Evidence map›Paper›PMID 22509487›Full record

ArticleCell reports2012

FoldEco: a model for proteostasis in E. coli.

Evan T Powers, David L Powers, Lila M Gierasch

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
3.5field-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

45 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Enhancement of heat resistance ofEngineering microbiology · 2026
    Article
  3. Review
  4. Protein homeostasis imprinting across evolution.NAR genomics and bioinformatics · 2024
    Article
  5. A proteome-wide map of chaperone-assisted protein refolding in a cytosol-like milieu.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Proteostasis collapse is a driver of cell aging and death.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Controlling and quantifying protein concentration in Escherichia coli.Protein science : a publication of the Protein Society · 2019
    Article
  19. 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 3 institutions in 1 country.

Evan T PowersDepartment of Chemistry, The Scripps Research Institute, La Jolla, CA 92037, USA. epowers@scripps.edu
David L Powers
Lila M Gierasch
Clarkson University · USScripps Research Institute · USUniversity of Massachusetts Amherst · US

Funding

PEPTIDE CONFORMATIONS &INTERACTIONS WITH MEMBRANESR01GM027616 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI GIERASCH, LILA M · 1985 to 2015
$5.3M
NIH DIRECTOR'S PIONEER AWARDDP1OD000945 · OD · UNIVERSITY OF MASSACHUSETTS AMHERST · PI GIERASCH, LILA M · 2006 to 2010
$3.9M
NIGMS NIH HHS GM027616NIGMS NIH HHS R01 GM027616NIH HHS DP1 OD000945NIH HHS OD000945
6 · The paper itself

Abstract

To gain insight into the interplay of processes and species that maintain a correctly folded, functional proteome, we have developed a computational model called FoldEco. FoldEco models the cellular proteostasis network of the E. coli cytoplasm, including protein synthesis, degradation, aggregation, chaperone systems, and the folding characteristics of protein clients. We focused on E. coli because much of the needed input information--including mechanisms, rate parameters, and equilibrium coefficients--is available, largely from in vitro experiments; however, FoldEco will shed light on proteostasis in other organisms. FoldEco can generate hypotheses to guide the design of new experiments. Hypothesis generation leads to system-wide questions and shows how to convert these questions to experimentally measurable quantities, such as changes in protein concentrations with chaperone or protease levels, which can then be used to improve our current understanding of proteostasis and refine the model. A web version of FoldEco is available at http://foldeco.scripps.edu.

Indexed as

Models, BiologicalProtein FoldingSoftwareComputational BiologyEscherichia coliEscherichia coli ProteinsInternetKineticsProtein BiosynthesisProtein Structure, QuaternaryProteolysisProteomeSubstrate SpecificityEscherichia coli ProteinsProteome

Identifiers

PMID22509487
PMCPMC3324317
OpenAlexW2165460335

What OpenQuestion holds

Textmetadata
LicenceTDM
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.