Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Shigeyasu Ito"'
Publikováno v:
Journal of Microbiological Methods. 202:106579
Some bacteria produce non-sulfated chondroitin (CH). Accurate, rapid, and high throughput methods to quantify CH in fermented cultures helps to improve microbial breeding and fermentation conditions efficiently. In this study, highly sensitive method
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ba0890162bede57189b583fac988401
https://doi.org/10.1016/j.mimet.2022.106579
https://doi.org/10.1016/j.mimet.2022.106579
Autor:
Shun-ichi Kawahara, Ryuichiro Suzuki, Satoshi Kaneko, Shigeyasu Ito, Zui Fujimoto, Atsushi Kuno, Kazunari Taira, Tsunemi Hasegawa
Publikováno v:
The Journal of Biochemistry. 146:61-70
Retaining glycosyl hydrolases, which catalyse both glycosylation and deglycosylation in a concerted manner, are the most abundant hydrolases. To date, their visualization has tended to be focused on glycosylation because glycosylation reactions can b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d9b90265abc172935c2b4092ef0cd3b
https://doi.org/10.1093/jb/mvp047
https://doi.org/10.1093/jb/mvp047
Autor:
Atsushi Kuno, Tsunemi Hasegawa, Shigeyasu Ito, Hikaru Hemmi, Ryuichiro Suzuki, Jun Hirabayashi
Publikováno v:
FEBS Journal. 276:2095-2105
The R-type lectin EW29, isolated from the earthworm Lumbricus terrestris, consists of two homologous domains (14 500 Da) showing 27% identity with each other. The C-terminal domain (Ch; C-half) of EW29 (EW29Ch) has two sugar-binding sites in subdomai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8821e708c8ad4a0dc70f73b382301c78
https://doi.org/10.1111/j.1742-4658.2009.06944.x
https://doi.org/10.1111/j.1742-4658.2009.06944.x
Autor:
Shigeyasu Ito
Publikováno v:
Journal of the Mass Spectrometry Society of Japan. 57:283-289
Numerous studies have been reported on structural analysis of chondroitin sulfate (CS) oligosaccharides using multiple-stage mass spectrometry (MSn). However, their sequence determination is highly complex because of the simply repeating backbone str
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2b075e2989ccf2161b877487d0802ebc
https://doi.org/10.5702/massspec.57.283
https://doi.org/10.5702/massspec.57.283
Autor:
Shigeyasu Ito, Atsushi Kuno, Satoshi Kaneko, Yasuyuki Kawabata, Ryuichiro Suzuki, Isao Kusakabe, Tsunemi Hasegawa
Publikováno v:
Journal of Biotechnology. 110:137-142
Xylanase SoXyn10A from Streptomyces olivaceoviridis E-86 comprises a family 10 catalytic module linked to a family 13 carbohydrate-binding module (SoCBM13). The SoCBM13 has a beta-trefoil structure, with binding sites in each subdomain (alpha, beta a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71bc548111b66151f1ce6b7f6d570a6b
https://doi.org/10.1016/j.jbiotec.2004.01.014
https://doi.org/10.1016/j.jbiotec.2004.01.014
Autor:
Hikaru, Hemmi, Atsushi, Kuno, Shigeyasu, Ito, Ryuichiro, Suzuki, Tsunemi, Hasegawa, Jun, Hirabayashi
Publikováno v:
The FEBS journal. 276(7)
The R-type lectin EW29, isolated from the earthworm Lumbricus terrestris, consists of two homologous domains (14,500 Da) showing 27% identity with each other. The C-terminal domain (Ch; C-half) of EW29 (EW29Ch) has two sugar-binding sites in subdomai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::70bd359bef12aa7b13613051861706ce
https://pubmed.ncbi.nlm.nih.gov/19292877
https://pubmed.ncbi.nlm.nih.gov/19292877
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 534
In order to understand glycoprotein functionality, information on the structure of both the core proteins and the glycan moieties is necessary. From a practical viewpoint, glycopeptides rather than whole glycoproteins are the general targets for stru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c8653c417eea9d4e60c022c9a7b7b2fd
https://pubmed.ncbi.nlm.nih.gov/19277551
https://pubmed.ncbi.nlm.nih.gov/19277551
Publikováno v:
Glycomics ISBN: 9781588297747
In order to understand glycoprotein functionality, information on the structure of both the core proteins and the glycan moieties is necessary. From a practical viewpoint, glycopeptides rather than whole glycoproteins are the general targets for stru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a400003a7517c7306a57b3f1a90aeda
https://doi.org/10.1007/978-1-59745-022-5_14
https://doi.org/10.1007/978-1-59745-022-5_14
Autor:
Hikaru, Hemmi, Atsushi, Kuno, Shigeyasu, Ito, Ryuichiro, Suzuki, Satoshi, Kaneko, Tsunemi, Hasegawa, Jun, Hirabayashi, Ken-Ichi, Kasai
Publikováno v:
Journal of biomolecular NMR. 30(3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::951fb69473ba805ae4230258f48946f3
https://pubmed.ncbi.nlm.nih.gov/15756471
https://pubmed.ncbi.nlm.nih.gov/15756471
Publikováno v:
Journal of biomolecular NMR. 27(1)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e95dcacec67820d6bfa85b601737e6f6
https://pubmed.ncbi.nlm.nih.gov/12878846
https://pubmed.ncbi.nlm.nih.gov/12878846