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

1

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Niklas Hellgren

2

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Susanne van Den Berg

3

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Helena Berglund

Structural proteomics of an archaeon

4

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language of work or name

English

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publication date

February 2002

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published in

Protein Science

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volume

11

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issue

2

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page(s)

313-21

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cites work

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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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Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein

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

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

27 November 2018

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inferred from PubMed ID database lookup

12 December 2020

based on heuristic

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PubMed

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

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

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

1 reference

PubMed

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