Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Lavan Khandan"'
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Multiple mechanisms regulate Wnt/ß-catenin signalling. Zhanget al. describe a novel regulatory pathway and show that the activator of canonical Wnt signalling, Norrin, triggers endocytosis of its receptor Frizzled4 by promoting Frizzled4 ubiquitinat
Externí odkaz:
https://doaj.org/article/42e7520136c84382908bf58215d8f91e
Autor:
Maria B. Lai, Chi Zhang, Jianli Shi, Verity Johnson, Lavan Khandan, John McVey, Michael W. Klymkowsky, Zhe Chen, Harald J. Junge
Publikováno v:
Cell Reports, Vol 19, Iss 13, Pp 2809-2822 (2017)
Accessory proteins in Frizzled (FZD) receptor complexes are thought to determine ligand selectivity and signaling amplitude. Genetic evidence indicates that specific combinations of accessory proteins and ligands mediate vascular β-catenin signaling
Externí odkaz:
https://doaj.org/article/af24154b07914062a601ee51ffff3106
Autor:
Jianli Shi, Zhe Chen, Harald J. Junge, Lavan Khandan, Verity Johnson, Maria B. Lai, Michael W. Klymkowsky, John C. McVey, Chi Zhang
Publikováno v:
Cell Reports, Vol 19, Iss 13, Pp 2809-2822 (2017)
Accessory proteins in Frizzled (FZD) receptor complexes are thought to determine ligand selectivity and signaling amplitude. Genetic evidence indicates that specific combinations of accessory proteins and ligands mediate vascular beta-catenin signali
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::883e16ba116ab592cc1fb898a8e7ea22
http://www.sciencedirect.com/science/article/pii/S2211124717307817
http://www.sciencedirect.com/science/article/pii/S2211124717307817
Publikováno v:
Nature Communications
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
Angiogenesis and blood–brain barrier formation are required for normal central nervous system (CNS) function. Both processes are controlled by Wnt or Norrin (NDP) ligands, Frizzled (FZD) receptors, and β-catenin-dependent signalling in vascular en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aa60a3780fb87bb106610f545339f02
https://doi.org/10.1038/ncomms16050
https://doi.org/10.1038/ncomms16050
Autor:
Stephanie Wood Baguley, Feng Li, Karin M. Reinisch, Frederic Pincet, Daniel Kümmel, Lavan Khandan, Jeff Coleman, Shyam S. Krishnakumar, James E. Rothman, Daniel T Radoff, Claudio G. Giraudo
Publikováno v:
Nature Structural & Molecular Biology. 18:934-940
The crystal structure of complexin bound to a prefusion SNAREpin mimetic shows that the accessory helix extends away from the SNAREpin in an 'open' conformation, binding another SNAREpin and inhibiting its assembly, to clamp fusion. In contrast, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8268e1498affea15852357ae2351f0be
https://doi.org/10.1038/nsmb.2103
https://doi.org/10.1038/nsmb.2103
Publikováno v:
The Journal of Cell Biology
Whittling away SNARE complex components reveals essential domains for Munc18-1–mediated membrane fusion.
Sec1/Munc18 (SM) proteins activate intracellular membrane fusion through binding to cognate SNAP receptor (SNARE) complexes. The synaptic
Sec1/Munc18 (SM) proteins activate intracellular membrane fusion through binding to cognate SNAP receptor (SNARE) complexes. The synaptic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02602eaa0d0119ea52d1cccffad9f422
http://europepmc.org/articles/PMC2911676
http://europepmc.org/articles/PMC2911676