{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T01:17:46Z","timestamp":1760059066193,"version":"build-2065373602"},"reference-count":46,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2025,5,20]],"date-time":"2025-05-20T00:00:00Z","timestamp":1747699200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Natural Science Foundation of China","award":["80870309"],"award-info":[{"award-number":["80870309"]}]},{"name":"Fellows\u2019 Research Fund of Trinity College, Cambridge","award":["80870309"],"award-info":[{"award-number":["80870309"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["CIMB"],"abstract":"<jats:p>The central role of angiotensinogen in the control of blood pressure is revealed by a series of crystallographic structures, including complexes with renin. Specifically, the structures provide an understanding of the sequential molecular events that lead to the pre-eclamptic hypertensive crises of pregnancy. The release of the precursor vasopressor peptide from the amino-terminal tail of angiotensinogen appears to be modulated by a redox-sensitive disulphide bridge. Our findings indicate that the activation of the thiol-switch in the circulating maternal angiotensinogen occurs at the placental level in response to oxidative stress, exacerbated by placental insufficiency. We propose here that a contributory factor is the inherent redox stress accompanying the placental exchange of oxygenation between the haemoglobin of the mother (oxy-HbA) and the deoxygenated haemoglobin of the foetus (deoxy-HbF).<\/jats:p>","DOI":"10.3390\/cimb47050375","type":"journal-article","created":{"date-parts":[[2025,5,20]],"date-time":"2025-05-20T06:54:28Z","timestamp":1747724068000},"page":"375","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The Molecular Pathology of Pre-Eclamptic Hypertension"],"prefix":"10.3390","volume":"47","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6898-9319","authenticated-orcid":false,"given":"Robin W.","family":"Carrell","sequence":"first","affiliation":[{"name":"Department of Haematology, Cambridge Institute for Medical Research, Trinity College, University of Cambridge, Cambridge CB2 1TQ, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8273-0047","authenticated-orcid":false,"given":"Randy J.","family":"Read","sequence":"additional","affiliation":[{"name":"Department of Haematology, Cambridge Institute for Medical Research, Trinity College, University of Cambridge, Cambridge CB2 1TQ, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2555-5091","authenticated-orcid":false,"given":"Aiwu","family":"Zhou","sequence":"additional","affiliation":[{"name":"Department of Haematology, Cambridge Institute for Medical Research, Trinity College, University of Cambridge, Cambridge CB2 1TQ, UK"},{"name":"Institute for Translational Medicine on Cell Fate and Disease, Department of Pathophysiology, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2025,5,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1126\/science.6604942","article-title":"Angiotensinogen is related to the antitrypsin-antithrombin-ovalbumin family","volume":"222","author":"Doolittle","year":"1983","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"8951","DOI":"10.1021\/bi00449a001","article-title":"Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins","volume":"28","author":"Huber","year":"1989","journal-title":"Biochemistry"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1042\/bj2620103","article-title":"Ovalbumin and angiotensinogen lack serpin S-R conformational change","volume":"262","author":"Stein","year":"1989","journal-title":"Biochem. 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