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1 generation of plasmin, it was independent of proteinase-activated receptor 1 (PAR-1) and instead refl
2 cardiomyocytes, and cardiac fibroblasts via proteinase-activated receptor 1 (PAR-1) and mammalian ta
3 f the major high-affinity thrombin receptor, proteinase-activated receptor 1 (PAR-1), during the deve
5 cantly increased, together with those of the proteinase-activated receptor 1 (PAR1), an inflammation-
10 As thrombin binding to the G protein-coupled proteinase activated receptor-1 (PAR-1) induces endothel
11 he mechanisms of restoration of cell surface proteinase-activated receptor-1 (PAR-1) by investigating
15 o transactivation of EGF receptor (EGFR) via proteinase-activated receptor 2 (PAR(2)) activation.
18 al sequencing, while its ability to activate proteinase-activated receptor 2 (PAR-2) was determined u
19 ses activate the G protein-coupled receptor, proteinase-activated receptor 2 (PAR-2), via cleavage an
23 ulation signaling via tissue factor (TF) and proteinase-activated receptor 2 (PAR2) in obesity-mediat
26 ta), serine proteinases such as trypsin, and proteinase-activated receptor 2 (PAR2) promote tumor dev
27 We report that agonists of Galphaq-coupled proteinase-activated receptor 2 (PAR2) stimulate formati
31 We then demonstrated that injection of the proteinase-activated receptor 2 activating peptide into
35 ctions was performed with antibodies against proteinase-activated receptor 2 and vanilloid receptor 1
38 gnals, whereas serine protease activation of proteinase-activated receptor 2 is a negative signal reg
40 Thus, tryptase inhibitors and antagonists of proteinase-activated receptor 2 may be useful anti-infla
43 imary spinal afferent neurons, which express proteinase-activated receptor 2, also contain the proinf
44 ucts), which likely led to the initiation of proteinase-activated receptor 2-mediated pruritus and My
50 orthern blot analysis completed with a human proteinase activated receptor-2 (PAR-2) cDNA as probe de
51 rk shows that the G-protein-coupled receptor proteinase activated receptor-2 activates signals that s
52 emarkably similar to the organization of the proteinase activated receptor-2 gene in which the putati
61 e disruption approaches, we demonstrate that proteinase-activated receptor-2 (PAR-2) plays a pivotal
62 synthase kinase 3beta, protein kinase C, and proteinase-activated receptor-2 (PAR-2), which is consis
65 inases can signal by cleaving and activating proteinase-activated receptor-2 (PAR2), a G-protein-coup
66 of the following key proinflammatory genes: proteinase-activated receptor-2 (PAR2), tumor necrosis f
67 ctivated receptor-2, either through specific proteinase-activated receptor-2 activating peptides or t
68 contrast, Rho activity did not affect either proteinase-activated receptor-2 activity or mRNA and pro
69 ed 5,6-EET via a mechanism that involved the proteinase-activated receptor-2 and cytochrome epoxygena
75 uman keratinocytes is Rho dependent and that proteinase-activated receptor-2 signals to activate Rho.
76 iated phagocytosis is Rho dependent and that proteinase-activated receptor-2 signals to Rho and cAMP
77 an keratinocytes and show that activation of proteinase-activated receptor-2, either through specific
79 ning GTPase activating protein 2) and F2rl2 (proteinase-activated receptor-3), 2 genes that were also
80 aggregation induced by low concentrations of proteinase-activated receptor 4-activating peptide, U466
83 cornea are activation of thrombin-sensitive, proteinase-activated receptors and cleavage of fibrinoge
86 reviously known to regulate inflammation via proteinase-activated receptors, can also play a substant
91 to examine whether HCECs express functional proteinase-activated receptor (PAR)-1 and -2 and evaluat
92 rmation of vasculature, we hypothesized that proteinase-activated receptor (Par)-2 (official name F2r
93 e use genetic epistasis analysis to identify proteinase-activated receptor (PAR)-2-dependent inflamma
94 ochemistry, we confirmed renal expression of proteinase-activated receptor (PAR-2) and demonstrated i
104 ding prostaglandin subtypes, growth factors, proteinase-activated receptors, peroxisome proliferator-
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