Antibody degradation in tobacco plants: a predominantly apoplastic process
about
C-Terminally fused affinity Strep-tag II is removed by proteolysis from recombinant human erythropoietin expressed in transgenic tobacco plants.Engineering, expression in transgenic plants and characterisation of E559, a rabies virus-neutralising monoclonal antibody.Characterization of VRC01, a potent and broadly neutralizing anti-HIV mAb, produced in transiently and stably transformed tobacco.Expression and subcellular targeting of human complement factor C5a in Nicotiana speciesGeneration of biologically active multi-sialylated recombinant human EPOFc in plants.Growth suppression of colorectal cancer by plant-derived multiple mAb CO17-1A × BR55 via inhibition of ERK1/2 phosphorylation.Protection of recombinant mammalian antibodies from development-dependent proteolysis in leaves of Nicotiana benthamiana.Production of hybrid-IgG/IgA plantibodies with neutralizing activity against Shiga toxin 1.Identification, Characterization and Down-Regulation of Cysteine Protease Genes in Tobacco for Use in Recombinant Protein Production.An Accessory Protease Inhibitor to Increase the Yield and Quality of a Tumour-Targeting mAb in Nicotiana benthamiana LeavesCharacterization of a plant-produced recombinant human secretory IgA with broad neutralizing activity against HIVSite-targeted mutagenesis for stabilization of recombinant monoclonal antibody expressed in tobacco (Nicotiana tabacum) plants.Antibody proteolysis: a common picture emerging from plants.Expression of human butyrylcholinesterase with an engineered glycosylation profile resembling the plasma-derived orthologuePutative signal peptides of two BURP proteins can direct proteins to their destinations in tobacco cell system.Extracellular peptidase hunting for improvement of protein production in plant cells and roots.The human anti-HIV antibodies 2F5, 2G12, and PG9 differ in their susceptibility to proteolytic degradation: down-regulation of endogenous serine and cysteine proteinase activities could improve antibody production in plant-based expression platformsSite-specific proteolytic degradation of IgG monoclonal antibodies expressed in tobacco plants.The transcriptome, extracellular proteome and active secretome of agroinfiltrated Nicotiana benthamiana uncover a large, diverse protease repertoire.Three unrelated protease inhibitors enhance accumulation of pharmaceutical recombinant proteins in N. benthamiana.An Effective Way of Producing Fully Assembled Antibody in Transgenic Tobacco Plants by Linking Heavy and Light Chains via a Self-Cleaving 2A PeptideAnti-inflammatory actions of plant-derived multiple monoclonal antibody CO17-1A × BR55 related with anti-cancer effects in AOM/DSS-induced colorectal cancer mouse via down-regulating of ERK1/2
P2860
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P2860
Antibody degradation in tobacco plants: a predominantly apoplastic process
description
2011 nî lūn-bûn
@nan
2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
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2011年学术文章
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2011年学术文章
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2011年学术文章
@zh-hans
2011年学术文章
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2011年学术文章
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2011年學術文章
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Antibody degradation in tobacco plants: a predominantly apoplastic process
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Antibody degradation in tobacco plants: a predominantly apoplastic process
@en
Antibody degradation in tobacco plants: a predominantly apoplastic process
@nl
type
label
Antibody degradation in tobacco plants: a predominantly apoplastic process
@ast
Antibody degradation in tobacco plants: a predominantly apoplastic process
@en
Antibody degradation in tobacco plants: a predominantly apoplastic process
@nl
prefLabel
Antibody degradation in tobacco plants: a predominantly apoplastic process
@ast
Antibody degradation in tobacco plants: a predominantly apoplastic process
@en
Antibody degradation in tobacco plants: a predominantly apoplastic process
@nl
P2860
P50
P356
P1433
P1476
Antibody degradation in tobacco plants: a predominantly apoplastic process
@en
P2093
Matthew J Paul
Verena K Hehle
P2860
P2888
P356
10.1186/1472-6750-11-128
P577
2011-12-30T00:00:00Z
P5875
P6179
1028936332