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FEBS Letters|July 29, 2006
Negative regulation of protein phosphatase 2Cbeta by ISG15 conjugationTomoharu Takeuchi, Takayasu Kobayashi, Shinri Tamura, et al.
Biological & Pharmaceutical Bulletin|December 6, 2005
Involvement of polyubiquitin chains via specific chain linkages in stress response in mammalian cellsMasahiro Fujimuro, Tadashi Nishiya, Yasuyuki Nomura, et al.
Comparative Biochemistry and Physiology. Toxicology & Pharmacology : CBP|November 30, 2002
Zymosan induces production of superoxide anions by hemocytes of the solitary ascidian Halocynthia roretziKaoru Azumi, Futoshi Kuribayashi, Shiro Kanegasaki, et al.
Developmental Biology|September 13, 2005
Highly polymorphic vitelline-coat protein HaVC80 from the ascidian, Halocynthia aurantium: structural analysis and involvement in self/nonself recognition during fertilizationSusumu Ban, Yoshito Harada, Hideyoshi Yokosawa, et al.
Methods in Molecular Biology (Clifton, N.J.)|July 1, 2019
An Approach for the Identification of Proteins Modified with ISG15Tomoharu Takeuchi, Shun Koinuma, Hideyoshi Yokosawa, et al.
Biological & Pharmaceutical Bulletin|December 2, 2008
Regulation of the nuclear factor (NF)-kappaB pathway by ISGylationMiki Minakawa, Takayuki Sone, Tomoharu Takeuchi, et al.
The Biochemical Journal|April 13, 2007
Scythe regulates apoptosis through modulating ubiquitin-mediated proteolysis of the Xenopus elongation factor XEF1AORyosuke Minami, Masumi Shimada, Hideyoshi Yokosawa, et al.
Biochemical and Biophysical Research Communications|June 8, 2002
Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysisYasushi Saeki, Aki Saitoh, Akio Toh-e, et al.
The Journal of Biological Chemistry|May 1, 2004
Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiaeTakayuki Sone, Yasushi Saeki, Akio Toh-e, et al.
The Journal of Biological Chemistry|April 23, 2004
Rpn7 Is required for the structural integrity of the 26 S proteasome of Saccharomyces cerevisiaeErika Isono, Yasushi Saeki, Hideyoshi Yokosawa, et al.
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