Zobrazeno 1 - 10
of 55
pro vyhledávání: '"Masaki Kurogochi"'
Autor:
Masaki Kurogochi, Junko Amano
Publikováno v:
Molecules, Vol 19, Iss 7, Pp 9944-9961 (2014)
We have developed an effective, sensitive method for quantitative glycopeptide profiling using stable isotope labeling and MALDI-TOF mass spectrometry (MS). In this study, we synthesized benzoic acid-d0 N-succinimidyl ester (BzOSu) and benzoic acid-d
Externí odkaz:
https://doaj.org/article/6ec39e2c682849d8a13580a5ccf80ba9
Autor:
Masaki Kurogochi, Masako Mori, Kenji Osumi, Mami Tojino, Shu-Ichi Sugawara, Shou Takashima, Yuriko Hirose, Wataru Tsukimura, Mamoru Mizuno, Junko Amano, Akio Matsuda, Masahiro Tomita, Atsushi Takayanagi, Shin-Ichiro Shoda, Takashi Shirai
Publikováno v:
PLoS ONE, Vol 10, Iss 7, p e0132848 (2015)
Many therapeutic antibodies have been developed, and IgG antibodies have been extensively generated in various cell expression systems. IgG antibodies contain N-glycans at the constant region of the heavy chain (Fc domain), and their N-glycosylation
Externí odkaz:
https://doaj.org/article/01cee135897a4ad7a120104af426bdf4
Autor:
Takashi Baba, Khadijeh Rajabi, Suya Liu, Pavel Ryumin, Zoe Zhang, Kerstin Pohl, Jason Causon, J. C. Yves Le Blanc, Masaki Kurogochi
Publikováno v:
Journal of the American Society for Mass Spectrometry. 33(9)
We report on the dissociation of singly protonated peptides by electrons using electron-activated dissociation (EAD), which comprises electron impact excitation of ions from organics (EIEIO), electronic-excitation dissociation (EED), and electron ion
Autor:
Shou Takashima, Sugawara Shuichi, Kenji Osumi, Akio Matsuda, Wataru Tsukimura, Masaki Kurogochi, Mamoru Mizuno, Yoshio Takada, Masako Mori, Junko Amano
Publikováno v:
Glycobiology. 31:1401-1414
Immunoglobulin G (IgG) has a conserved N-glycosylation site at Asn297 in the fragment crystallizable (Fc) region. Previous studies have shown that N-glycosylation of this site is a critical mediator of the antibody’s effector functions, such as ant
Autor:
Masaki Kurogochi
Publikováno v:
Trends in Glycoscience and Glycotechnology. 30:J169-J179
Publikováno v:
Carbohydrate research. 491
O-Glycopeptides derived from natural bioresources are an attractive material for a variety of purposes. Whey protein products are used as a human dietary supplement and in animal feed and are a readily available resource for the preparation of O-glyc
Autor:
Mamoru Mizuno, Akio Matsuda, Junko Amano, Yoshio Takada, Kenji Osumi, Sugawara Shuichi, Masaki Kurogochi, Shou Takashima
Publikováno v:
Glycobiology. 30(11)
Endo-β-N-acetylglucosaminidases are enzymes that hydrolyze the N,N′-diacetylchitobiose unit of N-glycans. Many endo-β-N-acetylglucosaminidases also exhibit transglycosylation activity, which corresponds to the reverse of the hydrolysis reaction.
Publikováno v:
ChemistrySelect. 3:8193-8198
Autor:
Masaki Kurogochi, Takashi Shirai, Wataru Tsukimura, Kiyoshi Furukawa, Kaoru Takegawa, Masako Mori, Akio Matsuda, Kenji Osumi
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 81:2353-2359
Recently, the absence of a core-fucose residue in the N-glycan has been implicated to be important for enhancing antibody-dependent cellular cytotoxicity (ADCC) activity of immunoglobulin G monoclonal antibodies (mAbs). Here, we first prepared anti-H
Publikováno v:
Tetrahedron Letters. 61:151475
We demonstrated a novel site-specific method of protein PEGylation that is catalyzed by endo-β-N-acetylglucosaminidase (ENGase) with PEGylated oxazoline (1) as a donor. PEGylation via transglycosylation using 1 proceeded smoothly to GlcNAc compounds