{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,3]],"date-time":"2025-12-03T18:08:25Z","timestamp":1764785305458,"version":"3.38.0"},"reference-count":87,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,3,1]],"date-time":"2024-03-01T00:00:00Z","timestamp":1709251200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,1,24]],"date-time":"2024-01-24T00:00:00Z","timestamp":1706054400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"DOI":"10.13039\/100007670","name":"Dalhousie Medical Research Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100007670","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100020170","name":"Research Nova Scotia","doi-asserted-by":"publisher","award":["MED-DI-2019-2022"],"award-info":[{"award-number":["MED-DI-2019-2022"]}],"id":[{"id":"10.13039\/501100020170","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100009874","name":"Universit\u00e9 de Sherbrooke","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100009874","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["376770"],"award-info":[{"award-number":["376770"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["510963","RGPIN-2023-03713","RGPIN-2023-05912"],"award-info":[{"award-number":["510963","RGPIN-2023-03713","RGPIN-2023-05912"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000196","name":"Canada Foundation for Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000196","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005785","name":"Faculty of Medicine, Dalhousie University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005785","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"published-print":{"date-parts":[[2024,3]]},"DOI":"10.1016\/j.bbamem.2024.184289","type":"journal-article","created":{"date-parts":[[2024,1,24]],"date-time":"2024-01-24T23:58:08Z","timestamp":1706140688000},"page":"184289","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"title":["Localized apelin-17 analogue-bicelle interactions as a facilitator of membrane-catalyzed receptor recognition and binding"],"prefix":"10.1016","volume":"1866","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5382-616X","authenticated-orcid":false,"given":"Tr\u1ea7n Thanh T\u00e2m","family":"Ph\u1ea1m","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2551-9135","authenticated-orcid":false,"given":"Alexandre","family":"Murza","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"\u00c9ric","family":"Marsault","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6245-1147","authenticated-orcid":false,"given":"John P.","family":"Frampton","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0793-5573","authenticated-orcid":false,"given":"Jan K.","family":"Rainey","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamem.2024.184289_bb0005","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1006\/bbrc.1998.9489","article-title":"Isolation and characterization of a novel endogenous peptide ligand for the human APJ receptor","volume":"251","author":"Tatemoto","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamem.2024.184289_bb0010","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1016\/j.devcel.2013.11.002","article-title":"ELABELA: a hormone essential for heart development signals via the apelin receptor","volume":"27","author":"Chng","year":"2013","journal-title":"Dev. Cell"},{"key":"10.1016\/j.bbamem.2024.184289_bb0015","doi-asserted-by":"crossref","first-page":"1248636","DOI":"10.1126\/science.1248636","article-title":"Toddler: an embryonic signal that promotes cell movement via Apelin receptors","volume":"343","author":"Pauli","year":"2014","journal-title":"Science"},{"key":"10.1016\/j.bbamem.2024.184289_bb0020","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1016\/0378-1119(93)90495-O","article-title":"A human gene that shows identity with the gene encoding the angiotensin receptor is located on chromosome 11","volume":"136","author":"O\u2019Dowd","year":"1993","journal-title":"Gene"},{"key":"10.1016\/j.bbamem.2024.184289_bb0025","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1002\/cphy.c170028","article-title":"Apelinergic system structure and function","volume":"8","author":"Shin","year":"2017","journal-title":"Compr. Physiol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0030","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1161\/01.RES.0000033522.37861.69","article-title":"Apelin, the novel endogenous ligand of the orphan receptor APJ, regulates cardiac contractility","volume":"91","author":"Szokodi","year":"2002","journal-title":"Circ. Res."