{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,7]],"date-time":"2026-07-07T01:10:56Z","timestamp":1783386656233,"version":"3.54.6"},"reference-count":42,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,10,1]],"date-time":"2017-10-01T00:00:00Z","timestamp":1506816000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001864","name":"Ministry of Education and Science, Republic of Latvia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001864","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003081","name":"Ministry of Education, Ethiopia","doi-asserted-by":"publisher","award":["III 46009"],"award-info":[{"award-number":["III 46009"]}],"id":[{"id":"10.13039\/501100003081","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000032","name":"Institute of Infection and Immunity","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000032","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.fr","clinicalkey.jp","clinicalkey.es","clinicalkey.com.au","clinicalkey.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Nutrition Research"],"published-print":{"date-parts":[[2017,10]]},"DOI":"10.1016\/j.nutres.2017.07.009","type":"journal-article","created":{"date-parts":[[2017,7,28]],"date-time":"2017-07-28T07:16:14Z","timestamp":1501226174000},"page":"22-30","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":36,"special_numbering":"C","title":["In silico identification of milk antihypertensive di- and tripeptides involved in angiotensin I\u2013converting enzyme inhibitory activity"],"prefix":"10.1016","volume":"46","author":[{"given":"Vladimir R.","family":"Vukic","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dajana V.","family":"Vukic","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Spasenija D.","family":"Milanovic","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mirela D.","family":"Ilicic","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katarina G.","family":"Kanuric","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mark S.","family":"Johnson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.nutres.2017.07.009_bb0005","doi-asserted-by":"crossref","first-page":"1170","DOI":"10.1038\/ajh.2010.172","article-title":"Obesity-related hypertension: epidemiology, pathophysiology, and clinical management","volume":"23","author":"Kotchen","year":"2010","journal-title":"Am J Hypertens"},{"issue":"Pt 1","key":"10.1016\/j.nutres.2017.07.009_bb0010","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1042\/bj2900205","article-title":"Evolutionary families of peptidases","volume":"290","author":"Rawlings","year":"1993","journal-title":"Biochem J"},{"key":"10.1016\/j.nutres.2017.07.009_bb0015","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1161\/HYPERTENSIONAHA.107.097865","article-title":"Angiotensin-converting enzyme C-terminal catalytic domain is the main site of angiotensin I cleavage in vivo","volume":"51","author":"Fuchs","year":"2008","journal-title":"Hypertension"},{"key":"10.1016\/j.nutres.2017.07.009_bb0020","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1161\/01.HYP.0000151323.93372.f5","article-title":"Selective angiotensin-converting enzyme C-domain inhibition is sufficient to prevent angiotensin I\u2013induced vasoconstriction","volume":"45","author":"van Esch","year":"2005","journal-title":"Hypertension"},{"key":"10.1016\/j.nutres.2017.07.009_bb0025","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1016\/S1357-2725(02)00309-6","article-title":"The angiotensin converting enzyme (ACE)","volume":"35","author":"Coates","year":"2003","journal-title":"Int J Biochem Cell Biol"},{"key":"10.1016\/j.nutres.2017.07.009_bb0030","doi-asserted-by":"crossref","first-page":"407","DOI":"10.2174\/0929866043406481","article-title":"The zinc metallopeptidase family: new facts, new functions","volume":"11","author":"Lew","year":"2004","journal-title":"Protein Pept Lett"},{"key":"10.1016\/j.nutres.2017.07.009_bb0035","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1038\/nrd1227","article-title":"ACE revisited: a new target for structure-based drug design","volume":"2","author":"Acharya","year":"2003","journal-title":"Nat