Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Ivan Bradić"'
Autor:
Ivan Bradić, Nemanja Vujić, Katharina B. Kuentzel, Hansjörg Habisch, Anita Pirchheim, Alena Akhmetshina, John D. Henderson, Tobias Madl, Atul S. Deshmukh, Dagmar Kratky
Publikováno v:
Gastro Hep Advances, Vol 3, Iss 6, Pp 711-723 (2024)
Background and Aims: Recent studies showed that patients suffering from lysosomal acid lipase deficiency (LAL-D) benefit from enzyme replacement therapy; however, liver histopathology improved in some but not all patients. We hypothesized that the pa
Externí odkaz:
https://doaj.org/article/3e7a6a2f5f9348cc9a94f0aba394ad76
Autor:
Alena Akhmetshina, Valentina Bianco, Ivan Bradić, Melanie Korbelius, Anita Pirchheim, Katharina B. Kuentzel, Thomas O. Eichmann, Helga Hinteregger, Dagmar Kolb, Hansjoerg Habisch, Laura Liesinger, Tobias Madl, Wolfgang Sattler, Branislav Radović, Simon Sedej, Ruth Birner-Gruenberger, Nemanja Vujić, Dagmar Kratky
Publikováno v:
Molecular Metabolism, Vol 79, Iss , Pp 101869- (2024)
Objective: Lysosomal acid lipase (LAL) is the only enzyme known to hydrolyze cholesteryl esters (CE) and triacylglycerols in lysosomes at an acidic pH. Despite the importance of lysosomal hydrolysis in skeletal muscle (SM), research in this area is l
Externí odkaz:
https://doaj.org/article/121b95e681f74b8e83bd5774d9dcc210
Autor:
Ivan Bradić, Laura Liesinger, Katharina B. Kuentzel, Nemanja Vujić, Michael Trauner, Ruth Birner-Gruenberger, Dagmar Kratky
Publikováno v:
Journal of Lipid Research, Vol 64, Iss 9, Pp 100427- (2023)
Lysosomal acid lipase (LAL) is the sole lysosomal enzyme responsible for the degradation of cholesteryl esters and triacylglycerols at acidic pH. Impaired LAL activity leads to LAL deficiency (LAL-D), a severe and fatal disease characterized by ectop
Externí odkaz:
https://doaj.org/article/cec401c7277a49c99853dc84748bd3d0
Autor:
Ivan Bradić, Katharina B. Kuentzel, Sophie Honeder, Gernot F. Grabner, Nemanja Vujić, Robert Zimmermann, Ruth Birner-Gruenberger, Dagmar Kratky
Publikováno v:
Molecular Metabolism, Vol 61, Iss , Pp 101510- (2022)
Objectives: Lysosomal acid lipase (LAL) is the key enzyme, which degrades neutral lipids at an acidic pH in lysosomes. The role of LAL in various cellular processes has mostly been studied in LAL-knockout mice, which share phenotypical characteristic
Externí odkaz:
https://doaj.org/article/9e9a94ef33d94480bffc59576b063088
Publikováno v:
Trends Mol Med
Lysosomal acid lipase (LAL) is the sole enzyme known to degrade neutral lipids in the lysosome. Mutations in the LAL-encoding LIPA gene lead to rare lysosomal lipid storage disorders with complete or partial absence of LAL activity. This review discu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5510d8b7e199b32cb7e3afb2e6924c0
https://doi.org/10.1016/j.molmed.2023.03.001
https://doi.org/10.1016/j.molmed.2023.03.001
Autor:
Madeleine Goeritzer, Katharina B. Kuentzel, Sarah Beck, Melanie Korbelius, Silvia Rainer, Ivan Bradić, Dagmar Kolb, Marion Mussbacher, Waltraud C. Schrottmaier, Alice Assinger, Axel Schlagenhauf, René Rost, Benjamin Gottschalk, Thomas O. Eichmann, Thomas Züllig, Wolfgang F. Graier, Nemanja Vujić, Dagmar Kratky
Publikováno v:
International Journal of Molecular Sciences
Volume 24
Issue 4
Pages: 3116
Volume 24
Issue 4
Pages: 3116
Monoglyceride lipase (MGL) hydrolyzes monoacylglycerols (MG) to glycerol and one fatty acid. Among the various MG species, MGL also degrades 2-arachidonoylglycerol, the most abundant endocannabinoid and potent activator of the cannabinoid receptors 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::803dc69bbbfad07922e3c49a12aa3c1e
Autor:
Katharina B. Kuentzel, Ivan Bradić, Zala N. Mihalič, Melanie Korbelius, Silvia Rainer, Anita Pirchheim, Julia Kargl, Dagmar Kratky
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 20; Pages: 12286
Advanced maternal age and obesity are the main risk factors to develop gestational diabetes mellitus (GDM). Obesity is a consequence of the increased storage of triacylglycerol (TG). Cytosolic and lysosomal lipid hydrolases break down TG and choleste
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::856da1524bd2d5949ae112c4c160b378
https://pubmed.ncbi.nlm.nih.gov/36293139
https://pubmed.ncbi.nlm.nih.gov/36293139
Autor:
Katharina B. Kuentzel, Ivan Bradić, Alena Akhmetshina, Melanie Korbelius, Silvia Rainer, Dagmar Kolb, Martin Gauster, Nemanja Vujić, Dagmar Kratky
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 19
International Journal of Molecular Sciences, Vol 22, Iss 10416, p 10416 (2021)
Volume 22
Issue 19
International Journal of Molecular Sciences, Vol 22, Iss 10416, p 10416 (2021)
Cholesterol and fatty acids are essential lipids that are critical for membrane biosynthesis and fetal organ development. Cholesteryl esters (CE) are degraded by hormone-sensitive lipase (HSL) in the cytosol and by lysosomal acid lipase (LAL) in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::f9c0a8ba2d2da59959d1ab539dd65bff
https://pubmed.ncbi.nlm.nih.gov/34638755
https://pubmed.ncbi.nlm.nih.gov/34638755
Autor:
Nemanja Vujic, Dagmar Kratky, Ivan Bradić, Madeleine Goeritzer, Katharina B. Kuentzel, Silvia Rainer, Branislav Radovic
Publikováno v:
Autophagy
article-version (VoR) Version of Record
article-version (VoR) Version of Record
Thioglycolate-elicited macrophages exhibit abundant conjugation of LC3 with PE (LC3-II). Among other autophagy-related (ATG) proteins, it is proposed that, like in yeast, both ATG5 and ATG7 are essential for LC3 conjugation. Using atg5-deficient (�
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9059204bb7bc1ce8b5a3b2ea3b55d0e2
Autor:
Nemanja Vujic, Martin Gauster, Melanie Korbelius, Katharina B. Kuentzel, Christian Wadsack, Ivan Bradić, Dagmar Kratky
Publikováno v:
Placenta. 112:e73
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b3edeaacb72f6fab30c29031d88b5719
https://doi.org/10.1016/j.placenta.2021.07.236
https://doi.org/10.1016/j.placenta.2021.07.236