Zobrazeno 1 - 10
of 116
pro vyhledávání: '"Morimitsu Nishikimi"'
Autor:
Yasunori Kozutsumi, Yoshio Kuroki, Motoko Araki, Tomomi Abe, Takeyuki Shimizu, Chiaki Nishitani, Morimitsu Nishikimi, Satoshi Miyata, Tomoyoshi Soga, Reiko Fujinawa, Yoko Inai, Motoko Takahashi, Junichi Fujii, Yoshito Ihara, Shigemitsu Ueyama, Naoyuki Taniguchi, Shigeru Ariki
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1820:1787-1796
Background Aldehyde reductase (AKR1A; EC 1.1.1.2) catalyzes the reduction of various types of aldehydes. To ascertain the physiological role of AKR1A, we examined AKR1A knockout mice. Methods Ascorbic acid concentrations in AKR1A knockout mice tissue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1719a663a3baec9af68dd1e1e2c2473
https://doi.org/10.1016/j.bbagen.2012.07.003
https://doi.org/10.1016/j.bbagen.2012.07.003
Publikováno v:
Bulletin of the Chemical Society of Japan. 85:1093-1101
The process of protein synthesis occurs in the ribosome and is an essential feature of life. The exact reaction mechanism for peptide bond formation in the peptidyl transferase center of the riboso...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::63f260d0be32364c350d24e4c21dff2c
https://doi.org/10.1246/bcsj.20120144
https://doi.org/10.1246/bcsj.20120144
Autor:
Mizuki Iwama, Morimitsu Nishikimi, Ryoya Takahashi, Akiko Amano, Yoshitaka Kondo, Hajime Furusawa, Akira Murata, Akihito Ishigami, Yasukazu Tanaka, Yoko Inai, Sataro Goto, Yasunori Sato, Naoki Maruyama, Setsuko Handa
Publikováno v:
Biological and Pharmaceutical Bulletin. 31:1673-1679
Carnitine is an essential cofactor in the transport of long-chain fatty acids into the mitochondrial matrix and plays an important role in energy production via beta-oxidation. Vitamin C (VC) has long been considered a requirement for the activities
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fb41fba47913c590636f3af4a6032d6
https://doi.org/10.1248/bpb.31.1673
https://doi.org/10.1248/bpb.31.1673
Autor:
Kentaro Shimokado, Morimitsu Nishikimi, Sataro Goto, Yasunori Sato, Akihito Ishigami, Yoko Inai, Yoshitaka Kondo, Sachiho Kubo, Naoki Maruyama, Setsuko Handa
Publikováno v:
Proceedings of the National Academy of Sciences. 103:5723-5728
We originally identified senescence marker protein 30 (SMP30) as a distinctive protein whose expression decreases in an androgen-independent manner with aging. Here, we report its sequence homology found in two kinds of bacterial gluconolactonases (G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd40ec2d759ac0f7f90bf91a475d108c
https://doi.org/10.1073/pnas.0511225103
https://doi.org/10.1073/pnas.0511225103
Autor:
Yoshifumi Takatsume, Yoko Inai, Noriyuki Shiraishi, Kazuhiro Maeta, Wenxiang Bi, Yoshiharu Inoue, Morimitsu Nishikimi
Publikováno v:
Journal of Clinical Biochemistry and Nutrition. 36:19-27
We compared relative copper-binding capacities of cellular components and determined the substance that dominantly sequesters excess copper incorporated into bakers' yeast cells before the copper homeostasis systems start to operate. The fluorescent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7282f7ba601264c028d5d0aa43427f9f
https://doi.org/10.3164/jcbn.36.19
https://doi.org/10.3164/jcbn.36.19
Autor:
Morimitsu Nishikimi, Yoko Inai
Publikováno v:
Archives of Biochemistry and Biophysics. 404:279-284
An Rpn9-disrupted yeast strain, Delta rpn9, whose growth is temperature sensitive with defective assembly of the 26 S proteasome complex, was studied. This mutant yeast was more resistant to hydrogen peroxide treatment and able to degrade carbonylate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8e1f50a4c78173cf58ca08b2f807e25
https://doi.org/10.1016/s0003-9861(02)00336-3
https://doi.org/10.1016/s0003-9861(02)00336-3
Publikováno v:
FEBS Letters. 511:118-122
The amino-terminal part of prion protein (PrP), containing a series of octapeptide repeats with the consensus sequence PHGGGWGQ, has been implicated in the binding of copper ion. This region possesses amino acid residues susceptible to oxidation, suc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59d73b5665dcb3aad57c65e0177c6752
https://doi.org/10.1016/s0014-5793(01)03324-5
https://doi.org/10.1016/s0014-5793(01)03324-5
Autor:
Masayasu Inoue, Misato Kashiba, Jun Oka, Takayo Inayama, Morimitsu Nishikimi, Takahiro Ishikawa, Haruaki Kageyama, Asako Kageyama, Rumi Ichikawa, Shuji Inoue
Publikováno v:
Biochemical Journal. 351:313-318
Ascorbic acid (AA) is a naturally occurring major antioxidant that is essential for the scavenging of toxic free radicals in both plasma and tissues. AA levels in plasma and tissues have been reported to be significantly lower than normal in diabetic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15c4ced83f657e75230ee13dd4e26304
https://doi.org/10.1042/bj3510313
https://doi.org/10.1042/bj3510313
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1474:378-382
Glutathione (GSH) is known to inhibit copper-catalyzed autoxidation of L-ascorbic acid (AA); in this study, AA was found to conversely inhibit copper-catalyzed autoxidation of GSH. To elucidate the mechanism of the mutual inhibition of the autoxidati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1c3ee6307ec3386a081c79356110924
https://doi.org/10.1016/s0304-4165(00)00034-9
https://doi.org/10.1016/s0304-4165(00)00034-9
Publikováno v:
Journal of Clinical Biochemistry and Nutrition. 29:37-44
Menkes' disease is an inherited disorder of copper homeostasis that arises from a deficiency in copper-transporting P-type ATPase, the mouse gene for which is designated Atp7a. The macular and the viable-brindled mouse are among Menkes' disease model
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3453d21249c7e1c4ed7071943b73dbd7
https://doi.org/10.3164/jcbn.29.37
https://doi.org/10.3164/jcbn.29.37