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Genomic association study identified deleterious rare variants in P2RY1 in patients with ischemic stroke.
Pin1 induces the ADP-induced migration of human dental pulp cells through P2Y1 stabilization.
predominant role of P2Y1 receptors in human embryonic stem cells and a transition of P2Y-IP3R coupling in derived cardiovascular progenitor cells are responsible for the differential Ca(2+) mobilization between these cells.
The negative feedback modulation between LncRNA-SARCC/AR complex and HIF-2alpha signaling may then lead to differentially modulated RCC progression in a VHL-dependent manner. Together, these results may provide us a new therapeutic approach via targeting this newly identified signal from LncRNA-SARCC to AR-mediated HIF-2alpha/C-MYC signals against RCC progression.
these data highlight a key role of the P2Y1/PI3Kbeta axis in endothelial cell proliferation downstream of ecto-F1-ATPase activation by apoA-I. Pharmacological targeting of this pathway could represent a promising approach to enhance vascular endothelial protection.
ALIX regulates P2Y1 degradation.
There is increased expression of P2Y1 receptors in the rectosigmoid mucosa of diarrhea-predominant irritable bowel syndrome patients.
High extracellular NaCl induces priming of the NLRP3 inflammasome in RPE cells, in part via P2Y1 receptor signaling
aim of this study was to evaluate the effects of platelet receptor gene (P2Y12, P2Y1) and glycoprotein gene (GPIIIa) polymorphisms, as well as their interactions, on antiplatelet drug responsiveness and clinical outcomes in patients with acute MIS
Early neurological deterioration (END) occurred significantly more frequently in patients with aspirin resistance (AR) or high-risk interactive genotypes. Moreover, AR and high-risk interactive genotypes were independently associated with END.
Synergistic inhibition of both P2Y1 and P2Y12 adenosine diphosphate receptors by GLS-409 immediately attenuates platelet-mediated thrombosis and effectively blocks agonist-stimulated platelet aggregation irrespective of concomitant aspirin therapy.
Antibody EL2Ab binds to and exhibits P2Y1R-dependent function-blocking activity in the context of platelets.
P2Y1 couples to and activates TRPV4. PKC inhibitors prevented P2Y1 receptor activation of TRPV4.
P2Y1 receptors are a potential pharmacological target leading smooth muscle relaxation to treat spasticity in colonic motor disorders.
crystal structures of the human P2Y1R in complex with a nucleotide antagonist MRS2500 at 2.7 A resolution, and with a non-nucleotide antagonist BPTU at 2.2 A resolution
Data indicate that ATP-evoked Hoechst 33258 uptake was dependent on activation of P2Y receptors P2Y1 and P2Y2.
This study shows that Up4A is a potent native agonist for P2Y1R and SK-channel activation in human and mouse colon.
These studies demonstrate a role for P2Y receptor activation in stimulation of ATP release.
The immunohistochemical results were reflected in the immunoblotting data P2RY1 receptors were detected at higher levels of expression in patient with cortical dysplasia with intractable epilepsy.
P2Y1 and P2Y12 genes were polymorphic in a Korean population; 3 intronic P2Y12 polymorphisms (i-139C>T, i-744T>C, i-801insA) were in complete linkage disequilibrium but not with the c.52C>T polymorphism; platelet aggregation in response to ADP associated with c.52C>T polymorphism but not with the 3 intronic polymorphisms or the P2Y1 c.1622A>T polymorphism
P2Y1 receptor-mediated responses involve Flt3 transactivation, and may identify a unique mechanism whereby cancer chemotherapy with receptor tyrosine kinase inhibitors promotes vascular dysfunction.
Purinergic P2Y1 receptor signaling mediates wound stimuli-induced cyclooxygenase-2 expression in intestinal subepithelial myofibroblasts.
P2Y1 and P2Y13 receptors play a major role in vasa vasorum endothelial cells growth responses.
The product of this gene belongs to the family of G-protein coupled receptors. This family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. This receptor functions as a receptor for extracellular ATP and ADP. In platelets binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and probably to platelet aggregation.
, P2Y purinoceptor 1
, P2Y1 receptor
, P2Y1 purinoceptor
, P2 purinoceptor subtype Y1
, platelet ADP receptor
, P2 purinoreceptor subclass 2Y
, P2Y ATP receptor 1
, ATP receptor P2Y1
, G protein-coupled receptor
, p2y1 purinoceptor