Evidence map›Paper›PMID 1705029›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1991

The use of sarkosyl in generating soluble protein after bacterial expression.

S Frankel, R Sohn, L Leinwand

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.7field-weighted citation impact, top 6% of its field
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

33 citing papers in PubMed, 130 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. A solution to the long-standing problem of actin expression and purification.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Purification of Tag-FreeBiochemistry · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
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  14. Article
  15. Histidine-tagged wild-type yeast actin: its properties and use in an approach for obtaining yeast actin mutants.Proceedings of the National Academy of Sciences of the United States of America · 1999
    Article
  16. Article
  17. Article
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  19. Activation of c-Jun N-terminal kinase in bacterial lipopolysaccharide-stimulated macrophages.Proceedings of the National Academy of Sciences of the United States of America · 1996
    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

3 authors at 1 institution in 1 country.

S FrankelDepartment of Microbiology and Immunology, Albert Einstein College of Medicine, Bronx, NY 10461.
R Sohn
L Leinwand
Albert Einstein College of Medicine · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007288 · NIGMS · YESHIVA UNIVERSITY · PI AKABAS, MYLES H. · 1985 to 2022
$35.6M
MYOSIN GENE DIVERSITY AND FUNCTIONR01GM029090 · NIGMS · YESHIVA UNIVERSITY · PI Leslie Anne Leinwand · 1985 to 2026
$12.3M
GENETICS AND BIOCHEMISTRY OF CELLULAR REGULATIONT32GM007128 · NIGMS · YESHIVA UNIVERSITY · PI STANLEY, PAMELA M · 1985 to 1996
–
NIGMS NIH HHS 5T32 GM07128NIGMS NIH HHS GM29090NIGMS NIH HHS T32 GM7288
6 · The paper itself

Abstract

Actin, like many other proteins, is highly insoluble after expression in Escherichia coli. In order to understand the origin of insoluble aggregates, we asked whether morphological inclusions were always correlated with insolubility. The strain expressing actin was compared to one that expresses part of the myosin tail; the latter strain yields soluble protein after various cell lysis or disruption procedures. Morphological inclusions were observed in both strains, indicating there is no obligate relationship between solubility and inclusions. Studies presented here suggest that extreme insolubility results from coaggregation of the actin with bacterial outer membrane components upon bacterial lysis. The properties of the outer membrane have been exploited in the development of nondenaturing procedures that yield soluble actin. One procedure involves the disruption of coaggregates with sarkosyl detergent (N-laurylsarcosine); another prevents the formation of coaggregates by lysing in the presence of sarkosyl. These methods may be useful for other proteins that become insoluble after bacterial expression.

Indexed as

Bacterial Outer Membrane ProteinsBlotting, WesternDetergentsElectrophoresis, Polyacrylamide GelEscherichia coliMicroscopy, ElectronMolecular WeightMyosinsRecombinant ProteinsSarcosineSolubilityBacterial Outer Membrane ProteinsDetergentsMyosinsRecombinant ProteinsSarcosinesarkosyl

Identifiers

PMID1705029
PMCPMC50983
OpenAlexW2064285509

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.