Results 131 to 140 of about 6,163 (183)
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Theoretical Study of the Human Bradykinin–Bradykinin B2 Receptor Complex
ChemBioChem, 2008AbstractThe interaction of bradykinin (BK) with the bradykinin B2 receptor (B2R) was analyzed by using molecular modeling (MM) and molecular dynamics (MD) simulations. A homology model for B2R has been generated and the recently determined receptor‐bound solid‐state NMR spectroscopic structure of BK (Lopez et al., Angew. Chem.
Artur Giełdoń +3 more
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Intramolecular signal transduction by the bradykinin B2 receptor
International Immunopharmacology, 2002To study the intramolecular signal transduction, we performed single point and cassette mutations in transmembranal and intracellular regions of the bradykinin B2 receptor. We studied the influence of the two intramembranal Cys residues at positions 304 and 348, the role of Arg at position 177 in the highly conserved tripeptide sequence Asp-Arg-Tyr ...
Sylvia, Mueller +2 more
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Localization of bradykinin B2 receptors in sheep uterus
Immunopharmacology, 1996The localization and characterization of bradykinin B2 receptors in sheep uterus was carried out using a radiolabelled B2 receptor ligand, 3,4-hydroxyphenypropionyl-D-Arg0-[Hyp3,Thi5,D-++ +Tic7,D-Oic8] bradykinin (HPP-HOE140). Competition of the radioligand, [125I]HPP-HOE140, from membrane preparations of anoestrus sheep uterus by bradykinin agonists ...
C, Murone +5 more
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Targeting the ‘Janus face' of the B2-bradykinin receptor
Expert Opinion on Therapeutic Targets, 2013Kinins are main active mediators of the kallikrein-kinin system (KKS) via bradykinin type 1 inducible (B1R) and type 2 constitutive (B2R) receptors. B2R mediates most physiological bradykinin (BK) responses, including vasodilation, natriuresis, NO, prostaglandins release.The article summarizes knowledge on kinins, B2R signaling and biological functions;
Nelly, Blaes, Jean-Pierre, Girolami
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B2 bradykinin receptor immunoreactivity in rat brain
The Journal of Comparative Neurology, 2000Bradykinin has long been known to exist in the central nervous system and has been hypothesized to mediate specific functions. Despite an increasing understanding of the functions of bradykinin, little is known about the cell types expressing the bradykinin receptor within the brain.
E Y, Chen +3 more
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Structural characterization of lipopeptide agonists for the bradykinin B2 receptor
Biopolymers, 2001The conformational features of Pam-Lys(0)-Arg(1)-Pro(2)-Pro(3)-Gly(4)-Phe(5)-Ser(6)-Pro(7)-Phe(8)-Arg(9)-OH (PKD) and Pam-Gly(-1)-Lys(0)-Arg(1)-Pro(2)-Pro(3)-Gly(4)-Phe(5)-Ser(6)-Pro(7)-Phe(8)-Arg(9)-OH (PGKD), the Pam-Lys and Pam-Gly-Lys analogues of bradykinin, have been determined by high-resolution NMR in a zwitterionic lipoid environment.
GIRAGOSSIAN C. +7 more
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Nonpeptide Mimic of Bradykinin with Long-Acting Properties at the Bradykinin B2 Receptor
Molecular Pharmacology, 1997Kinins, members of a family of peptides released from kininogens by the action of kallikreins, exhibit a variety of biological activities including vasodilation, increased vascular permeability, contraction of smooth muscle cells, and activation of sensory neurons.
I, Aramori +16 more
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Bradykinin B2 receptors – a target in diabetic nephropathy
Expert Opinion on Therapeutic Targets, 2005Diabetic nephropathy is the leading cause of chronic renal failure in westernized countries. The polymorphism in angiotensin-converting enzyme (ACE), which leads to higher than normal levels of this enzyme, is a predictor of nephropathy in patients with diabetes.
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Characterization of a B2-bradykinin receptor in human glomerular podocytes
American Journal of Physiology-Renal Physiology, 1996We characterized bradykinin (BK) receptors in a human line of glomerular visceral epithelial cells (hGVEC) transfected by the SV40 virus. [3H]BK bound specifically in a manner consistent with a single high-affinity site. Scatchard analysis yielded dissociation constant and maximum binding values of 0.28 +/- 0.04 nM and 76.6 +/- 4.9 fmol/mg ...
N, Ardaillou +4 more
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Role of ßarrestins in bradykinin B2 receptor-mediated signalling
Cellular Signalling, 2011G protein-coupled receptors (GPCRs) can engage multiple pathways to activate ERK1/2 via both G proteins and/or ßarrestin. Receptor recruitment of ßarrestin is also important for GPCR desensitization, internalization and resensitization. Modulation of the receptor/ßarrestin interaction through modification of either component would presumably alter the ...
Brandon, Zimmerman +6 more
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