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이병성 한국기독교학회 2019 한국기독교신학논총 Vol.113 No.-
Japanese colonialists viewed religious freedom as a modern and “civilized” value, and promised to guarantee religious freedom to Protestant missionaries. However, missionaries’ interpretations of religious freedom were very different from those of colonialists. The civilization-oriented understanding of Protestant missions provided a broad view of religious freedom. Missionaries saw the public role of religious practices, educational freedom, and the institutional autonomy of religious institutions as constituting elements of their religious freedom. However, Japanese colonizers saw such a liberal understanding of religious freedom as a political threat. Colonialists sought to monopolize the political and educational domains, and so the colonial power put a fundamental limit on the political dimension of religious freedom by privatizing and depoliticizing religious beliefs and practices, excluding religious influences from public education, and encroaching upon the institutional autonomy of Protestant institutions. This colonial policy on religious freedom necessarily brought colonialists into conflict with Protestant missionaries. Nevertheless, most Protestant missionaries were not antagonistic toward Japanese, at least until the rise of Shinto controversy in the mid-1930s. They supported colonial political order, offering theological legitimation to the regime. Missionaries saw political stability and public security as a necessary condition for religious freedom.
이병성,이유미,이상우,박지수,정보석,조미경,정상택,유태현 한국공업화학회 2019 한국공업화학회 연구논문 초록집 Vol.2019 No.1
Immunotoxins consisting of a toxin from bacteria or plants, and a targeting module have been developed as potent anti-cancer therapeutics. The majority of them, especially those in preclinical or clinical testing stages, are based on antibody fragments, even though the advantage of using full-length antibodies has been well documented. Here, we generated an immunotoxin via site-specific conjugation using a cysteine (Cys) residue introduced to IgG and a bio-orthogonally reactive unnatural amino acid. A Her2-targeting IgG, trastuzumab, was engineered to have an unpaired Cys at position 425 in the heavy chain, and an unnatural amino acid having the azido group (azidophenylalanine) was incorporated into an engineered Pseudomonas exotoxin A (PE24). The two protein molecules were conjugated site-specifically using a bifunctional linker having dibenzocyclooctyne and maleimide groups. The resulting trastuzumab-PE24 conjugate was cytotoxic to Her2-overexpressing cell lines.