Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Kathrin Gundel"'
Autor:
Jianmin Yin, Niels Schellinx, Ludovico Maggi, Kathrin Gundel, Cora Wiesner, Maria Paraskevi Kotini, Minkyoung Lee, Li-Kun Phng, Heinz-Georg Belting, Markus Affolter
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-18 (2024)
Abstract De novo lumen formation necessitates the precise segregation of junctional proteins from apical surfaces, yet the underlying mechanisms remain unclear. Using a zebrafish model, we develop a series of molecular reporters, photo-convertible an
Externí odkaz:
https://doaj.org/article/cac7d75bd81e4deaae5f1a4918d65a3d
Autor:
Aneliya Antonova, Barbara Hummel, Ashkan Khavaran, Desiree M. Redhaber, Fernando Aprile-Garcia, Prashant Rawat, Kathrin Gundel, Megan Schneck, Erik C. Hansen, Jan Mitschke, Gerhard Mittler, Cornelius Miething, Ritwick Sawarkar
Publikováno v:
Cell Reports, Vol 29, Iss 6, Pp 1645-1659.e9 (2019)
Summary: Molecular chaperones such as heat-shock proteins (HSPs) help in protein folding. Their function in the cytosol has been well studied. Notably, chaperones are also present in the nucleus, a compartment where proteins enter after completing de
Externí odkaz:
https://doaj.org/article/b0e8519e759d44d6bd040867ed687809
Autor:
Desiree M. Redhaber, Ritwick Sawarkar, Fernando Aprile-Garcia, Prashant Rawat, Jan Mitschke, Megan Schneck, Kathrin Gundel, Gerhard Mittler, Ashkan Khavaran, Barbara Hummel, Erik C Hansen, Cornelius Miething, Aneliya Antonova
Publikováno v:
Cell Reports
Cell Reports, Vol 29, Iss 6, Pp 1645-1659.e9 (2019)
Cell Reports, Vol 29, Iss 6, Pp 1645-1659.e9 (2019)
Summary: Molecular chaperones such as heat-shock proteins (HSPs) help in protein folding. Their function in the cytosol has been well studied. Notably, chaperones are also present in the nucleus, a compartment where proteins enter after completing de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0d1116d5c60acc6e4600fc077d84831
https://pubmed.ncbi.nlm.nih.gov/31693902
https://pubmed.ncbi.nlm.nih.gov/31693902