dishevelled gene (dsh) encodes a cytoplasmic phosphoprotein that regulates cell proliferation, acting as a transducer molecule for developmental processes, including segmentation and neuroblast specification. DVL1 is a candidate gene for neuroblastomatous transformation. The Schwartz-Jampel syndrome and Charcot-Marie-Tooth disease type 2A have been mapped to the same region as DVL1. The phenotypes of these diseases may be consistent with defects which might be expected from aberrant expression of a DVL gene during development.
dishevelled, dsh homolog 1
, DSH homolog 1
, dishevelled 1
, segment polarity protein dishevelled homolog DVL-1
, dishevelled 1 (homologous to Drosophila dsh)
, dishevelled, dsh homolog 2, like