Zobrazeno 1 - 10
of 75
pro vyhledávání: '"Mitsuhiko Ikura"'
Publikováno v:
International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 21, Iss 2751, p 2751 (2020)
International Journal of Molecular Sciences, Vol 21, Iss 2751, p 2751 (2020)
Calmodulin (CaM) is a Ca2+-sensor that regulates a wide variety of target proteins, many of which interact through short basic helical motifs bearing two hydrophobic ‘anchor’ residues. CaM comprises two globular lobes, each containing a pair of E
Autor:
Miguel, Burgos, Reginald, Philippe, Fabrice, Antigny, Paul, Buscaglia, Emmanuelle, Masson, Sreya, Mukherjee, Pauline, Dubar, Cédric, Le Maréchal, Florence, Campeotto, Nicolas, Lebonvallet, Maud, Frieden, Juan, Llopis, Beatriz, Domingo, Peter B, Stathopulos, Mitsuhiko, Ikura, Wesley, Brooks, Wayne, Guida, Jian-Min, Chen, Claude, Ferec, Thierry, Capiod, Olivier, Mignen
Publikováno v:
Journal of cell science. 134(3)
Since deregulation of intracellular Ca
Autor:
Noboru Ishiyama, Le Zheng, Peter B. Stathopulos, Sung-In Back, Masahiro Enomoto, Tadateru Nishikawa, Mitsuhiko Ikura
Publikováno v:
Journal of molecular biology. 432(2)
Store operated calcium (Ca2+) entry (SOCE) is the process whereby endoplasmic reticulum (ER) Ca2+ store depletion causes Orai1-composed Ca2+ channels on the plasma membrane (PM) to open, mediating a rise in cytosolic Ca2+ levels. Stromal interaction
Publikováno v:
Methods in Molecular Biology ISBN: 9781493990290
Calmodulin (CaM) is a ubiquitous calcium-sensing protein that has one of the most highly conserved sequences among eukaryotes. CaM has been a useful tool for biologists studying calcium signaling for decades. In recent years, CaM has also been implic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a75693135abf91723d8fa9f4567f73eb
https://doi.org/10.1007/978-1-4939-9030-6_13
https://doi.org/10.1007/978-1-4939-9030-6_13
Autor:
Masahiro, Enomoto, Tadateru, Nishikawa, Naveed, Siddiqui, Steve, Chung, Mitsuhiko, Ikura, Peter B, Stathopulos
Publikováno v:
Advances in experimental medicine and biology. 981
All eukaryotic cells have adapted the use of the calcium ion (Ca
Autor:
Mitsuhiko Ikura, Peter B. Stathopulos
Publikováno v:
Cell Calcium. 77:79-80
A single calcium (Ca2+) binding site within the canonical EF-hand loop was thought to govern the stromal interaction molecule-1 (STIM1) structural changes that lead to activation of Orai1 Ca2+ channels. Recent work by Gudlur et al., published in Nat
Autor:
Mate Maus, Stephan Ehl, Martin Muik, Sebastian Fuchs, Peter B. Stathopulos, Christoph Romanin, Murali Prakriya, Amit Jairaman, Mitsuhiko Ikura, Stefan Feske, Melina J. Benson, Marc Fahrner, Carl Weidinger
Publikováno v:
Proceedings of the National Academy of Sciences. 112:6206-6211
Store-operated Ca(2+) entry (SOCE) is a universal Ca(2+) influx pathway that is important for the function of many cell types. SOCE occurs upon depletion of endoplasmic reticulum (ER) Ca(2+) stores and relies on a complex molecular interplay between
Autor:
Mitsuhiko Ikura, Peter B. Stathopulos
Publikováno v:
Cell calcium. 63
In 1986, J.W. Putney presented a model for capacitative calcium (Ca2+) entry conveying that depletion of endoplasmic reticulum stored Ca2+ levels leads to activation of plasma membrane Ca2+ channels which mediate influx of Ca2+ from the extracellular
Autor:
Mitsuhiko Ikura, Peter B. Stathopulos
Publikováno v:
Channels. 7:344-353
Store-operated calcium (Ca(2+)) entry is the process by which molecules located on the endo/sarcoplasmic reticulum (ER/SR) respond to decreased luminal Ca(2+) levels by signaling Ca(2+) release activated Ca(2+) channels (CRAC) channels to open on the
Autor:
Le Zheng, Mitsuhiko Ikura, Peter B. Stathopulos, Guang-Yao Li, Rainer Schindl, Christoph Romanin
Publikováno v:
Proceedings of the National Academy of Sciences. 108:1337-1342
Stromal interaction molecules (STIM)s function as endoplasmic reticulum calcium (Ca 2+ ) sensors that differentially regulate plasma membrane Ca 2+ release activated Ca 2+ channels in various cells. To probe the structural basis for the functional di