Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Chantal Brees"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1864:1833-1843
Accumulating evidence indicates that peroxisome functioning, catalase localization, and cellular oxidative balance are intimately interconnected. Nevertheless, it remains largely unclear why modest increases in the cellular redox state especially int
Autor:
Marcus Nordgren, Celien Lismont, Marc Fransen, Chantal Brees, Paul P. Van Veldhoven, Bernard Knoops
Publikováno v:
Antioxidantsredox signaling. 30(1)
AIMS: Peroxisomes are ubiquitous, single-membrane-bounded organelles that contain considerable amounts of enzymes involved in the production or breakdown of hydrogen peroxide (H2O2), a key signaling molecule in multiple biological processes and disea
Autor:
Marc, Fransen, Chantal, Brees
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1595
Many biological processes and cell fate decisions are modulated by changes in redox environment. To gain insight into how subcellular compartmentalization of reactive oxygen species (ROS) formation contributes to (site-specific) redox signaling and o
Autor:
Marc Fransen, Chantal Brees
Publikováno v:
Methods in Molecular Biology ISBN: 9781493969357
Many biological processes and cell fate decisions are modulated by changes in redox environment. To gain insight into how subcellular compartmentalization of reactive oxygen species (ROS) formation contributes to (site-specific) redox signaling and o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f71ff57e96ad8a90f446c6ea6fac742f
https://doi.org/10.1007/978-1-4939-6937-1_15
https://doi.org/10.1007/978-1-4939-6937-1_15
Autor:
Oksana Apanasets, Bo Wang, Patrizia Agostinis, Paul P. Van Veldhoven, Chantal Brees, Markus Kunze, N Rubio, Marc Fransen, Myriam Baes, Marcus Nordgren
Publikováno v:
Free Radical Biology and Medicine. 65:882-894
Many cellular processes are driven by spatially and temporally regulated redox-dependent signaling events. Although mounting evidence indicates that organelles such as the endoplasmic reticulum and mitochondria can function as signaling platforms for
Autor:
Marcus Nordgren, Oksana Apanasets, Gabriele Dodt, Bo Wang, Jorge E. Azevedo, Cláudia P. Grou, Marc Fransen, Paul P. Van Veldhoven, Chantal Brees
Publikováno v:
Traffic. 15:94-103
Peroxisome maintenance depends on the import of nuclear-encoded proteins from the cytosol. The vast majority of these proteins is destined for the peroxisomal lumen and contains a C-terminal peroxisomal targeting signal, called PTS1. This targeting s
Publikováno v:
Journal of Microscopy. 245:229-235
KillerRed, a bright red fluorescent protein, is a genetically encoded photosensitizer, which generates radicals and hydrogen peroxide upon green light illumination. The protein is a potentially powerful tool for selective light-induced protein inacti
Autor:
Chantal Brees, Ye Shih Ho, Marc Fransen, Stanley R. Terlecky, Oksana Ivashchenko, Paul P. Van Veldhoven
Publikováno v:
Molecular Biology of the Cell
Peroxisomes are capable of reactive oxygen species (ROS) generation, but their contribution to cellular redox balance is not well understood. This study demonstrates that peroxisomes and mitochondria functionally interact via ROS signaling, suggestin
Autor:
Guy P. Mannaerts, Marc Fransen, Georgyi V. Los, Chantal Brees, Sofie Huybrechts, Paul P. Van Veldhoven
Publikováno v:
Traffic. 10:1722-1733
Despite the identification and characterization of various proteins that are essential for peroxisome biogenesis, the origin and the turnover of peroxisomes are still unresolved critical issues. In this study, we used the HaloTag technology as a new
Autor:
Paul P. Van Veldhoven, Anja Rabijns, Andreas Hartig, Guy P. Mannaerts, Marc Fransen, Chantal Brees, Leen Amery
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1783:864-873
Tetratricopeptide (TPR)-domain proteins are involved in various cellular processes. The TPR domain is known to be responsible for interaction with other proteins commonly recognizing sequence motifs at the C-termini. One such TPR-protein, TRIP8b, was