DC Field | Value | Language |
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dc.contributor.author | K Ko | - |
dc.contributor.author | M H Ahn | - |
dc.contributor.author | M Song | - |
dc.contributor.author | Y K Choo | - |
dc.contributor.author | Hyun Soon Kim | - |
dc.contributor.author | K Ko | - |
dc.contributor.author | Hyouk Joung | - |
dc.date.accessioned | 2017-04-19T09:11:09Z | - |
dc.date.available | 2017-04-19T09:11:09Z | - |
dc.date.issued | 2008 | - |
dc.identifier.issn | 1016-8478 | - |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/8493 | - |
dc.description.abstract | Many therapeutic glycoproteins have been successfully generated in plants. Plants have advantages regarding practical and economic concerns, and safety of protein production over other existing systems. However, plants are not ideal expression systems for the production of biopharmaceutical proteins, due to the fact that they are incapable of the authentic human N-glycosylation process. The majority of therapeutic proteins are glycoproteins which harbor N-glycans, which are often essential for their stability, folding, and biological activity. Thus, several glyco-engineering strategies have emerged for the tailor-making of N-glycosylation in plants, including glycoprotein subcellular targeting, the inhibition of plant specific glycosyltranferases, or the addition of human specific glycosyltransferases. This article focuses on plant N-glycosylation structure, glycosylation variation in plant cell, plant expression system of glycoproteins, and impact of glycosylation on immunological function. Furthermore, plant glyco-engineering techniques currently being developed to overcome the limitations of plant expression systems in the production of therapeutic glycoproteins will be discussed in this review. | - |
dc.publisher | Korea Soc-Assoc-Inst | - |
dc.title | Glyco-engineering of biotherapeutic proteins in plants | - |
dc.title.alternative | Glyco-engineering of biotherapeutic proteins in plants | - |
dc.type | Article | - |
dc.citation.title | Molecules and Cells | - |
dc.citation.number | 4 | - |
dc.citation.endPage | 503 | - |
dc.citation.startPage | 494 | - |
dc.citation.volume | 25 | - |
dc.contributor.affiliatedAuthor | Hyun Soon Kim | - |
dc.contributor.affiliatedAuthor | Hyouk Joung | - |
dc.contributor.alternativeName | 고기성 | - |
dc.contributor.alternativeName | 안미현 | - |
dc.contributor.alternativeName | 송미라 | - |
dc.contributor.alternativeName | 추영국 | - |
dc.contributor.alternativeName | 김현순 | - |
dc.contributor.alternativeName | 고기남 | - |
dc.contributor.alternativeName | 정혁 | - |
dc.identifier.bibliographicCitation | Molecules and Cells, vol. 25, no. 4, pp. 494-503 | - |
dc.subject.keyword | glycoprotein | - |
dc.subject.keyword | glycosylation | - |
dc.subject.keyword | molecular biopharming | - |
dc.subject.keyword | monoclonal antibody | - |
dc.subject.keyword | recombinant protein | - |
dc.subject.keyword | transgenic plant | - |
dc.subject.local | Glycoprotein | - |
dc.subject.local | Glycoproteins | - |
dc.subject.local | glycoprotein | - |
dc.subject.local | glycoproteins | - |
dc.subject.local | glycosylation | - |
dc.subject.local | Glycosylation | - |
dc.subject.local | molecular biopharming | - |
dc.subject.local | Monoclonal antibody (mAb) | - |
dc.subject.local | Monoclonal antibodies | - |
dc.subject.local | Monoclonal Antibodies | - |
dc.subject.local | Monoclonal antibody | - |
dc.subject.local | monoclonal antibody | - |
dc.subject.local | Monoclonal Antibody | - |
dc.subject.local | monoclonal antibodies | - |
dc.subject.local | Recombinant Protein | - |
dc.subject.local | recombinant protein | - |
dc.subject.local | recombinant proteins | - |
dc.subject.local | Recombinant protein | - |
dc.subject.local | ecombinant proteins | - |
dc.subject.local | Recombinant proteins | - |
dc.subject.local | Trans-genic plants | - |
dc.subject.local | Transgenic Plant | - |
dc.subject.local | Transgenic plant | - |
dc.subject.local | Transgenic plants | - |
dc.subject.local | transgenic plant | - |
dc.description.journalClass | Y | - |
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