Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli (Q28345106)

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scientific article

Language	Label	Description	Also known as
English	Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli	scientific article

Statements

scholarly article

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Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli (English)

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Escherichia coli

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5

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author name string

Martin Hammarström

1

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Niklas Hellgren

2

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Susanne van Den Berg

3

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Helena Berglund

4

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language of work or name

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publication date

February 2002

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Protein Science

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11

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2

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313-21

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

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Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Export of the Klenow polymerase into the periplasmic space

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Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase

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Protein production: feeding the crystallographers and NMR spectroscopists

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Recombinant protein expression in Escherichia coli

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Expression and purification of the first nucleotide-binding domain and linker region of human multidrug resistance gene product: comparison of fusions to glutathione S-transferase, thioredoxin and maltose-binding protein

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Solubility of proteins isolated from inclusion bodies is enhanced by fusion to maltose-binding protein or thioredoxin

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Major surface antigen p190 of Plasmodium falciparum: detection of common epitopes present in a variety of plasmodia isolates

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A synthetic IgG-binding domain based on staphylococcal protein A.

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Chelating peptide-immobilized metal ion affinity chromatography. A new concept in affinity chromatography for recombinant proteins

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2 June 2018

GATEWAY recombinational cloning: application to the cloning of large numbers of open reading frames or ORFeomes.

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21 January 2018

A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm.

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27 November 2018

Order of fusions between bacterial and mammalian proteins can determine solubility in Escherichia coli

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The Argonne Structural Genomics Workshop: Lamaze class for the birth of a new science

1 reference

https://pubmed.ncbi.nlm.nih.gov/11790841

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

New fusion protein systems designed to give soluble expression in Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/11790841

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1110/PS.22102

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release_a77exvsub5ddjei3epc4fbkaoe

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PMC publication ID

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PubMed publication ID

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