ArticleNature chemistry2011
Direct observation of disulfide isomerization in a single protein.
Article in Nature chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Force writes memory: proline isomerization as a molecular memory switch.Biochemical Society transactions · 2025Review
- The oxidative modification of transcription factor FOXM1 by Peroxiredoxin1 facilitates DNA damage repair and cancer progression.American journal of cancer research · 2025Article
- An innovative strategy for radical-mediated, bidirectional controlled disulfide exchange.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Synthetic exploration of electrophilic xanthylationChemical science · 2023Article
- Conformational antigenic heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.Retrovirology · 2023Article
- A Single-Molecule Strategy to Capture Non-native Intramolecular and Intermolecular Protein Disulfide Bridges.Nano letters · 2022Article
- Efficient preparation of unsymmetrical disulfides by nickel-catalyzed reductive coupling strategy.Nature communications · 2022Article
- Smart Flow Electrosynthesis and Application of Organodisulfides in Redox Flow Batteries.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- An ester bond underlies the mechanical strength of a pathogen surface protein.Nature communications · 2021Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Protein Hydrogels: The Swiss Army Knife for Enhanced Mechanical and Bioactive Properties of Biomaterials.Nanomaterials (Basel, Switzerland) · 2021Review
- Decarboxylative thiolation of redox-active esters to free thiols and further diversification.Nature communications · 2020Article
- Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway.Cells · 2020Review
- Unsymmetrical polysulfidation via designed bilateral disulfurating reagents.Nature communications · 2020Article
- The molecular mechanisms associated with the physiological responses to inflammation and oxidative stress in cardiovascular diseases.Biophysical reviews · 2020Review
- Catalytic site-selective substrate processing within a tubular nanoreactor.Nature nanotechnology · 2019Article
- The Mechanical Power of Titin Folding.Cell reports · 2019Article
- Maleimide-thiol adducts stabilized through stretching.Nature chemistry · 2019Article
- pDobz/pDobb protected diaminodiacid as a novel building block for peptide disulfide-bond mimic synthesis.RSC advances · 2019Article
- Redox regulation of protein nanomechanics in health and disease: Lessons from titin.Redox biology · 2019Review
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4 authors.
Funding
Abstract
Photochemical uncaging techniques use light to release active molecules from otherwise inert compounds. Here we expand this class of techniques by demonstrating the mechanical uncaging of a reactive species within a single protein. We proved this novel technique by capturing the regiospecific reaction between a thiol and a vicinal disulfide bond. We designed a protein that includes a caged cysteine and a buried disulfide. The mechanical unfolding of this protein in the presence of an external nucleophile frees the single reactive cysteine residue, which now can cleave the target disulfide via a nucleophilic attack on either one of its two sulfur atoms. This produces two different and competing reaction pathways. We used single-molecule force spectroscopy to monitor the cleavage of the disulfides, which extends the polypeptide by a magnitude unambiguously associated with each reaction pathway. This allowed us to measure, for the first time, the kinetics of disulfide-bond isomerization in a protein.
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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.