Induction of protein body formation in plant leaves by elastin-like polypeptide fusions - Wikidata - awgldk - TriplyDB

Induction of protein body formation in plant leaves by elastin-like polypeptide fusions

Induction of protein body formation in plant leaves by elastin-like polypeptide fusions

http://www.wikidata.org/entity/Q33491793

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Protein Bodies in Leaves Exchange Contents through the Endoplasmic Reticulum The Encapsulation of Hemagglutinin in Protein Bodies Achieves a Stronger Immune Response in Mice than the Soluble Antigen The expression of a xylanase targeted to ER-protein bodies provides a simple strategy to produce active insoluble enzyme polymers in tobacco plants Green to red photoconversion of GFP for protein tracking in vivo.Subcellular localization of Arabidopsis arogenate dehydratases suggests novel and non-enzymatic roles Influence of elastin-like polypeptide and hydrophobin on recombinant hemagglutinin accumulations in transgenic tobacco plants.Proteolysis of recombinant proteins in bioengineered plant cells A cost-effective ELP-intein coupling system for recombinant protein purification from plant production platform Relevant elements of a maize gamma-zein domain involved in protein body biogenesis.Elastin-like polypeptides as a promising family of genetically-engineered protein based polymers.The Induction of Recombinant Protein Bodies in Different Subcellular Compartments Reveals a Cryptic Plastid-Targeting Signal in the 27-kDa γ-Zein Sequence.Protein body formation in stable transgenic tobacco expressing elastin-like polypeptide and hydrophobin fusion proteins.Production of phytotoxic cationic α-helical antimicrobial peptides in plant cells using inducible promoters.Proteomic characterisation of endoplasmic reticulum-derived protein bodies in tobacco leaves Expression of hypoallergenic Der f 2 derivatives with altered intramolecular disulphide bonds induces the formation of novel ER-derived protein bodies in transgenic rice seeds Stable plastid transformation for high-level recombinant protein expression: promises and challenges.A Plant-Produced Bacteriophage Tailspike Protein for the Control of Salmonella.Comparison of membrane targeting strategies for the accumulation of the human immunodeficiency virus p24 protein in transgenic tobacco Protein body-inducing fusions for high-level production and purification of recombinant proteins in plants.Trafficking of endoplasmic reticulum-retained recombinant proteins is unpredictable in Arabidopsis thaliana.Dynamic trafficking of wheat γ-gliadin and of its structural domains in tobacco cells, studied with fluorescent protein fusions.High-level production of human interleukin-10 fusions in tobacco cell suspension cultures.Protein bodies: how the ER deals with high accumulation of recombinant proteins.Production of the Main Celiac Disease Autoantigen by Transient Expression in Nicotiana benthamiana.Expression of a new chimeric protein with a highly repeated sequence in tobacco cells.Comparative study of wheat low-molecular-weight glutenin and α-gliadin trafficking in tobacco cells.ELPylated haemagglutinins produced in tobacco plants induce potentially neutralizing antibodies against H5N1 viruses in mice.Protein bodies in nature and biotechnology.Scale-up of hydrophobin-assisted recombinant protein production in tobacco BY-2 suspension cells.Protein body formation in leaves of Nicotiana benthamiana: a concentration-dependent mechanism influenced by the presence of fusion tags.Identification of the region of rice 13 kDa prolamin essential for the formation of ER-derived protein bodies using a heterologous expression system.Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana.The production of recombinant cationic α-helical antimicrobial peptides in plant cells induces the formation of protein bodies derived from the endoplasmic reticulum.High CO2 concentration as an inductor agent to drive production of recombinant phytotoxic antimicrobial peptides in plant biofactories.Transient co-expression with three -glycosylation enzymes allows production of GalNAc--glycosylated Granulocyte-Colony Stimulating Factor in Maize 16-kD γ-zein forms very unusual disulfide-bonded polymers in the endoplasmic reticulum: implications for prolamin evolution Recombinant protein production in a variety of Nicotiana hosts: a comparative analysis

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P2860

Induction of protein body formation in plant leaves by elastin-like polypeptide fusions

http://www.wikidata.org/entity/Q33491793

description

2009 nî lūn-bûn

@nan

2009 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի օգոստոսին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Induction of protein body formation in plant leaves by elastin-like polypeptide fusions

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Induction of protein body formation in plant leaves by elastin-like polypeptide fusions.

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type

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Induction of protein body formation in plant leaves by elastin-like polypeptide fusions

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Induction of protein body formation in plant leaves by elastin-like polypeptide fusions.

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Induction of protein body formation in plant leaves by elastin-like polypeptide fusions

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Induction of protein body formation in plant leaves by elastin-like polypeptide fusions.

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Induction of protein body formation in plant leaves by elastin-like polypeptide fusions.

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Jim E Brandle

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Jussi J Joensuu

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Seed storage proteins: structures and biosynthesis

The green fluorescent protein

Exchange of protein molecules through connections between higher plant plastids

Influence of KDEL on the fate of trimeric or assembly-defective phaseolin: selective use of an alternative route to vacuoles

Retracted: An enhanced transient expression system in plants based on suppression of gene silencing by the p19 protein of tomato bushy stunt virus

Aggresomes, inclusion bodies and protein aggregation

Biogenesis of cytoplasmic membranous vesicles for plant potyvirus replication occurs at endoplasmic reticulum exit sites in a COPI- and COPII-dependent manner.

Overlapping functions of the four class XI myosins in Arabidopsis growth, root hair elongation, and organelle motility.

Green fluorescent protein rendered susceptible to proteolysis: positions for protease-sensitive insertions.

Endoplasmic reticulum export sites and Golgi bodies behave as single mobile secretory units in plant cells.

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