Rev Drug Discov"},{"key":"10.1016\/j.nutres.2017.07.009_bb0040","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1038\/nature01370","article-title":"Crystal structure of the human angiotensin-converting enzyme-lisinopril complex","volume":"421","author":"Natesh","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.nutres.2017.07.009_bb0045","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1038\/srep00717","article-title":"Molecular recognition and regulation of human angiotensin-I converting enzyme (ACE) activity by natural inhibitory peptides","volume":"2","author":"Masuyer","year":"2012","journal-title":"Sci Rep"},{"key":"10.1016\/j.nutres.2017.07.009_bb0050","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1146\/annurev.bi.45.070176.000445","article-title":"Angiotensin-converting enzyme and the regulation of vasoactive peptides","volume":"45","author":"Soffer","year":"1976","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.nutres.2017.07.009_bb0055","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1016\/0005-2744(73)90352-5","article-title":"Inhibition of homogeneous angiotensin-converting enzyme of rabbit lung by synthetic venom peptides of Bothrops jararaca","volume":"293","author":"Cheung","year":"1973","journal-title":"Biochim Biophys Acta (BBA) - Enzymology"},{"key":"10.1016\/j.nutres.2017.07.009_bb0060","doi-asserted-by":"crossref","first-page":"1032","DOI":"10.1007\/BF01930447","article-title":"Inhibition of angiotensin-converting enzyme by analogs of peptides from Bothrops jararaca venom","volume":"29","author":"Cushman","year":"1973","journal-title":"Experientia"},{"key":"10.1016\/j.nutres.2017.07.009_bb0065","doi-asserted-by":"crossref","first-page":"1034","DOI":"10.1096\/fj.06-0602ufm","article-title":"The ACE and I: how ACE inhibitors came to be","volume":"20","author":"Erd\u00f6s","year":"2006","journal-title":"FASEB J"},{"key":"10.1016\/j.nutres.2017.07.009_bb0070","doi-asserted-by":"crossref","first-page":"9496","DOI":"10.1016\/S0021-9258(18)98378-X","article-title":"Differences in the properties and enzymatic specificities of the two active sites of angiotensin I\u2013converting enzyme (kininase II). Studies with bradykinin and other natural peptides","volume":"268","author":"Jaspard","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1016\/j.nutres.2017.07.009_bb0075","doi-asserted-by":"crossref","first-page":"5473","DOI":"10.1021\/bi700275e","article-title":"The structure of testis angiotensin-converting enzyme in complex with the C domain-specific inhibitor RXPA380","volume":"46","author":"Corradi","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.nutres.2017.07.009_bb0080","doi-asserted-by":"crossref","first-page":"8405","DOI":"10.1021\/bi9011226","article-title":"Investigating the domain specificity of phosphinic inhibitors RXPA380 and RXP407 in angiotensin-converting enzyme","volume":"48","author":"Kroger","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.nutres.2017.07.009_bb0085","doi-asserted-by":"crossref","first-page":"980S","DOI":"10.1093\/jn\/134.4.980S","article-title":"Hypotensive peptides from milk proteins","volume":"134","author":"FritzGerald","year":"2004","journal-title":"J Nutr"},{"key":"10.1016\/j.nutres.2017.07.009_bb0090","first-page":"441","article-title":"Animal and plant origin proteins as the precursors of peptides with ACE inhibitory activity. Proteins evaluation by means of in silico methods","volume":"47","author":"Iwaniak","year":"2009","journal-title":"Food Technol Biotechnol"},{"key":"10.1016\/j.nutres.2017.07.009_bb0095","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1111\/1541-4337.12051","article-title":"Food-originating ACE inhibitors, including antihypertensive peptides, as preventive food components in blood pressure reduction","volume":"13","author":"Iwaniak","year":"2014","journal-title":"Compr Rev Food Sci Food Saf"},{"key":"10.1016\/j.nutres.2017.07.009_bb0100","article-title":"Effect of peptides derived from food proteins on blood pressure: a meta-analysis of randomized controlled