High-level synthesis of Johnson grass mosaic virus coat protein in Escherichia coli and its auto-assembly to form virus-like particles (Q45728659)

15 December 2017

title

High-level synthesis of Johnson grass mosaic virus coat protein in Escherichia coli and its auto-assembly to form virus-like particles (English)

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15 December 2017

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Manisha Saini

1

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15 December 2017

Sudhanshu Vrati

series ordinal

2

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15 December 2017

publication date

1 March 2003

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Protein Expression and Purification

15 December 2017

published in

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15 December 2017

volume

28

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15 December 2017

issue

1

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15 December 2017

page(s)

86-92

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Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines

15 December 2017

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Secondary structure of the ribosome binding site determines translational efficiency: a quantitative analysis

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Availability of a second upstream AUG can completely overcome inhibition of protein synthesis initiation engendered by mRNA secondary structure encompassing the start codon

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The N and C Termini of the Coat Proteins of Potyviruses Are Surface-located and the N Terminus Contains the Major Virus-specific Epitopes

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In vivo processing of N-terminal methionine in E. coli

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Codon bias at the 3'-side of the initiation codon is correlated with translation initiation efficiency in Escherichia coli

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A Japanese Encephalitis Virus Peptide Present on Johnson Grass Mosaic Virus-Like Particles Induces Virus-Neutralizing Antibodies and Protects Mice against Lethal Challenge

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Identifiers

DOI

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15 December 2017

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