Zobrazeno 1 - 10
of 42
pro vyhledávání: '"Takatoshi Ohkuri"'
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
Abstract Generally, intermolecular disulfide bond contribute to the conformational protein stability. To identify sites where intermolecular disulfide bond can be introduced into the Fab’s constant domain of the therapeutic IgG, Fab mutants were pr
Externí odkaz:
https://doaj.org/article/bd98ac20ab994f19be7387966c045670
Publikováno v:
Biochemistry and Biophysics Reports, Vol 20, Iss , Pp - (2019)
During treatment with protein therapeutics, such as monoclonal antibodies, the development of anti-drug antibodies is a serious side-effect of modern pharmacology. Anti-drug antibodies are produced as the number and exposure to therapeutic proteins i
Externí odkaz:
https://doaj.org/article/d602119382244a9aa951c1c8d0e68134
Autor:
Hitomi Nakamura, Noritaka Hashii, Takatoshi Ohkuri, Makoto Anraku, Naoko Oda-Ueda, Masato Kiyoshi, Tadashi Ueda
Publikováno v:
The Journal of Biochemistry. 169:435-443
Glycoengineering of therapeutic proteins has been applied to improve the clinical efficacy of several therapeutics. Here, we examined the effect of glycosylation on the properties of the Fab of the therapeutic antibody, adalimumab. An N-glycosylation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c1e91cc6c4d40a49053170ec73ed915
https://doi.org/10.1093/jb/mvaa116
https://doi.org/10.1093/jb/mvaa116
Publikováno v:
Biological and Pharmaceutical Bulletin. 43:418-423
Conjugation with polyethylene glycol (PEG) is performed to increase serum half-life of the Fab for clinical applications. However, current designs for recombinant Fab only allow PEGylation at the interchain SS bond (disulfide bond) at the C-terminal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b2bac92b545eb070183db611c784172
https://doi.org/10.1248/bpb.b19-00612
https://doi.org/10.1248/bpb.b19-00612
Publikováno v:
Journal of biochemistry. 172(1)
The introduction of intermolecular disulfide bonds by amino acid mutations is an effective method for stabilizing dimeric proteins. X-ray crystal structure of Fab of a therapeutic antibody, adalimumab, revealed the first loop of the CH1 domain to be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de6ebf771d21a07eaacb4d0835b1fdd6
https://pubmed.ncbi.nlm.nih.gov/35476872
https://pubmed.ncbi.nlm.nih.gov/35476872
Publikováno v:
Scientific Reports
Scientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
Scientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
Generally, intermolecular disulfide bond contribute to the conformational protein stability. To identify sites where intermolecular disulfide bond can be introduced into the Fab’s constant domain of the therapeutic IgG, Fab mutants were predicted u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e1ed5702cca379df4349a751bf71f96
https://doi.org/10.1038/s41598-021-92225-9
https://doi.org/10.1038/s41598-021-92225-9
Publikováno v:
Journal of biochemistry. 170(2)
Pichia pastoris is a popular eukaryotic system employed for the fast, simple and inexpensive production of recombinant protein including biotherapeutics such as human albumin. The CH2 domain of human Immunoglobulin G (IgG) is a promising scaffold for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::211bdf64f703aec9bf875aff9c372adc
https://pubmed.ncbi.nlm.nih.gov/33772592
https://pubmed.ncbi.nlm.nih.gov/33772592
Publikováno v:
Biochemical and Biophysical Research Communications. 495:7-11
We constructed a system for expressing the Fab of the therapeutic human monoclonal antibody adalimumab at a yield of 20 mg/L in the methylotrophic yeast Pichia pastoris. To examine the contribution of interchain disulfide bonds to conformational stab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ecb98f72052a23e60e57c42b6ad0938
https://doi.org/10.1016/j.bbrc.2017.10.140
https://doi.org/10.1016/j.bbrc.2017.10.140
Autor:
Tadashi Ueda, Yusuke Akama, Jun Ohtsuka, Shoichiro Horita, Yukari Sakiyama, Erika Miyazaki, Koji Nagata, Akitoshi Okada, Tsutomu Katayama, Masaru Tanokura, Takatoshi Ohkuri
Publikováno v:
Journal of biochemistry. 167(1)
Loading the bacterial replicative helicase DnaB onto DNA requires a specific loader protein, DnaC/DnaI, which creates the loading-competent state by opening the DnaB hexameric ring. To understand the molecular mechanism by which DnaC/DnaI opens the D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5db7918a74e12f0ce2ca29db29498f63
https://pubmed.ncbi.nlm.nih.gov/31665315
https://pubmed.ncbi.nlm.nih.gov/31665315
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1860:2279-2284
Background Protein antigens are degraded by endosomal protease in antigen presentation cell. T cells recognize peptides derived from antigen proteins bound to class II major histocompatibility complex molecules. We previously reported that an increas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff00ed19d6d6fd9e66cb8e865fb06be1
https://doi.org/10.1016/j.bbagen.2016.04.014
https://doi.org/10.1016/j.bbagen.2016.04.014