},{"key":"10.1016\/j.bbamem.2024.184289_bb0035","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0014-2999(03)01821-1","article-title":"Venous dilator effect of apelin, an endogenous peptide ligand for the orphan APJ receptor, in conscious rats","volume":"470","author":"Cheng","year":"2003","journal-title":"Eur. J. Pharmacol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0040","doi-asserted-by":"crossref","DOI":"10.1161\/01.CIR.0000138382.57325.5c","article-title":"Apelin has in vivo inotropic effects on normal and failing hearts","volume":"110","author":"Berry","year":"2004","journal-title":"Circulation"},{"key":"10.1016\/j.bbamem.2024.184289_bb0045","doi-asserted-by":"crossref","first-page":"908","DOI":"10.1016\/j.jacc.2008.06.013","article-title":"Vascular effects of apelin in vivo in man","volume":"52","author":"Japp","year":"2008","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0050","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1161\/HYPERTENSIONAHA.109.134619","article-title":"[Pyr1]apelin-13 identified as the predominant apelin isoform in the human heart: vasoactive mechanisms and inotropic action in disease","volume":"54","author":"Maguire","year":"2009","journal-title":"Hypertension"},{"key":"10.1016\/j.bbamem.2024.184289_bb0055","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1161\/CIRCHEARTFAILURE.111.000077","article-title":"Sustained cardiovascular actions of APJ agonism during renin-angiotensin system activation and in patients with heart failure","volume":"6","author":"Barnes","year":"2013","journal-title":"Circ. Heart Fail."},{"key":"10.1016\/j.bbamem.2024.184289_bb0060","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1161\/HYPERTENSIONAHA.114.05099","article-title":"Design, characterization, and first-in-human study of the vascular actions of a novel biased apelin receptor agonist","volume":"65","author":"Brame","year":"2015","journal-title":"Hypertension"},{"key":"10.1016\/j.bbamem.2024.184289_bb0065","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1016\/j.peptides.2011.06.025","article-title":"Apelin alleviates diabetes-associated endoplasmic reticulum stress in the pancreas of Akita mice","volume":"32","author":"Chen","year":"2011","journal-title":"Peptides"},{"key":"10.1016\/j.bbamem.2024.184289_bb0070","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1007\/s11010-011-0799-0","article-title":"Apelin stimulates glucose uptake through the PI3K\/Akt pathway and improves insulin resistance in 3T3-L1 adipocytes","volume":"353","author":"Zhu","year":"2011","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.bbamem.2024.184289_bb0075","doi-asserted-by":"crossref","first-page":"H1471","DOI":"10.1152\/ajpheart.00097.2011","article-title":"Apelin-13 protects the heart against ischemia-reperfusion injury through inhibition of ER-dependent apoptotic pathways in a time-dependent fashion","volume":"301","author":"Tao","year":"2011","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0080","doi-asserted-by":"crossref","first-page":"310","DOI":"10.2337\/db11-0100","article-title":"Apelin treatment increases complete fatty acid oxidation, mitochondrial oxidative capacity, and biogenesis in muscle of insulin-resistant mice","volume":"61","author":"Attane","year":"2012","journal-title":"Diabetes"},{"key":"10.1016\/j.bbamem.2024.184289_bb0085","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/j.yjmcc.2013.07.002","article-title":"Apelin administration ameliorates high fat diet-induced cardiac hypertrophy and contractile dysfunction","volume":"63","author":"Ceylan-Isik","year":"2013","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0090","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1038\/sj.emboj.7601982","article-title":"Spatial and temporal role of the apelin\/APJ system in the caliber size regulation of blood vessels during angiogenesis","volume":"27","author":"Kidoya","year":"2008","journal-title":"EMBO J."