Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Abril Escamilla-Ayala"'
Autor:
Mariana Hernández-Elvira, Francisco Torres-Quiroz, Abril Escamilla-Ayala, Eunice Domínguez-Martin, Ricardo Escalante, Laura Kawasaki, Laura Ongay-Larios, Roberto Coria
Publikováno v:
Cells, Vol 7, Iss 8, p 106 (2018)
Eukaryotic cells have evolved signalling pathways that allow adaptation to harmful conditions that disrupt endoplasmic reticulum (ER) homeostasis. When the function of the ER is compromised in a condition known as ER stress, the cell triggers the unf
Externí odkaz:
https://doaj.org/article/7fa4ce6de3a4413faddcbff5a0745977
Autor:
Wim Annaert, Katleen Dillen, Randy Schekman, Ragna Sannerud, Bertrand Kleizen, Rosanne Wouters, David Demedts, Christine Michiels, Abril Escamilla Ayala, Wendy Vermeire
Publikováno v:
Journal of Cell Biology, 220(9), 1. Rockefeller University Press
γ-Secretase affects many physiological processes through targeting >100 substrates; malfunctioning links γ-secretase to cancer and Alzheimer's disease. The spatiotemporal regulation of its stoichiometric assembly remains unresolved. Fractionation,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09d9039d96590f096bfacb0662aeabdb
https://doi.org/10.1083/jcb.201911104
https://doi.org/10.1083/jcb.201911104
Autor:
Carlotta Borgarelli, Abril Escamilla-Ayala, Ludo Van Den Bosch, Wim M. De Borggraeve, Sebastian Munck, Ermal Ismalaj, Yvonne E. Klingl
Publikováno v:
Chemistry – A European Journal. 27
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc527b5466cadf67335091e5cd84c617
https://doi.org/10.1002/chem.202183461
https://doi.org/10.1002/chem.202183461
Autor:
Wendy Vermeire, Magali Mondin, Sebastian Munck, Hideaki Mizuno, Maximilian H. Ulbrich, Abril Escamilla-Ayala, Karin Poersch, Lucía Chávez-Gutiérrez, Ragna Sannerud, Wim Annaert, Laura Paparelli, Caroline Berlage, Marcelle Koenig
Publikováno v:
eLife, Vol 9 (2020)
eLife
eLife
γ-Secretase is a multi-subunit enzyme whose aberrant activity is associated with Alzheimer's disease and cancer. While its structure is atomically resolved, γ-secretase localization in the membrane in situ relies mostly on biochemical data. Here, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb60eef94cd0993f27e9cab1d10b8b1a
https://lirias.kuleuven.be/handle/123456789/663411
https://lirias.kuleuven.be/handle/123456789/663411
Autor:
Karin Poersch, Wim Annaert, Caroline Berlage, Wendy Vermeire, Magali Mondin, Hideaki Mizuno, Abril Escamilla-Ayala, Sebastian Munck, Laura Paparelli, Lucía Chávez-Gutiérrez, Ragna Sannerud, Maximilian H. Ulbrich, Marcelle Koenig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::74575fbe2372aacbbeadf0a291ffa4c4
https://doi.org/10.7554/elife.56679.sa2
https://doi.org/10.7554/elife.56679.sa2
Publikováno v:
Seminars in celldevelopmental biology. 105
γ-Secretase cleavage is essential for many biological processes and its dysregulation is linked to disease, including cancer and Alzheimer's disease. Therefore, understanding the regulation of its activity is of major importance to improve drug desi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e43c8b4928ba7886b518f061969384f5
https://pubmed.ncbi.nlm.nih.gov/32146031
https://pubmed.ncbi.nlm.nih.gov/32146031
Autor:
Francisco Torres-Quiroz, Mariana Hernández-Elvira, Roberto Coria, Abril Escamilla-Ayala, Eunice Domínguez-Martín, Ricardo Escalante, Laura Ongay-Larios, Laura Kawasaki
Publikováno v:
Cells, Vol 7, Iss 8, p 106 (2018)
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
Eukaryotic cells have evolved signalling pathways that allow adaptation to harmful conditions that disrupt endoplasmic reticulum (ER) homeostasis. When the function of the ER is compromised in a condition known as ER stress, the cell triggers the unf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd4119324ae3f8709b064ec7e8c0a043
http://www.mdpi.com/2073-4409/7/8/106
http://www.mdpi.com/2073-4409/7/8/106