ArticleMicrobiology (Reading, England)2018
Electrostatic interactions are important for chaperone-client interaction in vivo.
Article in Microbiology (Reading, England), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
12 citing papers in PubMed.
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Dual functionality of MDM2 in PROTACs expands the horizons of targeted protein degradation.Biomarker research · 2025Review
- Distantly related Alteromonas bacteriophages share tail fibers exhibiting properties of transient chaperone caps.Nature communications · 2023Article
- Carrying Excess Baggage Can Slowdown Life: Protein Clearance Machineries That Go Awry During Aging and the Relevance of Maintaining Them.Molecular neurobiology · 2022Review
- Cell Non-autonomous Proteostasis Regulation in Aging and Disease.Frontiers in neuroscience · 2022Review
- Binding with heat shock cognate protein HSC70 fine-tunes the Golgi association of the small GTPase ARL5B.The Journal of biological chemistry · 2021Article
- The interactions of molecular chaperones with client proteins: why are they so weak?The Journal of biological chemistry · 2021Review
- Stress-Responsive Periplasmic Chaperones in Bacteria.Frontiers in molecular biosciences · 2021Review
- Why? - Successful Pseudomonas aeruginosa clones with a focus on clone C.FEMS microbiology reviews · 2020Review
- Increased surface charge in the protein chaperone Spy enhances its anti-aggregation activity.The Journal of biological chemistry · 2020Article
- Protein aggregation in bacteria.FEMS microbiology reviews · 2020Review
- The proteostasis network and its decline in ageing.Nature reviews. Molecular cell biology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
It has long been thought that chaperones are primarily attracted to their clients through the hydrophobic effect. However, in in vitro studies on the interaction between the chaperone Spy and its substrate Im7, we recently showed that long-range electrostatic interactions also play a key role. Spy functions in the periplasm of Gram-negative bacteria, which is surrounded by a permeable outer membrane. The ionic conditions in the periplasm therefore closely mimic those in the media, which allowed us to vary the ionic strength of the in vivo folding environment. Using folding biosensors that link protein folding to antibiotic resistance, we were able to monitor Spy chaperone activity in Escherichia coli in vivo as a function of media salt concentration. The chaperone activity of Spy decreased when the ionic strength of the media was increased, strongly suggesting that electrostatic forces play a vital role in the action of Spy in vivo.
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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.