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Coauthors
Satoshi Ninagawa Department of Biophysics, Graduate School of Science, Kyoto University, Japan
2 protocols

Kazutoshi Mori
  • Department of Biophysics, Graduate School of Science, Kyoto University, Japan
Contributions
  • 2 Author merit

Education

Ph.D. in Biochemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, 1987

Current position

Professor, Department of Biophysics, Graduate School of Science, Kyoto University

Publications

  1. Ninagawa, S., Okada, T., Sumitomo, Y., Horimoto, S., Sugimoto, T., Ishikawa, T., Takeda, S., Yamamoto, T., Suzuki, T., Kamiya, Y., Kato, K. and Mori, K. (2015). Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway. J Cell Biol 211(4): 775-784.

  2. Ninagawa, S., Okada, T., Sumitomo, Y., Kamiya, Y., Kato, K., Horimoto, S., Ishikawa, T., Takeda, S., Sakuma, T., Yamamoto, T. and Mori, K. (2014). EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step. J Cell Biol 206(3): 347-356.

  3. Horimoto, S., Ninagawa, S., Okada, T., Koba, H., Sugimoto, T., Kamiya, Y., Kato, K., Takeda, S. and Mori, K. (2013). The unfolded protein response transducer ATF6 represents a novel transmembrane-type endoplasmic reticulum-associated degradation substrate requiring both mannose trimming and SEL1L protein. J Biol Chem 288(44): 31517-31527.

2 Protocols published
Trypsin Sensitivity Assay to Study the Folding Status of Proteins
Authors:  Satoshi Ninagawa and Kazutoshi Mori, date: 10/05/2016, view: 1436, Q&A: 0
This protocol aims to evaluate folding status of proteins, utilizing trypsin sensitivity. Unfolded/misfolded proteins are more susceptible to trypsin than folded proteins, because trypsin easily accesses and cleaves loosely folded parts of proteins. ...
PNGase Sensitivity Assay to Study the Folding Status of Proteins
Authors:  Satoshi Ninagawa and Kazutoshi Mori, date: 10/05/2016, view: 1304, Q&A: 0
This protocol aims to evaluate folding status of proteins, utilizing peptide:N-glycanase (PNGase) sensitivity. In the cytosol, PNGase works as a deglycosylation-enzyme. N-glycans on unfolded/misfolded proteins are more susceptible to PNGase than ...