Fusion proteins towards fungi and bacteria in plant protection.

about

Fusion proteins towards fungi and bacteria in plant protection.

Item

http://www.wikidata.org/entity/Q47294731

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Fusion proteins towards fungi and bacteria in plant protection.

@en

Fusion proteins towards fungi and bacteria in plant protection.

@nl

type

Item

label

Fusion proteins towards fungi and bacteria in plant protection.

@en

Fusion proteins towards fungi and bacteria in plant protection.

@nl

prefLabel

Fusion proteins towards fungi and bacteria in plant protection.

@en

Fusion proteins towards fungi and bacteria in plant protection.

@nl

P1476

Fusion proteins towards fungi and bacteria in plant protection.

@en

P2093

Alexandra Carreira

http://www.w3.org/2001/XMLSchema#string

Ana Margarida Pinheiro

http://www.w3.org/2001/XMLSchema#string

Ricardo B Ferreira

http://www.w3.org/2001/XMLSchema#string

Sara Monteiro

http://www.w3.org/2001/XMLSchema#string

P2860

Expression of proteins in Escherichia coli as fusions with maltose-binding protein to rescue non-expressed targets in a high-throughput protein-expression and purification pipeline

Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused

A nontoxic polypeptide oligomer with a fungicide potency under agricultural conditions which is equal or greater than that of their chemical counterparts

High-throughput generation of small antibacterial peptides with improved activity.

The unique biosynthetic route from lupinus beta-conglutin gene to blad

Recombinant protein expression in Escherichia coli.

Bridging the Gap to Non-toxic Fungal Control: Lupinus-Derived Blad-Containing Oligomer as a Novel Candidate to Combat Human Pathogenic Fungi.

Design and characterization of structured protein linkers with differing flexibilities.

Recombinant protein expression in Escherichia coli: advances and challenges

A new method to customize protein expression vectors for fast, efficient and background free parallel cloning.

P304

11-19

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1099/MIC.0.000592

http://www.w3.org/2001/XMLSchema#string

P433

http://www.w3.org/2001/XMLSchema#string

P478

164

http://www.w3.org/2001/XMLSchema#string

P577

2017-12-14T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

29239714

http://www.w3.org/2001/XMLSchema#string

P932

5892777

http://www.w3.org/2001/XMLSchema#string