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Results demonstrate a novel mechanism of neuronal death and predict that inhibition of NP1 expression is a promising strategy to prevent hypoxic-ischemic injury in immature brain
results demonstrate that extracellular release of NP1 promote hypoxic-ischemic neuronal death possibly via surface clustering with GluR1 (show GRIA1 Proteins) at synaptic sites and that NP1, not its family member NP2 (show NRP2 Proteins), is involved in the neuronal death mechanisms
Genetic deletion of NP1 prevents hypoxic-ischemic neuronal death by reducing synaptic clustering of GluR1 (show GRIA1 Proteins).
These findings suggest that Narp (show NPTX2 Proteins) in the mPFC mediates the extinction of morphine conditioned place preference.
our findings demonstrate a novel mechanism by which NP1 regulates mitochondria-driven hippocampal cell death
NP1 facilitates the accumulation of BCL2-associated X protein (BAX (show BAX Proteins)) in mitochondria and regulates mitochondrial dynamics during apoptosis in mouse cerebellar granule neurons in culture.
Neuronal pentraxin 1 induction in hypoxic-ischemic neuronal death is regulated via a glycogen synthase kinase-3alpha/beta dependent mechanism
data indicate that the loss of NP1/2 disrupts several aspects of retinogeniculate development including the initial establishment of AMPAR transmission and the subsequent elimination of inappropriate circuit connections
The Id3 (show ID3 Proteins) and NP1 genes become transcriptionally active after MyoD (show MYOD1 Proteins) induction in undifferentiated myoblasts. This is a stable, heritable event that does not need continued MyoD (show MYOD1 Proteins) activity & is not subject to negative regulation by activated H-Ras (show HRAS Proteins) G12V.
Neuronal pentraxin 1 and 2 are necessary for early synaptic refinements in mammalian retina and dorsal lateral geniculate nucleus. May exert their effects through mechanisms paralleling known role of short pentraxins outside the CNS. (Pentraxin 1 (show CRP Proteins) and 2)
This review provides a general overview of current knowledge of the signalling pathways that are modulated by NRP1 (show NELL1 Proteins), with particular focus on neuronal and vascular roles in the brain and retina.
This study suggests that NRP1 (show NELL1 Proteins) expression and LVD are independent factors that are likely to predict the risk of LN metastasis in squamous cell carcinoma (SCC (show CYP11A1 Proteins))of the tongue, whereas the expression of VEGFC (show VEGFC Proteins), VEGFR3 (show FLT4 Proteins), CCR7 (show CCR7 Proteins), and SEMA3E (show SEMA3E Proteins) are nonindependent predictive factors
Curcumin-loaded nanoliposomes linked to homing peptides for integrin targeting and neuropilin-1 (show NRP1 Proteins)-mediated internalization reduced viability of breast cancer cells.
Upregulated expression of NRP1 (show NELL1 Proteins) is associated with glioma.
Studies suggest that the activation of NRP-1 (show NELL1 Proteins) by PlGF (show PGF Proteins) directly contributes to tumour aggressiveness and to melanoma escape from anti-VEGF-A (show VEGFA Proteins) therapies.
REVIEW: Nrp1 (show NELL1 Proteins) functions in the vasculature is critical for the development of targeted therapeutics for cancer and vascular diseases such as atherosclerosis and retinopathies.
High Expression of Neuropilin-1 (show NRP1 Proteins) Associates with Hepatocellular Carcinoma.
Increased NRP-1 (show NELL1 Proteins) expression is associated with metastatic endometrial and lung cancers.
miR (show MLXIP Proteins)-152 suppression in NSCLC cells might promote neuropilin-1 (show NRP1 Proteins) mediated cancer metastasis.
NRP-1 (show NELL1 Proteins) was found to be overexpressed in gastric cancer (GC) tissues, and its expression correlates with the clinical staging, tumor differentiation and pathological types of gastric cancer.
This gene encodes one of two neuropilins, which contain specific protein domains which allow them to participate in several different types of signaling pathways that control cell migration. Neuropilins contain a large N-terminal extracellular domain, made up of complement-binding, coagulation factor V/VIII, and meprin domains. These proteins also contains a short membrane-spanning domain and a small cytoplasmic domain. Neuropilins bind many ligands and various types of co-receptors\; they affect cell survival, migration, and attraction. Some of the ligands and co-receptors bound by neuropilins are vascular endothelial growth factor (VEGF) and semaphorin family members. Several alternatively spliced transcript variants that encode different protein isoforms have been described for this gene.
neuronal pentraxin 1
, neuronal pentraxin I
, neuronal pentraxin-1
, 47 kDa taipoxin-binding protein
, transmembrane receptor
, vascular endothelial cell growth factor 165 receptor