trials","volume":"52","author":"Pripp","year":"2008","journal-title":"Food Nutr Res"},{"key":"10.1016\/j.nutres.2017.07.009_bb0105","doi-asserted-by":"crossref","first-page":"315","DOI":"10.4081\/ijas.2009.315","article-title":"Bioactive peptides in dairy products","volume":"8","author":"Tidona","year":"2009","journal-title":"Ital J Anim Sci"},{"key":"10.1016\/j.nutres.2017.07.009_bb0110","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1016\/S0271-5317(04)00058-2","article-title":"Angiotensin I\u2013converting enzyme inhibitory peptides derived from food proteins and their physiological and pharmacological effects","volume":"24","author":"Li","year":"2004","journal-title":"Nutr Res"},{"key":"10.1016\/j.nutres.2017.07.009_bb0115","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.chroma.2006.03.006","article-title":"Effect of beta-lactoglobulin hydrolysis with thermolysin under denaturing temperatures on the release of bioactive peptides","volume":"1116","author":"Hern\u00e1ndez-Ledesma","year":"2006","journal-title":"J Chromatogr A"},{"key":"10.1016\/j.nutres.2017.07.009_bb0120","doi-asserted-by":"crossref","first-page":"4977","DOI":"10.1021\/jm4004285","article-title":"QSAR modeling: where have you been? Where are you going to?","volume":"57","author":"Cherkasov","year":"2014","journal-title":"J Med Chem"},{"key":"10.1016\/j.nutres.2017.07.009_bb0125","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1080\/1062936X.2016.1167774","article-title":"Development of a credible 3D-QSAR CoMSIA model and docking studies for a series of triazoles and tetrazoles containing 11\u03b2-HSD1 inhibitors","volume":"27","author":"Murumkar","year":"2016","journal-title":"SAR QSAR Environ Res"},{"key":"10.1016\/j.nutres.2017.07.009_bb0130","doi-asserted-by":"crossref","first-page":"965","DOI":"10.1093\/jaoac\/91.4.965","article-title":"BIOPEP database and other programs for processing bioactive peptide sequences","volume":"91","author":"Minkiewicz","year":"2008","journal-title":"J AOAC Int"},{"key":"10.1016\/j.nutres.2017.07.009_bb0135","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1186\/1758-2946-3-33","article-title":"Open babel: an open chemical toolbox","volume":"3","author":"O'Boyle","year":"2011","journal-title":"J Chem"},{"key":"10.1016\/j.nutres.2017.07.009_bb0140","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1002\/(SICI)1096-987X(199604)17:5\/6<587::AID-JCC4>3.0.CO;2-Q","article-title":"Merck molecular force field. IV. Conformational energies and geometries for MMFF94","volume":"17","author":"Halgren","year":"1996","journal-title":"J Comput Chem"},{"key":"10.1016\/j.nutres.2017.07.009_bb0145","doi-asserted-by":"crossref","first-page":"8101","DOI":"10.1021\/jf071031h","article-title":"Quantitative structure-activity relationship of rubiscolin analogues as \u03b4 opioid peptides using comparative molecular field analysis (CoMFA) and comparative molecular similarity indices analysis (CoMSIA)","volume":"55","author":"Caballero","year":"2007","journal-title":"J Agric Food Chem"},{"key":"10.1016\/j.nutres.2017.07.009_bb0150","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1021\/jm020406h","article-title":"Surflex: fully automatic flexible molecular docking using a molecular similarity-based search engine","volume":"46","author":"Jain","year":"2003","journal-title":"J Med Chem"},{"key":"10.1016\/j.nutres.2017.07.009_bb0155","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1007\/s10822-011-9495-0","article-title":"The inevitable QSAR renaissance","volume":"26","author":"Cramer","year":"2012","journal-title":"J Comput Aided Mol Des"},{"key":"10.1016\/j.nutres.2017.07.009_bb0160","doi-asserted-by":"crossref","first-page":"4130","DOI":"10.1021\/jm00050a010","article-title":"Molecular similarity indices in a comparative analysis (CoMSIA) of drug molecules to correlate and predict their biological activity","volume":"37","author":"Klebe","year":"1994","journal-title":"J Med Chem"},{"key":"10.1016\/j.nutres.2017.07.009_bb0165","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1023\/A:1008047919606","article-title":"Comparative molecular similarity index analysis (CoMSIA) to study hydrogen-bonding properties and to score combinatorial libraries","volume":"13","author":"Klebe","year":"1999","journal-title":"J Comput Aided Mol Des"},{"key":"10.1016\/j.nutres.2017.07.009_bb0170","doi-asserted-by":"crossref","first-page":"5959","DOI":"10.1021\/ja00226a005","article-title":"Comparative molecular field analysis (CoMFA). 