ArticleThe Journal of biological chemistry2017
Local energetic frustration affects the dependence of green fluorescent protein folding on the chaperonin GroEL.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled 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.
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.
Who cites it
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.
- Differential proteostatic regulation of insoluble and abundant proteins.Bioinformatics (Oxford, England) · 2019Pooled it
- Chaperonin recognition of protein dynamics drives drug resistance.bioRxiv : the preprint server for biology · 2026Article
- Frustration in physiology and molecular medicine.Molecular aspects of medicine · 2025Review
- Codeine 3-O-demethylase catalyzed biotransformation of morphinan alkaloids in Escherichia coli: site directed mutagenesis of terminal residues improves enzyme expression, stability and biotransformation yield.Journal of biological engineering · 2025Article
- Synonymous and non-synonymous codon substitutions can alleviate dependence on GroEL for folding.Protein science : a publication of the Protein Society · 2024Article
- Designed active-site library reveals thousands of functional GFP variants.Nature communications · 2023Article
- Prediction of chaperonin GroE substrates using small structural patterns of proteins.FEBS open bio · 2023Article
- Review
- A diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilization.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- SystematicACS synthetic biology · 2022Article
- Friends in need: How chaperonins recognize and remodel proteins that require folding assistance.Frontiers in molecular biosciences · 2022Review
- Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization.eLife · 2020Article
- Successes and challenges in simulating the folding of large proteins.The Journal of biological chemistry · 2020Review
- Protein tolerance to random circular permutation correlates with thermostability and local energetics of residue-residue contacts.Protein engineering, design & selection : PEDS · 2019Article
- Contact Order Is a Determinant for the Dependence of GFP Folding on the Chaperonin GroEL.Biophysical journal · 2019Article
- Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The GroE chaperonin system in
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.