Zobrazeno 1 - 10
of 127
pro vyhledávání: '"Mitsuhiko Ikura"'
Autor:
Marika Meyer zu Brickwedde, Dietmar Vestweber, Giuseppe Trapani, Ute Ipe, Hans R. Schöler, Laura J Braun, Hermann vom Bruch, Britta Trappmann, Martina Schmitt, Stephan Huveneers, Mirsana P. Ebrahimkutty, Noboru Ishiyama, Cao Nguyen Duong, Johan de Rooij, Astrid F. Nottebaum, Mitsuhiko Ikura, Randy Brückner
Publikováno v:
Journal of Cell Science
article-version (VoR) Version of Record
Journal of cell science, 134(24). Company of Biologists Ltd
article-version (VoR) Version of Record
Journal of cell science, 134(24). Company of Biologists Ltd
Cadherin-mediated cell adhesion requires anchoring via the β-catenin–α-catenin complex to the actin cytoskeleton, yet, α-catenin only binds F-actin weakly. A covalent fusion of VE-cadherin to α-catenin enhances actin anchorage in endothelial ce
Autor:
Teklab Gebregiworgis, Christopher B. Marshall, Fenneke KleinJan, Geneviève M.C. Gasmi-Seabrook, Ben J Eves, Masahiro Enomoto, Ningdi F Liu, Ki-Young Lee, Mitsuhiko Ikura, Zhenhao Fang
Publikováno v:
Journal of Biomolecular NMR. 74:531-554
Mutations in RAS oncogenes occur in ~ 30% of human cancers, with KRAS being the most frequently altered isoform. RAS proteins comprise a conserved GTPase domain and a C-terminal lipid-modified tail that is unique to each isoform. The GTPase domain is
Publikováno v:
Nature Chemical Biology. 18:578-579
Autor:
Etienne Coyaud, Mitsuhiko Ikura, Arun A. Chandrakumar, Robert Rottapel, Brian Raught, Christopher B. Marshall
Publikováno v:
Journal of Cell Biology
Journal of Cell Biology, 2021, Journal of Cell Biology, 220 (7), pp.e202008037. ⟨10.1083/jcb.202008037⟩
The Journal of Cell Biology
Journal of Cell Biology, 2021, Journal of Cell Biology, 220 (7), pp.e202008037. ⟨10.1083/jcb.202008037⟩
The Journal of Cell Biology
Chandrakumar et al. reveal that lumen formation in epithelial cells is regulated by ADP-ribosylation and ubiquitylation. Tankyrase inhibits its substrates SH3BP5 and SH3BP5L, which are Rab11a guanine nucleotide exchange factors, while the E3 ligase R
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::762381027868e558461dfc23c3863dba
http://hdl.handle.net/20.500.12210/75051
http://hdl.handle.net/20.500.12210/75051
Autor:
Christian W. Johnson, Hyuk-Soo Seo, Elizabeth M. Terrell, Moon-Hee Yang, Fenneke KleinJan, Teklab Gebregiworgis, Genevieve M.C. Gasmi-Seabrook, Ezekiel A. Geffken, Jimit Lakhani, Kijun Song, Puspalata Bashyal, Olesja Popow, Joao A. Paulo, Andrea Liu, Carla Mattos, Christopher B. Marshall, Mitsuhiko Ikura, Deborah K. Morrison, Sirano Dhe-Paganon, Kevin M. Haigis
Publikováno v:
Mol Cell
A unifying feature of the RAS superfamily is a conserved GTPase cycle by which these proteins transition between active and inactive states. We demonstrate that autophosphorylation of some GTPases is an intrinsic regulatory mechanism that reduces nuc
Autor:
Thierry Capiod, Emmanuelle Masson, Wesley H. Brooks, Reginald Philippe, Nicolas Lebonvallet, Wayne C. Guida, Pauline Dubar, Miguel Burgos, Juan Llopis, Fabrice Antigny, Olivier Mignen, Peter B. Stathopulos, Claude Férec, Mitsuhiko Ikura, Maud Frieden, F. Campeotto, Beatriz Domingo, Sreya Mukherjee, Cédric Le Maréchal, Paul Buscaglia, Jian-Min Chen
Publikováno v:
Journal of Cell Science, Vol. 134, No 3 (2021)
Journal of Cell Science
Journal of Cell Science, Company of Biologists, 2021, 134 (3), ⟨10.1242/jcs.244012⟩
Journal of Cell Science
Journal of Cell Science, Company of Biologists, 2021, 134 (3), ⟨10.1242/jcs.244012⟩
Since deregulation of intracellular Ca2+ can lead to intracellular trypsin activation, and stromal interaction molecule-1 (STIM1) protein is the main regulator of Ca2+ homeostasis in pancreatic acinar cells, we explored the Ca2+ signaling in 37 STIM1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cb375b757ccf1fc81d2061d83a917b5
https://archive-ouverte.unige.ch/unige:151400
https://archive-ouverte.unige.ch/unige:151400
Autor:
Le Zheng, Geneviève M.C. Gasmi-Seabrook, Mitsuhiko Ikura, Zhenhao Fang, Ku-Geng Huo, Christopher B. Marshall, Ming-Sound Tsao, Ki-Young Lee, Nadeem Moghal
Publikováno v:
Proc Natl Acad Sci U S A
Membrane anchoring of farnesylated KRAS is critical for activation of RAF kinases, yet our understanding of how these proteins interact on the membrane is limited to isolated domains. The RAS-binding domain (RBD) and cysteine-rich domain (CRD) of RAF
Autor:
Satoshi Kubo, Mitsuhiko Ikura, Christopher B. Marshall, Noritaka Nishida, Ryu Fujimiya, Qingci Zhao, Ichio Shimada
Publikováno v:
Cell Reports, Vol 32, Iss 8, Pp 108074-(2020)
Summary The small guanosine triphosphatase (GTPase) RAS serves as a molecular switch in signal transduction, and its mutation and aberrant activation are implicated in tumorigenesis. Here, we perform real-time, in-cell nuclear magnetic resonance (NMR
Autor:
M. Enomoto, Ki-Young Lee, Sung-In Back, Benjamin M M Grant, Teklab Gebregiworgis, Christopher B. Marshall, Mitsuhiko Ikura, Noboru Ishiyama
Publikováno v:
Science Signaling. 13
KRAS4b is a small guanosine triphosphatase (GTPase) protein that regulates several signal transduction pathways that underlie cell proliferation, differentiation, and survival. KRAS4b function requires prenylation of its C terminus and recruitment to
Autor:
Wesley H. Brooks, Juan Llopis, Olivier Mignen, Mitsuhiko Ikura, Fabrice Antigny, Emmanuelle Masson, Paul Buscaglia, Reginald Philippe, Sreya Mukherjee, F. Campeotto, Cédric Le Maréchal, Maud Frieden, Beatriz Domingo, Jian-Min Chen, Nicolas Lebonvallet, Wayne C. Guida, Peter B. Stathopulos, Claude Férec, Thierry Capiod, Pauline Dubar, Miguel Burgos
Since deregulation of intracellular Ca2+ can lead to intracellular trypsin activation and STIM1 (stromal interaction molecule-1) protein is the main regulator of Ca2+ homeostasis in pancreatic acinar cells, we explored the Ca2+ signaling in 37 STIM1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8db78d98eec1a116b093c8cc20e9b8e9
https://doi.org/10.1101/2020.01.22.916254
https://doi.org/10.1101/2020.01.22.916254