ArticleProtein science : a publication of the Protein Society1996
Influence of the GroE molecular chaperone machine on the in vitro refolding of Escherichia coli beta-galactosidase.
Article in Protein science : a publication of the Protein Society, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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
14 citing papers in PubMed, 46 citations in OpenAlex.
- Towards a generic prototyping approach for therapeutically-relevant peptides and proteins in a cell-free translation system.Nature communications · 2022Article
- Production of a toxic polypeptide as a fusion inside GroEL cavity.Scientific reports · 2020Article
- Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution.Biomolecules · 2020Article
- Single-Ring Intermediates Are Essential for Some Chaperonins.Frontiers in molecular biosciences · 2018Article
- Screening of Neem extracts for microbial anti-chaperone activity by employing in vitro enzyme refolding assay.3 Biotech · 2017Article
- Ring Separation Highlights the Protein-Folding Mechanism Used by the Phage EL-Encoded Chaperonin.Structure (London, England : 1993) · 2016Article
- Ternary system of solution additives with arginine and salt for refolding of beta-galactosidase.The protein journal · 2010Article
- Reconciling theories of chaperonin accelerated folding with experimental evidence.Cellular and molecular life sciences : CMLS · 2010Review
- Localization of chaperones DnaK and GroEL in bacterial inclusion bodies.Journal of bacteriology · 2005Article
- Misfolded forms of glyceraldehyde-3-phosphate dehydrogenase interact with GroEL and inhibit chaperonin-assisted folding of the wild-type enzyme.Protein science : a publication of the Protein Society · 2005Article
- Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity.Protein science : a publication of the Protein Society · 2004Article
- Recombinant protein folding and misfolding in Escherichia coli.Nature biotechnology · 2004Review
- ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Protein folding: how the mechanism of GroEL action is defined by kinetics.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have studied the effect of the components of the GroE molecular chaperone machine on the refolding of the Escherichia coli enzyme beta-galactosidase, a tetrameric protein whose 116-kDa promoters should not completely fit within the central cavity of the GroEL toroid. In the absence of other additives, GroEL formed a weak complex with chemically denatured beta-galactosidase, reduced its propensity to aggregate, and increased the recovery yields of active enzyme twofold without altering its folding pathway. When present together with the chaperonin, ATP--and to a lesser extent AMP-PNP--reduced the recovery yields and led to the resumption of aggregation. The use of the complete chaperonin system (GroEL, GroES, and ATP) eliminated the GroEL-mediated increase in recovery and folding proceeded less efficiently than in buffer alone. This unusual behavior can be explained in terms of a chaperonin "buffering" effect and the different affinities of GroE complexes for denatured beta-galactosidase.
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.