Use your antibodies-online credentials, if available.
Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher toutes les espèces
Afficher tous les synonymes
Sélectionnez vos espèces et l'application
anti-Rat (Rattus) Anticorps:
anti-Mouse (Murine) Anticorps:
Vous arrivez à notre recherche pré-filtrée.
results demonstrate that blocking doppel can control VEGF signaling in TECs and selectively inhibit tumor angiogenesis.
The association between the APOE, CYP46, PRNP and PRND genes and the profile of neuropsychiatric symptoms in Polish subjects with Alzheimer's disease and mild cognitive impairment, was evaluated.
in astrocytomas, Dpl undergoes different molecular processes that might constitute additional helpful tools to characterize the glial tumor progression
Cytotoxicity induced by the expression of Dpl and truncated PrP in neural derived cells are closely related with the apoptosis process.
expression pattern and biochemical characteristics in human tissues and in Chinese hamster ovary cells transfected with wild-type or variant human Dpl gene constructs
Doppel expression is not modified in the brains of patients with Creutzfeldt-Jakob disease.
human Doppel fails to interact with itself; Dpl and PrP are not related or are only marginally related with respect to their ligand binding behaviour
results demonstrate that Doppel and PrPc co-patch extensively at the plasma membrane
Doppel interacts with the full-length laminin receptor precursor protein
Doppel is expressed early during ontogenesis, and is found in both germ cells and Sertoli cells. Doppel may play a physiological role in acrosome biogenesis.
Dpl interacts with RACK1 by means of its structured globular carboxyl-terminal region
Extensive differences in PRND gene expression were also found within each grade of malignancy, suggesting that PRND mRNA quantitation might be useful to distinguish astrocytoma subtypes.
Study provides the foundation for further study of Dpl biological functions in vitro and in vivo.
Results might suggest a potential and functional role for Dpl in tumor cells migratory and morphological behaviours and address to future gene-targeted therapeutic interventions.
results suggested that the function of Dpl is antagonistic to PrP rather than synergistic
From the logistic regression ananlsis of this stidy showed that the highest risk for was found for Alzheimer's disease individuals who co-inherited APOE epsilon4 allele, PRNP codon 129 homozygosity, PRND codon 174 Thr allele, and CYP46 rs754203 g allele.
Disparate Modes of Evolution Shaped Modern Prion (PRNP) and Prion-Related Doppel (PRND) Variation in Domestic Cattle
Results showed that the region -323/+32 (+1 is the transcription start site) represents the promoter region and contains positive cis-acting elements
the genomic structure of three genes, PRNP, PRND, and RASSF2, within the syntenic region of the bovine genome is highly conserved in order and orientation.
in GC-1 spg cells, phosphorylation of p21 and N-terminal truncated PrP may play roles in the control of Dpl-induced apoptosis, which may benefit the physiological function of Dpl in the male reproduction system.
Data suggest that glycosylation status of the prion protein and yet-to-be-identified proteases modulate internal C1 and C2 endoproteolysis of Doppel (doppelganger prion) and Shadoo (shadow of prion protein) in mouse neurons.
Data on residue secondary structure propensities suggest that novel beta-sheets of doppel protein (Prnd) and prion protein (Prnp) are formed by amino acids belonging to helices that are the least stable in the respective native structures.
This finding identifies a protein domain that plays a role in mediating Dpl-related toxicity.
Findings raise the possibility that Bax and caspase-3 feature in Dpl-mediated apoptosis.
These results indicated that Dpl was glycosylated in a cell type- and tissue-specific manner regardless of PrP(C), while PrP(C) endoproteolysis was modulated by Dpl expression.
ectopic expression of PrP-like protein Doppel in central neurons induces significant Purkinje cell death resulting in late-onset ataxia
We suggest a mechanism for Doppel-mediated Purkinje cell degeneration linked to reduced gene expression of proteins related to neuronal activity.
interaction between Dpl and PrPC occurs in lipid rafts and is dependent on the integrity of these membrane microdomains
Expression of doppel in the CNS of mice does not modulate transmissible spongiform encephalopathy disease
Ectopic PrPLP/Dpl in the absence of PRNP is actively involved in the glial-cell activation in the brain.
Differences between the prion protein and its homolog Doppel: a partially structured state with implications for scrapie formation
absence causes male sterility
tested whether Doppel and PrP(C) share the same cell location, thereby sharing the same neighboring cell components, probably required to share the same cell function
Prion and doppel proteins bind to granule cells of the cerebellum, suggesting a scenario in which granule cells express a protein that mediates Dpl-induced neurodegeneration.
Dpl protein binds copper, which may serve to modulate the activity, stability, or localization of the Dpl protein
Doppel expression is not modified in scrapie-infected cells.
findings provide evidence that the N-terminal residues 23-88 of prion protein containing the unique octapeptide-repeat region is crucial for preventing Purkinje cell death in PrP deficient mice expressing Doppel in the neuron
The mechanism of toxicity involved stimulation of nitric oxide production via activation of the nitric oxide synthases, nNOS and iNOS.
transgenic mice selectively expressing Dpl in Purkinje cells showed ataxia and Purkinje cell loss that depended on the level of Dpl expression
This gene is found on chromosome 20, approximately 20 kbp downstream of the gene encoding cellular prion protein, to which it is biochemically and structurally similar. The protein encoded by this gene is a membrane glycosylphosphatidylinositol-anchored glycoprotein that is found predominantly in testis. Mutations in this gene may lead to neurological disorders.
prion protein 2 (dublet)
, prion-like protein doppel
, prion gene complex, downstream
, prion protein dublet
, prion protein-like protein
, prion protein-like protein, doppel