},{"key":"10.1016\/j.bbamem.2024.184289_bb0095","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1160\/TH08-06-0358","article-title":"Maturation of blood vessels by haematopoietic stem cells and progenitor cells: involvement of apelin\/APJ and angiopoietin\/Tie2 interactions in vessel caliber size regulation","volume":"101","author":"Takakura","year":"2009","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.bbamem.2024.184289_bb0100","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1016\/j.stem.2015.08.010","article-title":"ELABELA is an endogenous growth factor that sustains hESC self-renewal via the PI3K\/AKT pathway","volume":"17","author":"Ho","year":"2015","journal-title":"Cell Stem Cell"},{"key":"10.1016\/j.bbamem.2024.184289_bb0105","doi-asserted-by":"crossref","first-page":"18261","DOI":"10.1074\/jbc.M115.648238","article-title":"Apela regulates fluid homeostasis by binding to the APJ receptor to activate Gi signaling","volume":"290","author":"Deng","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2024.184289_bb0110","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1139\/bcb-2014-0072","article-title":"The apelin receptor: physiology, pathology, cell signalling, and ligand modulation of a peptide-activated class a GPCR","volume":"92","author":"Chapman","year":"2014","journal-title":"Biochem. Cell Biol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0115","doi-asserted-by":"crossref","first-page":"16104","DOI":"10.1038\/srep16104","article-title":"Apelin regulates FoxO3 translocation to mediate cardioprotective responses to myocardial injury and obesity","volume":"5","author":"Boal","year":"2015","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbamem.2024.184289_bb0120","doi-asserted-by":"crossref","first-page":"1850","DOI":"10.1111\/bph.13485","article-title":"Apelin-13 administration protects against ischaemia\/reperfusion-mediated apoptosis through the FoxO1 pathway in high-fat diet-induced obesity","volume":"173","author":"Boal","year":"2016","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0125","doi-asserted-by":"crossref","first-page":"1120","DOI":"10.1097\/JTO.0b013e3181e2c1ff","article-title":"Apelin expression in human non-small cell lung cancer: role in angiogenesis and prognosis","volume":"5","author":"Berta","year":"2010","journal-title":"J. Thorac. Oncol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0130","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1016\/j.ejca.2013.11.017","article-title":"Tumour co-expression of apelin and its receptor is the basis of an autocrine loop involved in the growth of colon adenocarcinomas","volume":"50","author":"Picault","year":"2014","journal-title":"Eur. J. Cancer"},{"key":"10.1016\/j.bbamem.2024.184289_bb0135","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1111\/cas.12836","article-title":"Apelin as a marker for monitoring the tumor vessel normalization window during antiangiogenic therapy","volume":"107","author":"Zhang","year":"2016","journal-title":"Cancer Sci."},{"key":"10.1016\/j.bbamem.2024.184289_bb0140","doi-asserted-by":"crossref","DOI":"10.3390\/ijms21114179","article-title":"Apelin controls angiogenesis-dependent glioblastoma growth","volume":"21","author":"Frisch","year":"2020","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbamem.2024.184289_bb0145","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.advms.2020.02.002","article-title":"Role of Apelin\/APJ axis in cancer development and progression","volume":"65","author":"Masoumi","year":"2020","journal-title":"Adv. Med. Sci."},{"key":"10.1016\/j.bbamem.2024.184289_bb0150","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1007\/s10557-022-07328-w","article-title":"A first-in-human study of AMG 986, a novel apelin receptor agonist, in healthy subjects and heart failure patients","volume":"37","author":"Winkle","year":"2023","journal-title":"Cardiovasc. Drugs Ther."},{"key":"10.1016\/j.bbamem.2024.184289_bb0155","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1111\/dom.13055","article-title":"Apelin administration improves insulin sensitivity in overweight men during hyperinsulinaemic-euglycaemic clamp","volume":"20","author":"Gourdy","year":"2018","journal-title":"Diabetes Obes. Metab."