ReviewProtein science : a publication of the Protein Society2017
The chaperone toolbox at the single-molecule level: From clamping to confining.
Review in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed.
- Protein Quality Control is a Master Modulator of Molecular Evolution in Bacteria.Genome biology and evolution · 2025Review
- Looking at Biomolecular Interactions through the Lens of Correlated Fluorescence Microscopy and Optical Tweezers.International journal of molecular sciences · 2023Review
- Single-molecule mechanical studies of chaperones and their clients.Biophysics reviews · 2022Review
- Protein Nanomechanics.Nanomaterials (Basel, Switzerland) · 2022Article
- Direct observation of chaperone-modulated talin mechanics with single-molecule resolution.Communications biology · 2022Article
- Picturing protein disaggregation.Nature chemical biology · 2022Article
- Chaperonin Abundance Enhances Bacterial Fitness.Frontiers in molecular biosciences · 2021Article
- Effects of Ligand Binding on the Energy Landscape of Acyl-CoA-Binding Protein.Biophysical journal · 2020Article
- Simultaneous sensing and imaging of individual biomolecular complexes enabled by modular DNA-protein coupling.Communications chemistry · 2020Article
- Small heat shock proteins: multifaceted proteins with important implications for life.Cell stress & chaperones · 2019Article
- The Molecular Chaperone HSP90 Promotes Notch Signaling in the Germline ofG3 (Bethesda, Md.) · 2018Article
- Folding while bound to chaperones.Current opinion in structural biology · 2018Review
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- Folding of maltose binding protein outside of and in GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Linking Microbial Community Structure and Function During the Acidified Anaerobic Digestion of Grass.Frontiers in microbiology · 2018Article
- Single-molecule fluorescence-based approach reveals novel mechanistic insights into human small heat shock protein chaperone function.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein folding is well known to be supervised by a dedicated class of proteins called chaperones. However, the core mode of action of these molecular machines has remained elusive due to several reasons including the promiscuous nature of the interactions between chaperones and their many clients, as well as the dynamics and heterogeneity of chaperone conformations and the folding process itself. While troublesome for traditional bulk techniques, these properties make an excellent case for the use of single-molecule approaches. In this review, we will discuss how force spectroscopy, fluorescence microscopy, FCS, and FRET methods are starting to zoom in on this intriguing and diverse molecular toolbox that is of direct importance for protein quality control in cells, as well as numerous degenerative conditions that depend on it.
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.