Evidence map›Paper›PMID 35089549›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2022

Overcoming the Solubility Problem in E. coli: Available Approaches for Recombinant Protein Production.

Claudia Ortega, Pablo Oppezzo, Agustín Correa

Abstract readReview
PubMed Publisher
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Insights into theInternational journal of molecular sciences · 2023
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Claudia OrtegaRecombinant Protein Unit, Institut Pasteur de Montevideo, Montevideo, Uruguay.
Pablo OppezzoRecombinant Protein Unit, Institut Pasteur de Montevideo, Montevideo, Uruguay.
Agustín CorreaRecombinant Protein Unit, Institut Pasteur de Montevideo, Montevideo, Uruguay. acorrea@pasteur.edu.uy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite the importance of recombinant protein production in the academy and industrial fields, many issues concerning the expression of soluble and homogeneous products are still unsolved. Several strategies were developed to overcome these obstacles; however, at present, there is no magic bullet that can be applied for all cases. Indeed, several key expression parameters need to be evaluated for each protein. Among the different hosts for protein expression, Escherichia coli is by far the most widely used. In this chapter, we review many of the different tools employed to circumvent protein insolubility problems.

Indexed as

Escherichia coliProteomicsRecombinant ProteinsSolubilityRecombinant ProteinsDirected evolutionE. coliHigh-throughput screeningInclusion bodiesProtein expressionRecombinant proteins

Identifiers

PMID35089549

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.