},{"key":"10.1016\/j.bbamem.2024.184289_bb0160","doi-asserted-by":"crossref","first-page":"10465","DOI":"10.1021\/jp904562q","article-title":"Headgroup-dependent membrane catalysis of apelin\u2212receptor interactions is likely","volume":"113","author":"Langelaan","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.bbamem.2024.184289_bb0165","doi-asserted-by":"crossref","first-page":"15433","DOI":"10.1038\/s41598-017-14784-0","article-title":"Apelin conformational and binding equilibria upon micelle interaction primarily depend on membrane-mimetic headgroup","volume":"7","author":"Shin","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbamem.2024.184289_bb0170","first-page":"767","article-title":"Apela exhibits isoform- and headgroup-dependent modulation of micelle binding, peptide conformation and dynamics","volume":"2017","author":"Huang","year":"1859","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2024.184289_bb0175","doi-asserted-by":"crossref","first-page":"5774","DOI":"10.1073\/pnas.83.16.5774","article-title":"Membrane lipid phase as catalyst for peptide-receptor interactions","volume":"83","author":"Sargent","year":"1986","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2024.184289_bb0180","doi-asserted-by":"crossref","first-page":"15931","DOI":"10.1021\/bi061199g","article-title":"Membrane interactions of dynorphins","volume":"45","author":"Lind","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2024.184289_bb0185","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1007\/s00249-009-0423-3","article-title":"The interaction of neuropeptide Y with negatively charged and zwitterionic phospholipid membranes","volume":"38","author":"Thomas","year":"2009","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.bbamem.2024.184289_bb0190","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1038\/84159","article-title":"Conformation of a peptide ligand bound to its G-protein coupled receptor","volume":"8","author":"Inooka","year":"2001","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0195","doi-asserted-by":"crossref","first-page":"1288","DOI":"10.1210\/endo-112-4-1288","article-title":"Biological activities and receptor interactions of des-Leu16 salmon and des-Phe16 human calcitonin","volume":"112","author":"Findlay","year":"1983","journal-title":"Endocrinology"},{"key":"10.1016\/j.bbamem.2024.184289_bb0200","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1002\/(SICI)1097-0134(19980815)32:3<314::AID-PROT7>3.0.CO;2-H","article-title":"Solution structure of human calcitonin in membrane-mimetic environment: the role of the amphipathic helix","volume":"32","author":"Motta","year":"1998","journal-title":"Proteins"},{"key":"10.1016\/j.bbamem.2024.184289_bb0205","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1016\/0005-2795(81)90205-1","article-title":"Combined use of proton-proton Overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations","volume":"667","author":"Braun","year":"1981","journal-title":"Application to micelle-bound glucagon, Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2024.184289_bb0210","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1016\/S0022-2836(83)80143-0","article-title":"Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance","volume":"169","author":"Braun","year":"1983","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0215","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1002\/bip.20418","article-title":"NMR conformational analysis of proadrenomedullin N-terminal 20 peptide, a proangiogenic factor involved in tumor growth","volume":"81","author":"Lucyk","year":"2006","journal-title":"Biopolymers"},{"key":"10.1016\/j.bbamem.2024.184289_bb0220","first-page":"195","article-title":"Adhesion ability of angiotensin II with model membranes","volume":"2017","author":"Preu","year":"1859","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2024.184289_bb0225","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1139\/bcb-2018-0172","article-title":"Bicelle composition-dependent modulation of phospholipid dynamics by apelin peptides","volume":"97","author":"Sarker","year":"2019","journal-title":"Biochem. Cell Biol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0230","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pnmrs.2011.06.003","article-title":"Current applications of 19F NMR to studies of protein structure and dynamics","volume":"62","author":"Kitevski-LeBlanc","year":"2012","journal-title":"Prog. Nucl. Magn. Reson. Spectrosc."},{"key":"10.1016\/j.bbamem.2024.184289_bb0235","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/0079-6565(94)80009-X","article-title":"Fluorine NMR of proteins","volume":"26","author":"Gerig","year":"1994","journal-title":"Prog. Nucl. Magn. Reson. Spectrosc."