Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Marion Weber-Boyvat"'
Autor:
Gülçin Vardar, Andrea Salazar-Lázaro, Marisa Brockmann, Marion Weber-Boyvat, Sina Zobel, Victor Wumbor-Apin Kumbol, Thorsten Trimbuch, Christian Rosenmund
Publikováno v:
eLife, Vol 10 (2021)
Syntaxin-1 (STX1) and Munc18-1 are two requisite components of synaptic vesicular release machinery, so much so synaptic transmission cannot proceed in their absence. They form a tight complex through two major binding modes: through STX1’s N-pepti
Externí odkaz:
https://doaj.org/article/55b4807767164058a2892123920a2a74
Funding Information: We thank Marisa Brockmann and Gülcin Vardar for initial help with SynGCamp6f imaging and electrophysiology, respectively. We thank Katja Pötschke, Bettina Brokowski, Heike Lerch, Nadine Albrecht-Koepke, and Berit Söhl-Kielczyn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3b8ac34c0cbb690db9fe643be3fb408
http://hdl.handle.net/10138/354844
http://hdl.handle.net/10138/354844
Autor:
Huanzhao Chen, Chen Lu, Yuhui Tan, Marion Weber-Boyvat, Jie Zheng, Mengyang Xu, Jie Xiao, Shuang Liu, Zhiquan Tang, Chaofeng Lai, Mingchuan Li, Vesa M. Olkkonen, Daoguang Yan, Wenbin Zhong
Publikováno v:
Journal of Biological Chemistry. :104812
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7ffcca59b612a4daa0bbfaf63d41b4f5
https://doi.org/10.1016/j.jbc.2023.104812
https://doi.org/10.1016/j.jbc.2023.104812
Autor:
Christian Rosenmund, Victor Wumbor-Apin Kumbol, Marion Weber-Boyvat, Marisa M Brockmann, Gülçin Vardar, Thorsten Trimbuch, Sina Zobel, Andrea Salazar-Lázaro
Publikováno v:
eLife, Vol 10 (2021)
eLife
eLife
Syntaxin-1 (STX1) and Munc18-1 are two requisite components of synaptic vesicular release machinery, so much so synaptic transmission cannot proceed in their absence. They form a tight binary complex through two major binding modes: one through STX1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07522c4f932c889baf77018a7d815210
https://doi.org/10.7554/elife.69498
https://doi.org/10.7554/elife.69498
Autor:
Victor Wumbor-Apin Kumbol, Marion Weber-Boyvat, Gülçin Vardar, Marisa M Brockmann, Christian Rosenmund, Thorsten Trimbuch, Andrea Salazar-Lázaro, Sina Zobel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5dee9fac003dee381adcd35c2f829374
https://doi.org/10.7554/elife.69498.sa2
https://doi.org/10.7554/elife.69498.sa2
Autor:
Jussi Jäntti, Vesa M. Olkkonen, Saundarya Shah, Marion Weber-Boyvat, Thorsten Trimbuch, Christian Rosenmund
Publikováno v:
Weber-Boyvat, M, Trimbuch, T, Shah, S, Jäntti, J, Olkkonen, V M & Rosenmund, C 2021, ' ORP/Osh mediate cross-talk between ER-plasma membrane contact site components and plasma membrane SNAREs ', Cellular and Molecular Life Sciences, vol. 78, no. 4, pp. 1689-1708 . https://doi.org/10.1007/s00018-020-03604-w
Cellular and Molecular Life Sciences
Cellular and Molecular Life Sciences
OSBP-homologous proteins (ORPs, Oshp) are lipid binding/transfer proteins. Several ORP/Oshp localize to membrane contacts between the endoplasmic reticulum (ER) and the plasma membrane, where they mediate lipid transfer or regulate lipid-modifying en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72e4c51d1f1484f7fe77e72bc891cd99
http://hdl.handle.net/10138/333095
http://hdl.handle.net/10138/333095
Autor:
Marion Weber-Boyvat, Jussi Jäntti, Vesa M. Olkkonen, Gerd Wohlfahrt, Nina Aro, Konstantin G. Chernov
Publikováno v:
Traffic. 17:131-153
The Sec1/Munc18 (SM) proteins constitute a conserved family with essential functions in SNARE-mediated membrane fusion. Recently, a new protein-protein interaction site in Sec1p, designated the groove, was proposed. Here, we show that a sec1 groove m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0741de383690ede3d051783f96d0c18c
https://doi.org/10.1111/tra.12349
https://doi.org/10.1111/tra.12349
Publikováno v:
Steroids. 99:248-258
Oxysterol-binding protein (OSBP) and its homologues (ORPs) are lipid-binding/transfer proteins with affinity for oxysterols, cholesterol and glycerophospholipids. In addition to a ligand-binding domain, a majority of the ORPs carry a pleckstrin homol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9710283b3b33b6c16c895adae0619ff7
https://doi.org/10.1016/j.steroids.2015.01.027
https://doi.org/10.1016/j.steroids.2015.01.027
Autor:
Johanna Ivaska, Johan Peränen, Henriikka Kentala, You Zhou, Raisa Hanninen, Terhi Vihervaara, Johanna Lilja, Vesa M. Olkkonen, Tuula A. Nyman, Marion Weber-Boyvat
Publikováno v:
Experimental Cell Research. 331(2):278-291
ORP3 is an R-Ras interacting oxysterol-binding protein homolog that regulates cell adhesion and is overexpressed in several cancers. We investigated here a novel function of ORP3 dependent on its targeting to both the endoplasmic reticulum (ER) and t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6ce75acab894213744fd51d8cc66c96
http://juuli.fi/Record/0006572015
http://juuli.fi/Record/0006572015
Publikováno v:
Cellular and Molecular Life Sciences. 72:1967-1987
Oxysterol-binding protein/OSBP-related proteins (ORPs) constitute a conserved family of sterol/phospholipid-binding proteins with lipid transporter or sensor functions. We investigated the spatial occurrence and regulation of the interactions of huma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0544258ca66f163c3d3f19fdfb151881
https://doi.org/10.1007/s00018-014-1786-x
https://doi.org/10.1007/s00018-014-1786-x