Evidence map›Paper›PMID 23219982›Full record

ArticleAnalytical biochemistry2013

In vivo detection and quantification of chemicals that enhance protein stability.

Tsinatkeab T Hailu, Linda Foit, James C A Bardwell

Abstract read
In one paragraph

Article in Analytical biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  2. Article
  3. Article
  4. Using protein engineering to understand and modulate aggregation.Current opinion in structural biology · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. 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.

Tsinatkeab T HailuHoward Hughes Medical Institute, Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Linda Foit
James C A Bardwell

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

We have devised protein-folding sensors that link protein stability to TEM-1 β-lactamase activity. The addition of osmolytes and other compounds with chemical chaperone activity to the growth medium of bacteria containing these sensors increases β-lactamase activity up to 207-fold in a dose-dependent manner. This enables the rapid detection and sensitive quantification of compounds that enhance in vivo protein stability.

Indexed as

Colorimetrybeta-LactamasesCarbohydratesCaseinsEscherichia coliLipidsMolecular ChaperonesPlant Proteins, DietaryProtein FoldingProtein Stabilitybeta-Lactamasesbeta-lactamase TEM-1CarbohydratesCaseinsLipidsMolecular ChaperonesOsmolitePlant Proteins, Dietary

Identifiers

PMID23219982
PMCPMC3670414

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.