},{"key":"10.1016\/j.bbamem.2024.184289_bb0240","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0014-5793(02)02577-2","article-title":"Placement of 19F into the center of GB1: effects on structure and stability","volume":"517","author":"Campos-Olivas","year":"2002","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbamem.2024.184289_bb0245","doi-asserted-by":"crossref","first-page":"1579","DOI":"10.1016\/S0006-3495(97)78190-6","article-title":"Effects of fluorine substitution on the structure and dynamics of complexes of dihydrofolate reductase (Escherichia coli)","volume":"73","author":"Lau","year":"1997","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2024.184289_bb0250","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1006\/jmbi.1998.1935","article-title":"Conformational changes in the crystal structure of rat glutathione transferase M1-1 with global substitution of 3-fluorotyrosine for tyrosine","volume":"281","author":"Xiao","year":"1998","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2024.184289_bb0255","doi-asserted-by":"crossref","first-page":"3048","DOI":"10.1021\/acs.biochem.6b00429","article-title":"Tracking transitions in spider wrapping silk conformation and dynamics by 19F nuclear magnetic resonance spectroscopy","volume":"55","author":"Sarker","year":"2016","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2024.184289_bb0260","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/s10858-010-9443-7","article-title":"Optimizing 19F NMR protein spectroscopy by fractional biosynthetic labeling","volume":"48","author":"Kitevski-LeBlanc","year":"2010","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.bbamem.2024.184289_bb0265","doi-asserted-by":"crossref","first-page":"3391","DOI":"10.1002\/chem.201705638","article-title":"Mixed fluorotryptophan substitutions at the same residue expand the versatility of 19F protein NMR spectroscopy","volume":"24","author":"Kenward","year":"2018","journal-title":"Chem. A Eur. J."},{"key":"10.1016\/j.bbamem.2024.184289_bb0270","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20153658","article-title":"Simultaneous ligand and receptor tracking through NMR spectroscopy enabled by distinct 19F labels","volume":"20","author":"Simmons","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbamem.2024.184289_bb0275","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1002\/cbic.202000601","article-title":"Self-organization properties of a GPCR-binding peptide with a fluorinated tail studied by fluorine NMR spectroscopy","volume":"22","author":"Jourdain de Muizon","year":"2021","journal-title":"Chembiochem"},{"key":"10.1016\/j.bbamem.2024.184289_bb0280","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1021\/acsptsci.2c00219","article-title":"Signaling modulation via minimal C-terminal modifications of apelin-13","volume":"6","author":"Theroux","year":"2023","journal-title":"ACS Pharmacol. Transl. Sci."},{"key":"10.1016\/j.bbamem.2024.184289_bb0285","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1096\/fj.201600784R","article-title":"Development of original metabolically stable apelin-17 analogs with diuretic and cardiovascular effects","volume":"31","author":"Gerbier","year":"2017","journal-title":"FASEB J."},{"key":"10.1016\/j.bbamem.2024.184289_bb0290","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1002\/cmdc.201100492","article-title":"Elucidation of the structure-activity relationships of apelin: influence of unnatural amino acids on binding, signaling, and plasma stability","volume":"7","author":"Murza","year":"2012","journal-title":"ChemMedChem"},{"key":"10.1016\/j.bbamem.2024.184289_bb0295","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1063\/1.1695690","article-title":"Spin diffusion measurements: spin echoes in the presence of a time-dependent field gradient","volume":"42","author":"Stejskal","year":"1965","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbamem.2024.184289_bb0300","doi-asserted-by":"crossref","first-page":"3139","DOI":"10.1021\/ja00034a071","article-title":"Diffusion-ordered two-dimensional nuclear magnetic resonance spectroscopy","volume":"114","author":"Morris","year":"1992","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbamem.2024.184289_bb0305","doi-asserted-by":"crossref","first-page":"1784","DOI":"10.1002\/(SICI)1521-3773(19990614)38:12<1784::AID-ANIE1784>3.0.CO;2-Q","article-title":"Characterization of ligand binding by saturation transfer difference NMR spectroscopy","volume":"38","author":"Mayer","year":"1999","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.bbamem.2024.184289_bb0310","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/magnetochemistry5010001","article-title":"Improved 19F{1H} saturation transfer difference experiments for sensitive detection to fluorinated compound bound to