{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,14]],"date-time":"2026-02-14T00:48:56Z","timestamp":1771030136995,"version":"3.50.1"},"reference-count":31,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2012,2,1]],"date-time":"2012-02-01T00:00:00Z","timestamp":1328054400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"name":"Canadian Institutes of Health Research (CIHR)","award":["MOP-93773"],"award-info":[{"award-number":["MOP-93773"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmacological Research"],"published-print":{"date-parts":[[2012,2]]},"DOI":"10.1016\/j.phrs.2011.11.004","type":"journal-article","created":{"date-parts":[[2011,11,18]],"date-time":"2011-11-18T08:51:33Z","timestamp":1321606293000},"page":"247-253","source":"Crossref","is-referenced-by-count":18,"title":["Prolonged signalling and trafficking of the bradykinin B2 receptor stimulated with the amphibian peptide maximakinin: Insight into the endosomal inactivation of kinins"],"prefix":"10.1016","volume":"65","author":[{"given":"Marie-Th\u00e9r\u00e8se","family":"Bawolak","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Caroline","family":"Roy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lajos","family":"Gera","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fran\u00e7ois","family":"Marceau","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.phrs.2011.11.004_bib0005","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.regpep.2004.04.007","article-title":"The smooth muscle pharmacology of maximakinin, a receptor-selective bradykinin-related nonadecapeptide from the venom of the Chinese toad, Bombina maxima","volume":"121","author":"O\u2019Rourke","year":"2004","journal-title":"Regul Pept"},{"key":"10.1016\/j.phrs.2011.11.004_bib0010","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1016\/S0196-9781(03)00167-0","article-title":"Cloning of maximakinin precursor cDNAs from Chinese toad, Bombina maxima, venom","volume":"24","author":"Chen","year":"2003","journal-title":"Peptides"},{"key":"10.1016\/j.phrs.2011.11.004_bib0015","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/0041-0101(91)90098-C","article-title":"Neurotoxic kinins from wasp and ant venoms","volume":"29","author":"Piek","year":"1991","journal-title":"Toxicon"},{"key":"10.1016\/j.phrs.2011.11.004_bib0020","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1042\/bj1410915","article-title":"Hydrolysis of bradykinin and its higher homologues by angiotensin-converting enzyme","volume":"141","author":"Dorer","year":"1974","journal-title":"Biochem J"},{"key":"10.1016\/j.phrs.2011.11.004_bib0025","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1124\/jpet.107.123422","volume":"323","author":"Bawolak","year":"2007","journal-title":"J Pharmacol Exp Ther"},{"key":"10.1016\/j.phrs.2011.11.004_bib0030","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1111\/j.1476-5381.2009.00409.x","article-title":"Effects of inactivation-resistant agonists on the signalling, desensitization and down-regulation of bradykinin B2 receptors","volume":"158","author":"Bawolak","year":"2009","journal-title":"Br J Pharmacol"},{"key":"10.1016\/j.phrs.2011.11.004_bib0035","doi-asserted-by":"crossref","first-page":"22411","DOI":"10.1074\/jbc.M109.026674","article-title":"Endosomal endothelin-converting enzyme-1: a regulator of \u03b2-arrestin-dependent ERK signaling","volume":"284","author":"Cottrell","year":"2009","journal-title":"J Biol Chem"},{"key":"10.1016\/j.phrs.2011.11.004_bib0040","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1016\/j.peptides.2007.12.004","article-title":"Lack of direct interaction between enalaprilat and the kinin B1 receptors","volume":"29","author":"Morissette","year":"2008","journal-title":"Peptides"},{"key":"10.1016\/j.phrs.2011.11.004_bib0045","doi-asserted-by":"crossref","first-page":"1546","DOI":"10.1016\/j.peptides.2010.04.027","article-title":"Ligand-based approaches to investigate the expression