A deep learning based method for left ventricular strain measurements: repeatability and accuracy compared to experienced echocardiographers

Autor: Magnus Rogstadkjernet, Sigurd Z. Zha, Lars G. Klæboe, Camilla K. Larsen, John M. Aalen, Esther Scheirlynck, Bjørn-Jostein Singstad, Steven Droogmans, Bernard Cosyns, Otto A. Smiseth, Kristina H. Haugaa, Thor Edvardsen, Eigil Samset, Pål H. Brekke

Publikováno v: BMC Medical Imaging, Vol 24, Iss 1, Pp 1-10 (2024)

Abstract Background Speckle tracking echocardiography (STE) provides quantification of left ventricular (LV) deformation and is useful in the assessment of LV function. STE is increasingly being used clinically, and every effort to simplify and stand

Externí odkaz: https://doaj.org/article/5d494022ecb341ab8768554221743f05

The covalent reactivity of functionalized 5-hydroxy-butyrolactams is the basis for targeting of fatty acid binding protein 5 (FABP5) by the neurotrophic agent MT-21

Autor: Esben B. Svenningsen, Rasmus N. Ottosen, Katrine H. Jørgensen, Marija Nisavic, Camilla K. Larsen, Bente K. Hansen, Yong Wang, Kresten Lindorff-Larsen, Thomas Tørring, Stephan M. Hacker, Johan Palmfeldt, Thomas B. Poulsen

Publikováno v: Svenningsen, E B, Ottosen, R N, Jørgensen, K H, Nisavic, M, Larsen, C K, Hansen, B K, Wang, Y, Lindorff-Larsen, K, Tørring, T, Hacker, S M, Palmfeldt, J & Poulsen, T B 2022, ' The covalent reactivity of functionalized 5-hydroxy-butyrolactams is the basis for targeting of fatty acid binding protein 5 (FABP5) by the neurotrophic agent MT-21 ', RSC Chemical Biology, vol. 3, no. 10, pp. 1216-1229 . https://doi.org/10.1039/d2cb00161f
RSC Chemical Biology, 3(10), 1216-1229. ROYAL SOC CHEMISTRY

Covalently acting compounds experience a strong interest within chemical biology both as molecular probes in studies of fundamental biological mechanisms and/or as novel drug candidates. In this context, the identification of new classes of reactive

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9a351c21acb8ea1a8fe4082e4a7f639
https://doi.org/10.1039/d2cb00161f

Structure and Function of the Bacterial Protein Toxin Phenomycin

Autor: Kristian M. Jacobsen, Esben B. Svenningsen, Rasmus K. Flygaard, Thomas B. Poulsen, Lasse Jenner, Ditlev E. Brodersen, Thomas Tørring, Jakob Nielsen, Camilla K. Larsen, Bente Krogh Hansen, Lan B. Van, Lene N. Nejsum, Frans A. A. Mulder, Morten Bjerring

Publikováno v: Structure
Structure, 2020, 28 (5), pp.528-539. ⟨10.1016/j.str.2020.03.003⟩
Hansen, B K, Larsen, C K, Nielsen, J T, Svenningsen, E B, Van, L B, Jacobsen, K M, Bjerring, M, Flygaard, R K, Jenner, L B, Nejsum, L N, Brodersen, D E, Mulder, F A A, Tørring, T & Poulsen, T B 2020, ' Structure and Function of the Bacterial Protein Toxin Phenomycin ', Structure, vol. 28, no. 5, pp. 528-539.e9 . https://doi.org/10.1016/j.str.2020.03.003

SummaryPhenomycin is a bacterial mini-protein of 89 amino acids discovered more than 50 years ago with toxicity in the nanomolar regime towards mammalian cells. The protein inhibits the function of the eukaryotic ribosome in cell free systems and app

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b66d48cdf32bd64ee96a20bcfec3b3a
https://doi.org/10.1016/j.str.2020.03.003