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A step ahead: combining protein purification and correct folding selection

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A step ahead: combining protein purification and correct folding selection (English)

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Ario de Marco

1

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publication date

2004

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published in

Microbial Cell Factories

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volume

3

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issue

1

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page(s)

12

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cites work

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Protein aggregation as bacterial inclusion bodies is reversible

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28 September 2017

Bacteria co-transformed with recombinant proteins and chaperones cloned in independent plasmids are suitable for expression tuning

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28 November 2018

Recombinant proteins fused to thermostable partners can be purified by heat incubation

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Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.

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Gene expression response to misfolded protein as a screen for soluble recombinant protein

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A strategy for optimizing the monodispersity of fusion proteins: application to purification of recombinant HPV E6 oncoprotein

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Rapid protein-folding assay using green fluorescent protein

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The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network

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https://pubmed.ncbi.nlm.nih.gov/15471550

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Formation of soluble inclusion bodies by hpv e6 oncoprotein fused to maltose-binding protein

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Aggregation-resistant domain antibodies selected on phage by heat denaturation

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Protein solubility and folding monitored in vivo by structural complementation of a genetic marker protein

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https://pubmed.ncbi.nlm.nih.gov/15471550

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12 December 2020

based on heuristic

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Identifiers

DOI

10.1186/1475-2859-3-12

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Dimensions Publication ID

1022604397

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PMC publication ID

524515

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PubMed publication ID

15471550

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ResearchGate publication ID

8243348

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(Q24806060)

A step ahead: combining protein purification and correct folding selection

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