H
Hidehiko Kawai
Researcher at Hiroshima University
Publications - 49
Citations - 2558
Hidehiko Kawai is an academic researcher from Hiroshima University. The author has contributed to research in topics: DNA damage & Ubiquitin ligase. The author has an hindex of 24, co-authored 42 publications receiving 2335 citations. Previous affiliations of Hidehiko Kawai include Harvard University & Yokohama City University.
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Journal ArticleDOI
Phosphorylation by aurora kinase A induces Mdm2-mediated destabilization and inhibition of p53
Hiroshi Katayama,Kaori Sasai,Hidehiko Kawai,Hidehiko Kawai,Zhi-Min Yuan,Jolanta Bondaruk,Fumio Suzuki,Satoshi Fujii,Ralph B. Arlinghaus,Bogdan Czerniak,Subrata Sen +10 more
TL;DR: It is concluded that aurora Kinase A is a key regulatory component of the p53 pathway and that overexpression of aurora kinase A leads to increased degradation of p53, causing downregulation of checkpoint-response pathways and facilitating oncogenic transformation of cells.
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Periostin promotes invasion and anchorage-independent growth in the metastatic process of head and neck cancer.
Yasusei Kudo,Ikuko Ogawa,Shojiro Kitajima,Masae Kitagawa,Hidehiko Kawai,Patrick M. Gaffney,Mutsumi Miyauchi,Takashi Takata +7 more
TL;DR: It is suggested that periostin plays an important role in the invasion and anchorage-independent growth of HNSCC.
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The p53 inhibitors MDM2/MDMX complex is required for control of p53 activity in vivo
Lei Huang,Zheng Yan,Xiaodong Liao,Yuan Li,Jie Yang,Zhugang Wang,Yong Zuo,Hidehiko Kawai,Miriam Shadfan,Suthakar Ganapathy,Zhi-Min Yuan +10 more
TL;DR: It is demonstrated that MDM2 and MDMX function as an integral complex in p53 control, providing insights into the nonredundant nature of the function of MDM1 and MDX, and the finding that concomitant deletion of p53 completely rescued the embryonic lethality in MdmxC462A/ C462A homozygous mice.
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DNA damage-induced MDMX degradation is mediated by MDM2.
Hidehiko Kawai,Dmitri Wiederschain,Hiroyuki Kitao,Jeremy Stuart,Kelvin K C Tsai,Zhi-Min Yuan +5 more
TL;DR: It is shown that DNA damage-induced p53 induction is associated with rapid down-regulation of the MDMX protein, and it is demonstrated that DNAdamage-induced MDMX reduction is mediated by MDM2, which targets MDMX for proteasomal degradation by a distinct mechanism that ensures optimal p53 activation.
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RING Domain–Mediated Interaction Is a Requirement for MDM2's E3 Ligase Activity
TL;DR: Disruption of the binding between MDM2 and MDMX resulted in a marked increase in both abundance and activity of p53, emphasizing the functional importance of this heterocomplex in p53 control.