of angiotensin converting enzyme in intact human umbilical vein endothelial cells","volume":"31","author":"Koumbadinga","year":"2010","journal-title":"Peptides"},{"key":"10.1016\/j.phrs.2011.11.004_bib0050","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1124\/jpet.110.177147","article-title":"Design of fluorescent bradykinin analogs: application to imaging of B2 receptor-mediated agonist endocytosis and trafficking and of angiotensin converting enzyme","volume":"337","author":"Gera","year":"2011","journal-title":"J Pharmacol Exp Ther"},{"key":"10.1016\/j.phrs.2011.11.004_bib0055","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/S0162-3109(99)00128-9","article-title":"Pharmacological profile of LF 16-0687, a new potent non peptide bradykinin B2 receptor antagonist","volume":"43","author":"Pruneau","year":"1999","journal-title":"Immunopharmacology"},{"key":"10.1016\/j.phrs.2011.11.004_bib0060","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1124\/pr.57.1.2","article-title":"International union of pharmacology. XLV. Classification of the kinin receptor family: from molecular mechanisms to pathophysiological consequences","volume":"57","author":"Leeb-Lundberg","year":"2005","journal-title":"Pharmacol Rev"},{"key":"10.1016\/j.phrs.2011.11.004_bib0065","doi-asserted-by":"crossref","first-page":"300","DOI":"10.1016\/j.pep.2007.04.020","article-title":"High-level expression and purification of the human bradykinin B2 receptor in a tetracycline-inducible stable HEK293S cell line","volume":"55","author":"Camponova","year":"2007","journal-title":"Protein Expr Purif"},{"key":"10.1016\/j.phrs.2011.11.004_bib0070","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0026-895X(25)09890-6","article-title":"Differential pharmacology of cloned human and mouse B2 bradykinin receptors","volume":"45","author":"Hess","year":"1994","journal-title":"Mol Pharmacol"},{"key":"10.1016\/j.phrs.2011.11.004_bib0075","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1111\/j.1476-5381.1990.tb12947.x","article-title":"Structure\u2013activity studies on bradykinin and related peptides: agonists","volume":"99","author":"Rhaleb","year":"1990","journal-title":"Br J Pharmacol"},{"key":"10.1016\/j.phrs.2011.11.004_bib0080","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/S0022-3565(24)29506-9","article-title":"Bradykinin B2 receptor endocytosis, recycling, and down-regulation assessed using green fluorescent protein conjugates","volume":"297","author":"Bachvarov","year":"2001","journal-title":"J Pharmacol Exp Ther"},{"key":"10.1016\/j.phrs.2011.11.004_bib0085","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1016\/j.phrs.2011.08.001","article-title":"Met-Lys-bradykinin-Ser-Ser, a peptide produced by the neutrophil from kininogen, is metabolically activated by angiotensin converting enzyme","volume":"64","author":"Gera","year":"2011","journal-title":"Pharmacol Res"},{"key":"10.1016\/j.phrs.2011.11.004_bib0090","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/S0021-9258(18)48494-3","article-title":"Receptor-mediated internalization of bradykinin. DDT1 MF-2 smooth muscle cells process internalized bradykinin via multiple degradative pathways","volume":"267","author":"Munoz","year":"1992","journal-title":"J Biol Chem"},{"key":"10.1016\/j.phrs.2011.11.004_bib0095","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1016\/j.cellsig.2010.11.016","article-title":"Role of \u03b2arrestins in bradykinin B2 receptor-mediated signalling","volume":"23","author":"Zimmerman","year":"2011","journal-title":"Cell Signal"},{"key":"10.1016\/j.phrs.2011.11.004_bib0100","doi-asserted-by":"crossref","first-page":"917","DOI":"10.1038\/nrm2272","article-title":"Vacuolar ATPases: rotary pumps in physiology and pathophysiology","volume":"8","author":"Forgac","year":"2007","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1016\/j.phrs.2011.11.004_bib0105","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1083\/jcb.200704053","article-title":"Endothelin-converting