Directed evolution of single-chain Fv for cytoplasmic expression using the beta-galactosidase complementation assay results in proteins highly susceptible to protease degradation and aggregation (Q24803075)

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English	Directed evolution of single-chain Fv for cytoplasmic expression using the beta-galactosidase complementation assay results in proteins highly susceptible to protease degradation and aggregation	scientific article

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scholarly article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15606918%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

Directed evolution of single-chain Fv for cytoplasmic expression using the beta-galactosidase complementation assay results in proteins highly susceptible to protease degradation and aggregation (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15606918%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

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directed evolution

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protein evolution

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Pascal Philibert

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15606918%20AND%20SRC:MED&resulttype=core&format=json

6 January 2020

Pierre Martineau

2

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6 January 2020

author name string

Pascal Philibert

1

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Pierre Martineau

2

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publication date

17 December 2004

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6 January 2020

Microbial Cell Factories

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6 January 2020

3

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6 January 2020

1

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6 January 2020

16

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Directed evolution approach to a structural genomics project: Rv2002 from Mycobacterium tuberculosis

1 reference

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7 April 2017

High resolution refinement of β-galactosidase in a new crystal form reveals multiple metal-binding sites and provides a structural basis for α-complementation

1 reference

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1 reference

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

1 reference

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Characterization by in vitro complementation of a peptide corresponding to an operator-proximal segment of the β-galactosidase structural gene of Escherichia coli

1 reference

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Error-prone polymerase chain reaction for modification of scFvs

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Antigen-independent selection of stable intracellular single-chain antibodies

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IS186 insertion at a hot spot in the lon promoter as a basis for lon protease deficiency of Escherichia coli B: identification of a consensus target sequence for IS186 transposition

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Selection of antibodies for intracellular function using a two-hybrid in vivo system

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Proteolysis and chaperones: the destruction/reconstruction dilemma

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Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli

1 reference

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

1 reference

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Folding and association versus misfolding and aggregation of proteins

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The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La.

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Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli

1 reference

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1 reference

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1 reference

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In vitro folding and thermodynamic stability of an antibody fragment selected in vivo for high expression levels in Escherichia coli cytoplasm

1 reference

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12 December 2020

based on heuristic

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The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/15606918

12 December 2020

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inferred from PubMed ID database lookup

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

1 reference

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based on heuristic

inferred from PubMed ID database lookup

beta-Galactosidase alpha-complementation. Overlapping sequences

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Accessing the Kabat antibody sequence database by computer

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Production of fluorescent single-chain antibody fragments in Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/15606918

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based on heuristic

inferred from PubMed ID database lookup

Tolerance of Escherichia coli beta-galactosidase C-terminus to different-sized fusions

1 reference

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

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Identifiers

10.1186/1475-2859-3-16

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Europe PubMed Central

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6 January 2020

Dimensions Publication ID

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https://scigraph.springernature.com/pub.10.1186/1475-2859-3-16

9 September 2019

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Europe PubMed Central

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6 January 2020

PubMed publication ID

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6 January 2020

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