ReviewCurrent opinion in structural biology2013
The roles of conditional disorder in redox proteins.
Review in Current opinion in structural biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 55 citations in OpenAlex.
- Protein disulfide isomerase dissolves and detoxifies oligomeric assemblies of amyloid beta peptide.FEBS letters · 2026Article
- Shining light on the dark proteome with unstructural biology.Current research in structural biology · 2026Article
- Muscleblind-like proteins dimerize by forming disulfide bonds to regulate alternative splicing and pathogenic RNA foci formation.Nucleic acids research · 2026Article
- Muscleblind-like proteins dimerize by forming disulfide bonds to regulate alternative splicing and pathogenic RNA foci formation.bioRxiv : the preprint server for biology · 2026Article
- Fundamentals of redox regulation in biology.Nature reviews. Molecular cell biology · 2024Review
- Conformational Disorder Analysis of the Conditionally Disordered Protein CP12 fromInternational journal of molecular sciences · 2023Article
- HslO ameliorates arrested ΔrecA polA cell growth and reduces DNA damage and oxidative stress responses.Scientific reports · 2022Article
- Vitamin C Maintenance against Cell Growth Arrest and Reactive Oxygen Species Accumulation in the Presence of Redox Molecular ChaperoneInternational journal of molecular sciences · 2022Article
- A Trajectory of Discovery: Metabolic Regulation by the Conditionally Disordered Chloroplast Protein, CP12.Biomolecules · 2022Review
- Reduction in Phosphoribulokinase Amount and Re-Routing Metabolism inInternational journal of molecular sciences · 2022Article
- Experimental Evidence of Intrinsic Disorder and Amyloid Formation by theInternational journal of molecular sciences · 2022Article
- MemDis: Predicting Disordered Regions in Transmembrane Proteins.International journal of molecular sciences · 2021Article
- Flexibility of Oxidized and Reduced States of the Chloroplast Regulatory Protein CP12 in Isolation and in Cell Extracts.Biomolecules · 2021Article
- Small but Smart: On the Diverse Role of Small Proteins in the Regulation of Cyanobacterial Metabolism.Life (Basel, Switzerland) · 2020Review
- Bacterial Defense Systems against the Neutrophilic Oxidant Hypochlorous Acid.Infection and immunity · 2020Review
- Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions.Progress in molecular biology and translational science · 2020Review
- Structural basis of light-induced redox regulation in the Calvin-Benson cycle in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding.Nucleic acids research · 2018Article
- Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry.Journal of visualized experiments : JoVE · 2018Article
- Disulfide driven folding for a conditionally disordered protein.Scientific reports · 2017Article
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 2 institutions in 2 countries.
Funding
Abstract
Cells are constantly exposed to various oxidants, either generated endogenously due to metabolic activity or exogenously. One way that cells respond to oxidants is through the action of redox-regulated proteins. These proteins also play important roles in oxidant signaling and protein biogenesis events. The key sensors built into redox-regulated proteins are cysteines, which undergo reversible thiol oxidation in response to changes in the oxidation status of the cellular environment. In this review, we discuss three examples of redox-regulated proteins found in bacteria, mitochondria, and chloroplasts. These proteins use oxidation of their redox-sensitive cysteines to reversibly convert large structural domains into more disordered regions or vice versa. These massive structural rearrangements are directly implicated in the functions of these proteins.
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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.