enzyme-1 regulates endosomal sorting of calcitonin receptor-like receptor and \u03b2-arrestins","volume":"179","author":"Padilla","year":"2007","journal-title":"J Cell Biol"},{"key":"10.1016\/j.phrs.2011.11.004_bib0110","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/S0065-2571(01)00034-6","article-title":"Lysosomal cathepsins: structure, role in antigen processing and presentation, and cancer","volume":"42","author":"Turk","year":"2002","journal-title":"Adv Enzyme Regul"},{"key":"10.1016\/j.phrs.2011.11.004_bib0115","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1042\/BJ20040864","article-title":"Cathepsin K: a cysteine protease with unique kinin-degrading properties","volume":"383","author":"Godat","year":"2004","journal-title":"Biochem J"},{"key":"10.1016\/j.phrs.2011.11.004_bib0120","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/0014-5793(87)80268-5","article-title":"Action of rat liver cathepsin B on bradykinin and on the oxidized insulin A-chain","volume":"219","author":"Br\u00f6mme","year":"1987","journal-title":"FEBS Lett"},{"key":"10.1016\/j.phrs.2011.11.004_bib0125","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1093\/oxfordjournals.jbchem.a131325","article-title":"Studies on cathepsins of rat liver lysosomes. III. Hydrolysis of peptides, and inactivation of angiotensin and bradykinin by cathepsin A","volume":"80","author":"Matsuda","year":"1976","journal-title":"J Biochem"},{"key":"10.1016\/j.phrs.2011.11.004_bib0130","doi-asserted-by":"crossref","first-page":"1977","DOI":"10.1016\/j.peptides.2003.09.018","article-title":"Human brain cathepsin H as a neuropeptide and bradykinin metabolizing enzyme","volume":"24","author":"Brguljan","year":"2003","journal-title":"Peptides"},{"key":"10.1016\/j.phrs.2011.11.004_bib0135","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1124\/jpet.103.059188","article-title":"Action of bradykinin in the submucosal plexus of guinea pig small intestine","volume":"309","author":"Hu","year":"2004","journal-title":"J Pharmacol Exp Ther"},{"key":"10.1016\/j.phrs.2011.11.004_bib0140","first-page":"G1","article-title":"Kinins as mediators of intestinal secretion","volume":"256","author":"Gaginella","year":"1989","journal-title":"Am J Physiol"},{"key":"10.1016\/j.phrs.2011.11.004_bib0145","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.3181\/00379727-142-37219","article-title":"Release of histamine from mast cells by vasoactive peptides","volume":"142","author":"Johnson","year":"1973","journal-title":"Proc Soc Exp Biol Med"},{"key":"10.1016\/j.phrs.2011.11.004_bib0150","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.ejphar.2011.06.041","article-title":"Bradykinin B2 receptor-mediated transport into intact cells: anti-receptor antibody-based cargoes","volume":"668","author":"Bawolak","year":"2011","journal-title":"Eur J Pharmacol"},{"key":"10.1016\/j.phrs.2011.11.004_bib0155","doi-asserted-by":"crossref","first-page":"220","DOI":"10.7150\/thno\/v01p0220","article-title":"F-labeled GRPR agonists and antagonists: a comparative study in prostate cancer imaging","volume":"1","author":"Yang","year":"2011","journal-title":"Theranostics"}],"container-title":["Pharmacological Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1043661811002830?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1043661811002830?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,3,14]],"date-time":"2025-03-14T06:14:57Z","timestamp":1741932897000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1043661811002830"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,2]]},"references-count":31,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2012,2]]}},"alternative-id":["S1043661811002830"],"URL":"https:\/\/doi.org\/10.1016\/j.phrs.2011.11.004","relation":{},"ISSN":["1043-6618"],"issn-type":[{"value":"1043-6618","type":"print"}],"subject":[],"published":{"date-parts":[[2012,2]]}}}