Evidence map›Paper›PMID 18429271›Full record

ArticleCurrent protocols in protein science2004

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, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Trial
  2. Article
  3. Article
  4. A Novel Method to Monitor the Evolution of Antimicrobial Resistance inInternational journal of molecular sciences · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Structure-Based Design of an RNase Chimera for Antimicrobial Therapy.International journal of molecular sciences · 2021
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Harnessing synthetic biology to enhance heterologous protein expression.Protein science : a publication of the Protein Society · 2020
    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

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; alternatively, if a secretion vector is used, they can form in the periplasmic space. Inclusion bodies can be recovered from cell lysates and this unit describes preparation of washed pellets and solubilization of the protein using guanidine x HCl. The extracted protein, which is unfolded, is either directly folded as described in UNIT or further purified by gel filtration in the presence of guanidine x HCl as idescribed here. A support protocol describes the removal of guanidine x HCl from column fractions so they can be monitored by SDS-PAGE.

Indexed as

Chromatography, GelElectrophoresis, Polyacrylamide GelEscherichia coliGuanidineRecombinant ProteinsSolubilityUreaGuanidineRecombinant ProteinsUrea

Identifiers

PMID18429271
PMCPMC3518028

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.