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Yusuke Saijo
Researcher at Nara Institute of Science and Technology
Publications - 52
Citations - 5707
Yusuke Saijo is an academic researcher from Nara Institute of Science and Technology. The author has contributed to research in topics: Arabidopsis & Pattern recognition receptor. The author has an hindex of 28, co-authored 48 publications receiving 4894 citations. Previous affiliations of Yusuke Saijo include Kyoto University & National Archives and Records Administration.
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Journal ArticleDOI
Over-expression of a single Ca2+-dependent protein kinase confers both cold and salt/drought tolerance on rice plants.
TL;DR: OsCDPK7 was shown to be a positive regulator commonly involved in the tolerance to both stresses in rice, and simple manipulation of CDPK activity has great potential with regard to plant improvement.
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Nuclear Activity of MLA Immune Receptors Links Isolate-Specific and Basal Disease-Resistance Responses
Qian-Hua Shen,Yusuke Saijo,Stefan Mauch,Christoph Biskup,Stéphane Bieri,Beat Keller,Hikaru Seki,Bekir Ülker,Imre E. Somssich,Paul Schulze-Lefert +9 more
TL;DR: In barley, intracellular mildew A (MLA) R proteins function in the nucleus to confer resistance against the powdery mildew fungus, revealing a mechanism by which these polymorphic immune receptors integrate distinct pathogen signals.
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The COP1–SPA1 interaction defines a critical step in phytochrome A-mediated regulation of HY5 activity
Yusuke Saijo,James A. Sullivan,Haiyang Wang,Jianping Yang,Yunping Shen,Vicente Rubio,Ligeng Ma,Ute Hoecker,Xing Wang Deng +8 more
TL;DR: It is reported that COP1 acts as part of a large protein complex and interacts with SPA1 in a light-dependent manner and defines a critical step in coordinating COP1-mediated ubiquitination and subsequent degradation of HY5 with PHYA signaling.
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Pattern recognition receptors and signaling in plant-microbe interactions.
TL;DR: The functional significance and molecular basis of PRR-mediated pathogen recognition and disease resistance, and also an emerging role for PRRs in homeostatic association with beneficial or commensal microbes are reviewed.
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Coiled-Coil Domain-Dependent Homodimerization of Intracellular Barley Immune Receptors Defines a Minimal Functional Module for Triggering Cell Death
Takaki Maekawa,Wei Cheng,Laurentiu N. Spiridon,Armin Töller,Ewa Lukasik,Yusuke Saijo,Peiyuan Liu,Qian-Hua Shen,Marius A. Micluta,Imre E. Somssich,Frank L. W. Takken,Andrei-Jose Petrescu,Jijie Chai,Paul Schulze-Lefert +13 more
TL;DR: In this article, the crystal structure of an MLA receptor's invariant coiled-coil domain was revealed, which reveals a rod-shaped homodimer, which implies a role for the dimeric CC module in downstream immune signaling.