Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Takamasa Fukunaga"'
Autor:
Takamasa Fukunaga, Masahiro Watanabe, Yusuke Nakamichi, Tomotake Morita, Yujiro Higuchi, Hiromi Maekawa, Kaoru Takegawa
Publikováno v:
Journal of Bioscience and Bioengineering. 135:423-432
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a3178a82d94f26b6ee19778d0531bd8
https://doi.org/10.1016/j.jbiosc.2023.03.002
https://doi.org/10.1016/j.jbiosc.2023.03.002
Autor:
Kaoru Takegawa, Takamasa Fukunaga, Yujiro Higuchi, Hiromi Maekawa, Yuki Sakurai, Takao Ohashi
Publikováno v:
Applied Microbiology and Biotechnology. 105:8771-8781
The glycoproteins of yeast contain a large outer chain on N-linked oligosaccharides; therefore, yeast is not suitable for producing therapeutic glycoproteins for human use. Using a deletion mutant strain of α1,6-mannosyltransferase (och1Δ), we prev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb3e91aeb59e2cfb61df88e5f4968173
https://doi.org/10.1007/s00253-021-11649-5
https://doi.org/10.1007/s00253-021-11649-5
Autor:
Takamasa Fukunaga, Takao Ohashi, Yutaka Tanaka, Tomoki Yoshimatsu, Yujiro Higuchi, Hiromi Maekawa, Kaoru Takegawa
Publikováno v:
Journal of bioscience and bioengineering. 134(5)
Schizosaccharomyces japonicus is a dimorphic yeast, transiting between unicellular and hyphal growth. The glycoproteins of fission yeast contain, in addition to mannose (Man), a large number of galactose (Gal) residues. Previously, we reported that t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26c07d56fa17abc623b6f1204db97314
https://pubmed.ncbi.nlm.nih.gov/36058798
https://pubmed.ncbi.nlm.nih.gov/36058798
Autor:
Kaoru Takegawa, Shiori Matsuura, Keisuke Hirai, Naotaka Tanaka, Takamasa Fukunaga, Akinari Kagami, Shotaro Suzuki, Mitsuaki Tabuchi
Publikováno v:
The Journal of General and Applied Microbiology. 67:67-76
The gmn2 mutant of Schizosaccharomyces pombe has previously been shown to exhibit defects in protein glycosylation of N-linked oligosaccharides (Ballou, L. and Ballou, CE., Proc. Natl. Acad. Sci. USA, 92, 2790-2794 (1995)). Like most glycosylation-de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0c303d30dcbb5b48d8b6db98bc19d52d
https://doi.org/10.2323/jgam.2020.07.002
https://doi.org/10.2323/jgam.2020.07.002
Publikováno v:
Applied Microbiology and Biotechnology. 104:8897-8909
The majority of Golgi glycosyltransferases are type II membrane proteins with a small cytosolic tail at their N-terminus. Several mechanisms for localizing these glycosyltransferases to the Golgi have been proposed. In Saccharomyces cerevisiae, the p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9f8c8334ea977841e4159fb51694a36
https://doi.org/10.1007/s00253-020-10881-9
https://doi.org/10.1007/s00253-020-10881-9
Autor:
Yujiro Higuchi, Hiromi Maekawa, Toshio Furumoto, Naotaka Tanaka, Takao Ohashi, Kaoru Takegawa, Takamasa Fukunaga, Shin-ichi Nakakita
Publikováno v:
Journal of Bioscience and Bioengineering. 130:128-136
The N- and O-linked oligosaccharides from fission yeast Schizosaccharomyces pombe not only contain large amounts of d -mannose (Man) but also contain large amounts of d -galactose (Gal). Although the galactomannans of S. pombe are mainly composed of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dec906757f0e4fe483c3356761d8a706
https://doi.org/10.1016/j.jbiosc.2020.03.008
https://doi.org/10.1016/j.jbiosc.2020.03.008
Autor:
Ryoichiro Fukuhara, Akihiro Ogura, Sho Yoshinaga, Takamasa Fukunaga, Takashi Kinoshita, Wataru Sumiyoshi, Yujiro Higuchi, Katsunori Tanaka, Kaoru Takegawa
Publikováno v:
Bioorganic & Medicinal Chemistry. 70:116943
Both pyruvylation and sialylation onto the terminus of oligosaccharides of N-glycoproteins seem to be structurally and functionally similar with a property of conferring negative charge. However, detailed molecular characteristics of pyruvylation and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e9b060dc8e1c5ba9b8f0f975383e592
https://doi.org/10.1016/j.bmc.2022.116943
https://doi.org/10.1016/j.bmc.2022.116943
Autor:
Naotaka, Tanaka, Akinari, Kagami, Keisuke, Hirai, Shotaro, Suzuki, Shiori, Matsuura, Takamasa, Fukunaga, Mitsuaki, Tabuchi, Kaoru, Takegawa
Publikováno v:
The Journal of general and applied microbiology. 67(2)
The gmn2 mutant of Schizosaccharomyces pombe has previously been shown to exhibit defects in protein glycosylation of N-linked oligosaccharides (Ballou, L. and Ballou, CE., Proc. Natl. Acad. Sci. USA, 92, 2790-2794 (1995)). Like most glycosylation-de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b8cc3ea751aed4cd12ac907b011a1cba
https://pubmed.ncbi.nlm.nih.gov/33536395
https://pubmed.ncbi.nlm.nih.gov/33536395
Autor:
Kaoru Takegawa, Takamasa Fukunaga, Naotaka Tanaka, Toshio Furumoto, Hiromi Maekawa, Yujiro Higuchi, Takao Ohashi, Shin-ichi Nakakita
Publikováno v:
Glycobiology. 31(8)
In the fission yeast Schizosaccharomyces pombe, α1,2- and α1,3-linked D-galactose (Gal) residues are transferred to N- and O-linked oligosaccharides of glycoproteins by galactosyltransferases. Although the galactomannans are important for cell–ce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d828c261e936810ebb9e076965c7015
https://pubmed.ncbi.nlm.nih.gov/33909078
https://pubmed.ncbi.nlm.nih.gov/33909078