The protein disulfide isomerase family: from proteostasis to pathogenesis M Matsusaki, S Kanemura, M Kinoshita, YH Lee, K Inaba, M Okumura Biochimica et Biophysica Acta (BBA)-General Subjects 1864 (2), 129338, 2020 | 91 | 2020 |
Cooperative protein folding by two protein thiol disulfide oxidoreductases and ERO1 in soybean M Matsusaki, A Okuda, T Masuda, K Koishihara, R Mita, K Iwasaki, K Hara, ... Plant physiology 170 (2), 774-789, 2016 | 29 | 2016 |
Coupling effects of thiol and urea-type groups for promotion of oxidative protein folding S Okada, M Matsusaki, K Arai, Y Hidaka, K Inaba, M Okumura, T Muraoka Chemical communications 55 (6), 759-762, 2019 | 28 | 2019 |
PDI family members as guides for client folding and assembly S Kanemura, M Matsusaki, K Inaba, M Okumura International journal of molecular sciences 21 (24), 9351, 2020 | 27 | 2020 |
Accumulation of β-conglycinin in soybean cotyledon through the formation of disulfide bonds between α′-and α-subunits H Wadahama, K Iwasaki, M Matsusaki, K Nishizawa, M Ishimoto, ... Plant physiology 158 (3), 1395-1405, 2012 | 24 | 2012 |
Regulation of plant ER oxidoreductin 1 (ERO1) activity for efficient oxidative protein folding M Matsusaki, A Okuda, K Matsuo, K Gekko, T Masuda, Y Naruo, A Hirose, ... Journal of Biological Chemistry 294 (49), 18820-18835, 2019 | 20 | 2019 |
Identification and characterization of GmPDIL7, a soybean ER membrane‐bound protein disulfide isomerase family protein A Okuda, M Matsusaki, T Masuda, R Urade The FEBS Journal 284 (3), 414-428, 2017 | 14 | 2017 |
A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization M Okumura, S Kanemura, M Matsusaki, M Kinoshita, T Saio, D Ito, ... Structure 29 (12), 1357-1370. e6, 2021 | 11 | 2021 |
Disulfide bond formation activity of soybean quiescin sulfhydryl oxidase A Okuda, M Matsusaki, Y Higashino, T Masuda, R Urade The FEBS journal 281 (23), 5341-5355, 2014 | 11 | 2014 |
Ca2+ Regulates ERp57-Calnexin Complex Formation Y Tanikawa, S Kanemura, D Ito, Y Lin, M Matsusaki, K Kuroki, ... Molecules 26 (10), 2853, 2021 | 6 | 2021 |
Zinc-Dependent Oligomerization of Thermus thermophilus Trigger Factor Chaperone H Zhu, M Matsusaki, T Sugawara, K Ishimori, T Saio Biology 10 (11), 1106, 2021 | 5 | 2021 |
Conjugate of thiol and guanidyl units with oligoethylene glycol linkage for manipulation of oxidative protein folding S Okada, M Matsusaki, M Okumura, T Muraoka Molecules 26 (4), 879, 2021 | 4 | 2021 |
Functional interplay between p5 and pdi/erp72 to drive protein folding M Matsusaki, R Okada, Y Tanikawa, S Kanemura, D Ito, Y Lin, M Watabe, ... Biology 10 (11), 1112, 2021 | 3 | 2021 |
A novel soybean protein disulphide isomerase family protein possesses dithiol oxidation activity: identification and characterization of GmPDIL6 A Okuda, M Matsusaki, T Masuda, K Morishima, N Sato, R Inoue, ... The journal of biochemistry 168 (4), 393-405, 2020 | 3 | 2020 |
A unique adhesive motif of protein disulfide isomerase P5 supports its function via dimerization M Okumura, S Kanemura, M Matsusaki, M Kinoshita, T Saio, D Ito, ... bioRxiv, 2020.11. 17.387910, 2020 | 2 | 2020 |
Protein folding agent T Muraoka, S Okada, Y Matsumoto, M Okumura, K Inaba, M Matsusaki US Patent App. 18/264,520, 2024 | | 2024 |
Ca2+-driven PDIA6 phase separation to ensure proinsulin quality control YH Lee, T Saio, M Watabe, M Matsusaki, S Kanemura, Y Lin, T Mannen, ... bioRxiv, 2024.07. 30.605722, 2024 | | 2024 |
Redox-active chemical chaperones exhibiting promiscuous binding promote oxidative protein folding under condensed sub-millimolar conditions K Suzuki, R Nojiri, M Matsusaki, T Mabuchi, S Kanemura, K Ishii, ... Chemical Science 15 (32), 12676-12685, 2024 | | 2024 |
Conserved loop of a phase modifier endows protein condensates with fluidity H Kawamukai, M Matsusaki, T Tanimoto, M Watabe, K Morishima, ... bioRxiv, 2024.07. 03.601791, 2024 | | 2024 |
Client recognition differences between PDI and ERp46 to guide oxidative folding T Saio, K Ishii, M Matsusaki, H Kumeta, S Kenemura, M Okumura bioRxiv, 2024.03. 04.583432, 2024 | | 2024 |