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work highlights a potential role for synaptic proteins, such as NP1 and glutamate (show GRIN1 Proteins) receptors in lysosomal storage diseases.
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.
Data provide evidence that NRP1 (show NELL1 Proteins) functions to enhance the metastatic potential of prostate tumors.
NRP1 (show NELL1 Proteins) is an important niche component
our data suggest a novel molecular mechanism by which tMUC1 may modulate NRP1 (show NELL1 Proteins)-dependent VEGFR (show KDR Proteins) signaling in PDA cells.
Our findings identify aberrant active integrin b1-driven Src (show SRC Proteins)-Akt (show AKT1 Proteins) hyperactivation as a primary resistance mechanism to cetuximab in PDAC cells and offer an effective therapeutic strategy to overcome this resistance using an EGFR (show EGFR Proteins) and NRP1 (show NELL1 Proteins) dual targeting antibody
VEGF-A (show VEGFA Proteins) acts via interaction with NRP-1 (show NELL1 Proteins) to trigger intracellular events leading to ECS cell survival and formation of aggressive, invasive and highly vascularized tumors.
These data identify a new molecular mechanism of brain microvascular endothelial inflammatory response through NRP1 (show NELL1 Proteins)-IFNgamma crosstalk.
This study indicates that capsaicin application results in significant loss of epidermal NRP-1 (show NELL1 Proteins) receptor expression, whereas diabetic subjects presenting small fiber neuropathy show full epidermal NRP-1 (show NELL1 Proteins) expression in contrast to the basal expression pattern seen in healthy controls
Study show that a high percentage of intratumoral NRP1 (show NELL1 Proteins)(+) Tregs correlates with poor prognosis in melanoma and head and neck squamous cell carcinoma.
Study revels the structural description of the neuropilin-1 (show NRP1 Proteins) ectopic region by reporting the crystal structure of its MAM domain. The domain adopts a jellyroll fold that is stabilized by a Ca2 (show CA2 Proteins)+ ion while forming a molecular surface that is distinct from its structural homologs.
Data suggest that neuropilin-1 (NRP1 (show NRP1 Proteins)) functions as a receptor for neutrophil elastase (NE (show ELANE Proteins)), mediates uptake/absorption of NE, and facilitates cross-presentation of PR1 (show TMEM37 Proteins) (a peptide fragment of NE) in breast cancer cells.
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