Protein folding: Chaperoning protein evolution.

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

9 citing papers in PubMed.

1. Chemical rescue of mutant proteins in living Saccharomyces cerevisiae cells by naturally occurring small molecules.G3 (Bethesda, Md.) · 2021
   Article
2. The fitness cost and benefit of phase-separated protein deposits.Molecular systems biology · 2019
   Article
3. A conserved R type Methionine Sulfoxide Reductase reverses oxidized GrpEL1/Mge1 to regulate Hsp70 chaperone cycle.Scientific reports · 2018
   Article
4. Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease.Cellular and molecular life sciences : CMLS · 2017
   Review
5. Counteraction of Trehalose on N, N-Dimethylformamide-Induced Candida rugosa Lipase Denaturation: Spectroscopic Insight and Molecular Dynamic Simulation.PloS one · 2016
   Article
6. Methionine sulfoxide reductase 2 reversibly regulates Mge1, a cochaperone of mitochondrial Hsp70, during oxidative stress.Molecular biology of the cell · 2015
   Article
7. Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.Cellular and molecular life sciences : CMLS · 2014
   Review
8. Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK.Frontiers in molecular biosciences · 2014
   Article
9. Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates.The Journal of biological chemistry · 2013
   Article

Corrections and comments

• Comment on
  Chemical chaperones assist intracellular folding to buffer mutational variations.2012

Authors and funding

2 authors.

Funding

No grant is acknowledged in the PubMed record.

Abstract

PubMed holds no abstract for this paper.

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