(Q48050941)

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Optimization of a heterologous signal peptide by site-directed mutagenesis for improved secretion of recombinant proteins in Escherichia coli.

scientific article published on 23 March 2012

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22456489%20AND%20SRC:MED&resulttype=core&format=json

27 January 2020

Optimization of a heterologous signal peptide by site-directed mutagenesis for improved secretion of recombinant proteins in Escherichia coli (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22456489%20AND%20SRC:MED&resulttype=core&format=json

27 January 2020

Escherichia coli

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based on heuristic

inferred from title

7

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27 January 2020

author name string

Mohd Anuar Jonet

1

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27 January 2020

Nor Muhammad Mahadi

2

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27 January 2020

Abdul Munir Abdul Murad

3

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27 January 2020

Amir Rabu

4

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27 January 2020

Farah Diba Abu Bakar

5

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27 January 2020

Raha Abdul Rahim

6

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27 January 2020

Rosli Md Illias

8

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27 January 2020

publication date

23 March 2012

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27 January 2020

Journal of Molecular Microbiology and Biotechnology

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27 January 2020

22

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27 January 2020

1

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27 January 2020

48-58

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27 January 2020

describes a project that uses

site-directed mutagenesis

1 reference

based on heuristic

inferred from title

Recombinant protein expression in Escherichia coli

1 reference

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21 January 2018

Positively charged lysine at the N-terminus of the signal peptide of the Escherichia coli alkaline phosphatase provides the secretion efficiency and is involved in the interaction with anionic phospholipids.

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21 January 2018

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21 January 2018

Juxtaposition of signal-peptide charge and core region hydrophobicity is critical for functional signal peptides.

1 reference

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21 January 2018

Growth rate-dependent changes in Escherichia coli membrane structure and protein leakage

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21 January 2018

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21 January 2018

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