C
Christina Lyngsø
Researcher at National Research Foundation of South Africa
Publications - 8
Citations - 307
Christina Lyngsø is an academic researcher from National Research Foundation of South Africa. The author has contributed to research in topics: Angiotensin II & Receptor. The author has an hindex of 5, co-authored 8 publications receiving 283 citations. Previous affiliations of Christina Lyngsø include Glostrup Hospital & Copenhagen University Hospital.
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Journal ArticleDOI
Quantitative Phosphoproteomics Dissection of Seven-transmembrane Receptor Signaling Using Full and Biased Agonists
Gitte Lund Christensen,Gitte Lund Christensen,Gitte Lund Christensen,Christian D. Kelstrup,Christina Lyngsø,Christina Lyngsø,Uzma Sarwar,Rikke Bøgebo,Søren P. Sheikh,Steen Gammeltoft,Jesper V. Olsen,Jakob Lerche Hansen,Jakob Lerche Hansen +12 more
TL;DR: This study provides substantial novel insight into angiotensin II signal transduction and is the first study dissecting the differences between a full agonist and a biased agonist from a 7TMR on a systems-wide scale.
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Lack of Evidence for AT1R/B2R Heterodimerization in COS-7, HEK293, and NIH3T3 Cells HOW COMMON IS THE AT1R/B2R HETERODIMER?
Jakob Lerche Hansen,Jakob Lerche Hansen,Jonas Tind Hansen,Jonas Tind Hansen,Tobias Speerschneider,Tobias Speerschneider,Christina Lyngsø,Christina Lyngsø,Niels Erikstrup,Niels Erikstrup,Ethan S. Burstein,David M. Weiner,Thomas Walther,Noriko Makita,Taroh Iiri,Nicole Merten,Evi Kostenis,Søren P. Sheikh +17 more
TL;DR: The data collectively suggest that AT1R/B2R heterodimerization does not occur as a natural consequence of their simultaneous expression in the same cell nor does the B2R influence the At1R signaling.
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Functional interactions between 7TM receptors in the renin-angiotensin system--dimerization or crosstalk?
TL;DR: This review will present and critically discuss the current data on 7TM receptor dimerization with a clear focus on the RAS, and delineate future challenges within the field.
Journal ArticleDOI
Biased signaling of the angiotensin II type 1 receptor can be mediated through distinct mechanisms.
Marie Mi Bonde,Jonas Tind Hansen,Jonas Tind Hansen,Samra Joke Sanni,Stig Haunsø,Steen Gammeltoft,Christina Lyngsø,Christina Lyngsø,Jakob Lerche Hansen,Jakob Lerche Hansen +9 more
TL;DR: The analysis reveals that the underlying conformations induced by these AT1R mutants most likely represent principally different mechanisms of uncoupling the G protein, which for some mutants may be due to their increased ability to recruit β-arrestin2.
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The angiotensin II type 1 receptor antagonist Losartan binds and activates bradykinin B2 receptor signaling.
Marie Mi Bonde,Kristine Boisen Olsen,Niels Erikstrup,Niels Erikstrup,Tobias Speerschneider,Christina Lyngsø,Christina Lyngsø,Stig Haunsø,Morten Schak Nielsen,Søren P. Sheikh,Jakob Lerche Hansen,Jakob Lerche Hansen +11 more
TL;DR: Investigation of the ability of six clinically available ARBs to specifically bind and activate the B2R found that only Losartan activated the B1R, working as a partial agonist compared to the endogenous ligand bradykinin.