Now showing items 1-4 of 4

  • Lunde, Ngoc Nguyen; Osoble, Nimo Mukhtar Mohamud; Dalmao-Fernandez, Andrea; Antobreh, Alfreda S.; Jafari, Abbas; Singh, Sachin; Nyman, Tuula Anneli; Rustan, Arild Christian; Solberg, Rigmor; Thoresen, G. Hege (Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2023)
    The interplay between skeletal muscle and bone is primarily mechanical; however, biochemical crosstalk by secreted mediators has recently gained increased attention. The aim of this study was to investigate metabolic effects ...
  • Gregersen, Ida; Michelsen, Annika; Lunde, Ngoc Nguyen; Åkerblom, Axel; Lakic, Tatevik G.; Skjelland, Mona; Skagen, Karolina Ryeng; Becker, Richard C.; Lindbäck, Johan; Himmelmann, Anders; Solberg, Rigmor; Johansen, Harald Thidemann; James, Stefan K.; Siegbahn, Agneta; Storey, Robert F.; Kontny, Frederic; Aukrust, Pål; Ueland, Thor; Wallentin, Lars; Halvorsen, Bente (Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2020)
    Background The cysteine protease legumain is increased in patients with atherosclerosis, but its causal role in atherogenesis and cardiovascular disease is still unclear. The aim of the study was to investigate the ...
  • Forbord, Karl Martin; Okla, Meshail; Lunde, Ngoc Nguyen; Bosnjak, Tatjana; Arnekleiv, Guro Lorvik; Hesselson, Daniel; Johansen, Harald Thidemann; Tang, Jonathan C.Y.; Kassem, Moustapha; Solberg, Rigmor; Jafari, Abbas (Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2023)
    Legumain is a lysosomal cysteine protease that has been implicated in an increasing amount of physiological and pathophysiological processes. However, the upstream mechanisms regulating the expression and function of ...
  • Solberg, Rigmor; Lunde, Ngoc Nguyen; Forbord, Karl Martin Frøseth; Okla, Meshail; Kassem, Moustapha; Jafari, Abbas (Journal article / Tidsskriftartikkel / PublishedVersion; Peer reviewed, 2022)
    The cysteine protease legumain (also known as asparaginyl endopeptidase or δ-secretase) is the only known mammalian asparaginyl endopeptidase and is primarily localized to the endolysosomal system, although it is also found ...