Zobrazeno 1 - 10
of 91
pro vyhledávání: '"Hirofumi Komori"'
Autor:
Satoshi Nagao, Mariko Ueda, Hisao Osuka, Hirofumi Komori, Hironari Kamikubo, Mikio Kataoka, Yoshiki Higuchi, Shun Hirota
Publikováno v:
PLoS ONE, Vol 10, Iss 4, p e0123653 (2015)
Cytochrome c (cyt c) family proteins, such as horse cyt c, Pseudomonas aeruginosa cytochrome c551 (PA cyt c551), and Hydrogenobacter thermophilus cytochrome c552 (HT cyt c552), have been used as model proteins to study the relationship between the pr
Externí odkaz:
https://doaj.org/article/548607fc3d8d4ac3ad5998a22934fe9e
Autor:
Cheng Xie, Naoki Shibata, Hiromitsu Shimoyama, Yoshiki Higuchi, Satoshi Nagao, Yasuteru Shigeta, Shun Hirota, Hirofumi Komori, Masaru Yamanaka
Publikováno v:
RSC Advances. 11:37604-37611
Various factors, such as helical propensity and hydrogen bonds, control protein structures. A frequently used model protein, myoglobin (Mb), can perform 3D domain swapping, in which the loop at the hinge region is converted to a helical structure in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f44f235b1b37a3110922bf34ef32dd5a
https://doi.org/10.1039/d1ra06888a
https://doi.org/10.1039/d1ra06888a
Autor:
Hirofumi Komori, Yoko Nitta
Publikováno v:
Journal of Biological Macromolecules. 21:69-74
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2ae189b2cc9e599f885168fab51c4b2b
https://doi.org/10.14533/jbm.21.69
https://doi.org/10.14533/jbm.21.69
Autor:
Hirofumi Komori1, Kunishige Kataoka2, Sakiko Tanaka2, Nana Matsuda2, Yoshiki Higuchi3, Takeshi Sakurai2 tasakura@staff.kanazawa-u.ac.jp
Publikováno v:
Acta Crystallographica: Section F, Structural Biology Communications. Jul2016, Vol. 72 Issue 7, p558-563. 6p.
Autor:
Yoshiki Higuchi, Mahfuza Akter, Takeshi Sakurai, Hirofumi Komori, Kunishige Kataoka, Naoki Shibata, Nana Matsuda, Chika Inoue
Publikováno v:
Acta Crystallographica Section F Structural Biology Communications. 72:788-794
Multicopper oxidases oxidize various phenolic and nonphenolic compounds by using molecular oxygen as an electron acceptor to produce water. A multicopper oxidase protein, CueO, fromEscherichia coliis involved in copper homeostasis in the bacterial ce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff70badaee4e9696b82b5d7002554702
https://doi.org/10.1107/s2053230x1601400x
https://doi.org/10.1107/s2053230x1601400x
Autor:
Frank Y. J. Chen, Hirofumi Komori, Hong-Wei Lee, Richard Scott Johnson, Jaroslav Hynecek, Sergey Velichko, Victor Lenchenkov
Publikováno v:
IEEE Transactions on Electron Devices. 63:106-112
We describe different charge-storage-based global shutter (GS) pixel architectures with improved performance resulting from low dark current and effective pixel pitch reduction from 6 to 2.8 $\mu \text{m}$ pixel size. Smaller pixels showed better ima
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::24aa1a252041e405d914f6f9d42596a2
https://doi.org/10.1109/ted.2015.2443495
https://doi.org/10.1109/ted.2015.2443495
Autor:
Hirofumi Komori1,2 komori@ed.kagawa-u.ac.jp, Yoshiki Higuchi2,3 hig@sci.u-hyogo.ac.jp
Publikováno v:
Journal of Biochemistry. Oct2015, Vol. 158 Issue 4, p293-298. 6p.
Publikováno v:
Archives of Biochemistry and Biophysics. 693:108551
Histidine decarboxylase (HDC; EC 4.1.1.22), an enzyme that catalyzes histamine synthesis with high substrate specificity, is a member of the group II pyridoxal 5'-phosphate (PLP) -dependent decarboxylase family. Tyrosine is a conserved residue among
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e58dd1ba8ac9d86206272d55b4018f2
https://doi.org/10.1016/j.abb.2020.108551
https://doi.org/10.1016/j.abb.2020.108551
Publikováno v:
Protein Science. 24:366-375
Cytochrome c555 from hyperthermophilic bacteria Aquifex aeolicus (AA cyt c555) is a hyperstable protein belonging to the cyt c protein family, which possesses a unique long 310-α-310 helix containing the heme-ligating Met61. Herein, we show that AA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d369535aec139e3f52ba36c33df463e9
https://doi.org/10.1002/pro.2627
https://doi.org/10.1002/pro.2627
Autor:
Megha S. Deshpande, Partha Pratim Parui, Hironari Kamikubo, Yoshiki Higuchi, Shun Hirota, Masaru Yamanaka, Hirofumi Komori, Mikio Kataoka, Satoshi Nagao
Publikováno v:
Biochemistry. 53:4696-4703
Many proteins, including cytochrome c (cyt c), have been shown to form domain-swapped oligomers, but the factors governing the oligomerization process remain unrevealed. We obtained oligomers of cyt c by refolding cyt c from its acid molten globule s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c8e9f68b0dd2783805d845f7a2265cd
https://doi.org/10.1021/bi500497s
https://doi.org/10.1021/bi500497s