proteins","volume":"5","author":"Furihata","year":"2019","journal-title":"Magnetochemistry"},{"key":"10.1016\/j.bbamem.2024.184289_bb0315","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1016\/j.bbagen.2017.05.017","article-title":"Bioactivity of the putative apelin proprotein expands the repertoire of apelin receptor ligands","volume":"1861","author":"Shin","year":"2017","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2024.184289_bb0320","doi-asserted-by":"crossref","first-page":"2332","DOI":"10.1038\/nprot.2007.329","article-title":"Bicelle samples for solid-state NMR of membrane proteins","volume":"2","author":"De Angelis","year":"2007","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.bbamem.2024.184289_bb0325","doi-asserted-by":"crossref","first-page":"5445","DOI":"10.1021\/jf070337l","article-title":"Prediction of molar extinction coefficients of proteins and peptides using UV absorption of the constituent amino acids at 214 nm to enable quantitative reverse phase high-performance liquid chromatography\u2212mass spectrometry analysis","volume":"55","author":"Kuipers","year":"2007","journal-title":"J. Agr. Food Chem."},{"key":"10.1016\/j.bbamem.2024.184289_bb0330","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1006\/jmra.1995.1047","article-title":"Water suppression that works. Excitation sculpting using arbitrary wave-forms and pulsed-field gradients","volume":"112","author":"Hwang","year":"1995","journal-title":"J Magn Reson A"},{"key":"10.1016\/j.bbamem.2024.184289_bb0335","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1002\/mrc.2225","article-title":"Further conventions for NMR shielding and chemical shifts (IUPAC recommendations 2008)","volume":"46","author":"Harris","year":"2008","journal-title":"Magn. Reson. Chem."},{"key":"10.1016\/j.bbamem.2024.184289_bb0340","doi-asserted-by":"crossref","DOI":"10.1016\/j.jmr.2022.107357","article-title":"Deconvolution of 1D NMR spectra: a deep learning-based approach","volume":"347","author":"Schmid","year":"2023","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.bbamem.2024.184289_bb0345","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1006\/jmra.1995.1176","article-title":"An improved diffusion-ordered spectroscopy experiment incorporating bipolar-gradient pulses","volume":"115","author":"Wu","year":"1995","journal-title":"J. Magn. Reson. A"},{"key":"10.1016\/j.bbamem.2024.184289_bb0350","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1002\/bbpc.19840880112","article-title":"Diffusion in liquid mixtures of light and heavy water","volume":"88","author":"Weing\u00e4rtner","year":"1984","journal-title":"Ber. Bunsen. Phys. Chem"},{"key":"10.1016\/j.bbamem.2024.184289_bb0355","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.bbrc.2004.09.039","article-title":"Amantadine partition and localization in phospholipid membrane: a solution NMR study","volume":"324","author":"Wang","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamem.2024.184289_bb0360","first-page":"1494","article-title":"An NMR investigation of the structure, function and role of the hERG channel selectivity filter in the long QT syndrome","volume":"2013","author":"Gravel","year":"1828","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2024.184289_bb0365","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0005-2736(01)00358-3","article-title":"Morphology of fast-tumbling bicelles: a small angle neutron scattering and NMR study","volume":"1513","author":"Luchette","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2024.184289_bb0370","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.1016\/S0006-3495(04)74226-5","article-title":"A multidimensional 1H NMR investigation of the conformation of methionine-enkephalin in fast-tumbling bicelles","volume":"86","author":"Marcotte","year":"2004","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2024.184289_bb0375","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1021\/bi801864b","article-title":"Structural insight into G-protein coupled receptor binding by apelin","volume":"48","author":"Langelaan","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2024.184289_bb0380","doi-asserted-by":"crossref","first-page":"32627","DOI":"10.1074\/jbc.M110.127167","article-title":"By interacting with the C-terminal Phe of apelin, Phe255 and Trp259 in helix VI of the apelin receptor are critical for internalization","volume":"285","author":"Iturrioz","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2024.184289_bb0385","doi-asserted-by":"crossref","DOI":"10.1002\/pep2.24064","article-title":"Apelins, ELABELA, and their derivatives: Peptidic regulators of the cardiovascular system and beyond","volume":"111","author":"Murza","year":"2019","journal-title":"Pept. Sci."