1. Effect of shape on binding of steroids to carrier proteins","volume":"110","author":"Cramer","year":"1988","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.nutres.2017.07.009_bb0175","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1007\/BF00124364","article-title":"Sample-distance partial least squares: PLS optimized for many variables, with application to CoMFA","volume":"7","author":"Bush","year":"1993","journal-title":"J Comput Aided Mol Des"},{"key":"10.1016\/j.nutres.2017.07.009_bb0180","doi-asserted-by":"crossref","first-page":"1407","DOI":"10.1021\/ci010368v","article-title":"Prediction of n-octanol\/water partition coefficients from PHYSPROP database using artificial neural networks and E-state indices","volume":"41","author":"Tetko","year":"2001","journal-title":"J Chem Inf Comput Sci"},{"key":"10.1016\/j.nutres.2017.07.009_bb0185","article-title":"Effects of tryptophan-containing peptides on angiotensin-converting enzyme activity and vessel tone ex vivo and in vivo","author":"Khedr","year":"2017","journal-title":"Eur J Nutr"},{"key":"10.1016\/j.nutres.2017.07.009_bb0190","doi-asserted-by":"crossref","first-page":"7219","DOI":"10.1016\/j.bmcl.2011.09.107","article-title":"3D-QSAR and molecular docking studies of 2-pyrimidinecarbonitrile derivatives as inhibitors against falcipain-3","volume":"21","author":"Potshangbam","year":"2011","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.nutres.2017.07.009_bb0195","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1023\/A:1018982505021","article-title":"Intestinal peptide transport systems and oral drug availability","volume":"16","author":"Yang","year":"1999","journal-title":"Pharm Res"},{"key":"10.1016\/j.nutres.2017.07.009_bb0200","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1271\/bbb.66.378","article-title":"Transepithelial transport of the bioactive tripeptide, Val-Pro-Pro, in human intestinal Caco-2 cell monolayers","volume":"66","author":"Satake","year":"2002","journal-title":"Biosci Biotechnol Biochem"},{"key":"10.1016\/j.nutres.2017.07.009_bb0205","doi-asserted-by":"crossref","first-page":"3063","DOI":"10.1093\/jn\/126.12.3063","article-title":"Antihypertensive peptides are present in aorta after oral administration of sour milk containing these peptides to spontaneously hypertensive rats","volume":"126","author":"Masuda","year":"1996","journal-title":"J Nutr"},{"key":"10.1016\/j.nutres.2017.07.009_bb0210","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1021\/js960085v","article-title":"Physicochemical and physiological mechanisms for the effects of food on drug absorption: the role of lipids and pH","volume":"86","author":"Charman","year":"1997","journal-title":"J Pharm Sci"}],"container-title":["Nutrition Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0271531717301446?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0271531717301446?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,6,27]],"date-time":"2022-06-27T02:21:52Z","timestamp":1656296512000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0271531717301446"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,10]]},"references-count":42,"alternative-id":["S0271531717301446"],"URL":"https:\/\/doi.org\/10.1016\/j.nutres.2017.07.009","relation":{},"ISSN":["0271-5317"],"issn-type":[{"value":"0271-5317","type":"print"}],"subject":[],"published":{"date-parts":[[2017,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"In silico identification of milk antihypertensive di- and tripeptides involved in angiotensin I\u2013converting enzyme inhibitory activity","name":"articletitle","label":"Article Title"},{"value":"Nutrition Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.nutres.2017.07.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}