ArticleNature communications2021
Two-colour single-molecule photoinduced electron transfer fluorescence imaging microscopy of chaperone dynamics.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- Distinct phosphorylation mechanisms as dynamic switches for Hsp90 regulation.Nature communications · 2026Article
- