Evidence map›Paper›PMID 23151747›Full record

ArticleCurrent protocols in protein science2012

Preparation and extraction of insoluble (inclusion-body) proteins from Escherichia coli.

Ira Palmer, Paul T Wingfield

Abstract read
In one paragraph

Article in Current protocols in protein science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing 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

53 citing papers in PubMed.

  1. Article
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  10. A distinct, high-affinity, alkaline phosphatase facilitates occupation of P-depleted environments by marine picocyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Review
  12. Article
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  19. CRISPR-Cas9 Mediated Knockout ofMicroorganisms · 2022
    Article
  20. 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

2 authors.

Ira PalmerNational Institutes of Health, Bethesda, Maryland.
Paul T WingfieldNational Institutes of Health, Bethesda, Maryland.

Funding

Production Of HIV And HIV Related Proteins For Structural StudiesZIAAR041115 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2025
$16.9M
RECOMBINANT DNA PRODUCED HIV PROTEINS--PURIFICATION/STRUCTURAL CHARACTERZ01AR041115 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 1996 to 2008
$889k
Intramural NIH HHS Z01 AR041115
6 · The paper itself

Abstract

High-level expression of many recombinant proteins in Escherichia coli leads to the formation of highly aggregated protein commonly referred to as inclusion bodies. Inclusion bodies are normally formed in the cytoplasm; however, if a secretion vector is used, they can form in the periplasmic space. Inclusion bodies can be recovered from cell lysates by low-speed centrifugation. Following pre-extaction (or washing), protein is extracted from washed pellets using guanidine⋅HCl. The solubilized and unfolded protein is either directly folded or further purified by gel filtration in the presence of guanidine⋅HCl as described in this unit. A support protocol describes the removal of guanidine⋅HCl from column fractions so they can be monitored by SDS-PAGE.

Indexed as

Recombinant ProteinsCytoplasmEscherichia coliEscherichia coli ProteinsGenetic VectorsInclusion BodiesPeriplasmProtein FoldingSolubilityEscherichia coli ProteinsRecombinant Proteins

Identifiers

PMID23151747
PMCPMC3809847

What OpenQuestion holds

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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.