},{"key":"10.1016\/j.bbamem.2024.184289_bb0390","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1006\/jmrb.1996.0187","article-title":"Magnetically oriented phospholipid bilayered micelles for structural studies of polypeptides. Does the ideal bicelle exist?","volume":"113","author":"Vold","year":"1996","journal-title":"J. Magn. Reson. B"},{"key":"10.1016\/j.bbamem.2024.184289_bb0395","doi-asserted-by":"crossref","first-page":"8453","DOI":"10.1021\/bi060615u","article-title":"Current applications of bicelles in NMR studies of membrane-associated amphiphiles and proteins","volume":"45","author":"Prosser","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2024.184289_bb0400","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1023\/A:1008302110884","article-title":"Improved dilute bicelle solutions for high-resolution NMR of biological macromolecules","volume":"12","author":"Losonczi","year":"1998","journal-title":"J. Biomol. NMR"},{"key":"10.1016\/j.bbamem.2024.184289_bb0405","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/S0006-3495(00)76591-X","article-title":"Acidic phospholipid bicelles: A versatile model membrane system","volume":"78","author":"Struppe","year":"2000","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2024.184289_bb0410","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.jmr.2007.11.016","article-title":"Solid state 19F NMR parameters of fluorine-labeled amino acids. Part II: Aliphatic substituents","volume":"191","author":"Grage","year":"2008","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.bbamem.2024.184289_bb0415","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.jmr.2007.11.017","article-title":"Solid state 19F NMR parameters of fluorine-labeled amino acids. Part I: Aromatic substituents","volume":"191","author":"Durr","year":"2008","journal-title":"J. Magn. Reson."},{"key":"10.1016\/j.bbamem.2024.184289_bb0420","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1006\/bbrc.2001.6230","article-title":"Apelin (65\u201377) activates extracellular signal-regulated kinases via a PTX-sensitive G protein","volume":"290","author":"Masri","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbamem.2024.184289_bb0425","first-page":"1471","article-title":"Structural features of the apelin receptor N-terminal tail and first transmembrane segment implicated in ligand binding and receptor trafficking","volume":"2013","author":"Langelaan","year":"1828","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2024.184289_bb0430","doi-asserted-by":"crossref","first-page":"8868","DOI":"10.1073\/pnas.160259697","article-title":"Speeding molecular recognition by using the folding funnel: the fly-casting mechanism","volume":"97","author":"Shoemaker","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2024.184289_bb0435","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pnmrs.2013.02.001","article-title":"Using chemical shift perturbation to characterise ligand binding","volume":"73","author":"Williamson","year":"2013","journal-title":"Prog. Nucl. Magn. Reson. Spectrosc."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Biomembranes"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273624000208?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0005273624000208?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,3,1]],"date-time":"2025-03-01T05:07:05Z","timestamp":1740805625000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0005273624000208"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,3]]},"references-count":87,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2024,3]]}},"alternative-id":["S0005273624000208"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamem.2024.184289","relation":{},"ISSN":["0005-2736"],"issn-type":[{"type":"print","value":"0005-2736"}],"subject":[],"published":{"date-parts":[[2024,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Localized apelin-17 analogue-bicelle interactions as a facilitator of membrane-catalyzed receptor recognition and binding","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Biomembranes","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbamem.2024.184289","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"184289"}}