Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Simone Schopper"'
Autor:
Gang Zhang, Thomas Kruse, Blanca López-Méndez, Kathrine Beck Sylvestersen, Dimitriya H. Garvanska, Simone Schopper, Michael Lund Nielsen, Jakob Nilsson
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
The spindle assembly checkpoint ensures correct chromosome segregation and relies on kinetochore localization of the Bub1 and Mad1/Mad2 checkpoint proteins. Here the authors show that main function of Bub1 is to position Mad1 close to KNL1 MELT repea
Externí odkaz:
https://doaj.org/article/443aced42d614c6d811e9ee26b08fd00
Autor:
Oliver Müller, Pascal Leuenberger, Simone Schopper, Ilaria Piazza, Paul J. Boersema, Abdullah Kahraman, Paola Picotti, Yuehan Feng
Publikováno v:
Nature Protocols, 12 (11)
Protein structural changes induced by external perturbations or internal cues can profoundly influence protein activity and thus modulate cellular physiology. A number of biophysical approaches are available to probe protein structural changes, but t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::600a01f3f6e076993706a6a926209081
https://doi.org/10.1038/nprot.2017.100
https://doi.org/10.1038/nprot.2017.100
Autor:
Wenya Hou, Britta Qualmann, Michael L. Nielsen, Michael M. Kessels, Sabine Nemitz, Simone Schopper
Publikováno v:
Developmental cell. 45(2)
The complex architecture of neuronal networks in the brain requires tight control of the actin cytoskeleton. The actin nucleator Cobl is critical for neuronal morphogenesis. Here we reveal that Cobl is controlled by arginine methylation. Coprecipitat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dccc8e0e3857df30d93abf835c625ff2
https://pubmed.ncbi.nlm.nih.gov/29689199
https://pubmed.ncbi.nlm.nih.gov/29689199
Autor:
Linda Hellborg, Carolin Sörensson, Simone Schopper, E Andreasson, Joerg Fettke, Susanne Widell, P Mühlenbock, Marit Lenman
Publikováno v:
Plant Biology. 17:74-80
Arabidopsis thaliana has two isoforms of alpha-glycan phosphorylase (EC 2.4.1.1), one residing in the plastid and the other in the cytosol. The cytosolic phosphorylase, PHS2, acts on soluble heteroglycans that constitute a part of the carbohydrate po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a9b7aaa30473121c54ff1ee333d914b
https://doi.org/10.1111/plb.12190
https://doi.org/10.1111/plb.12190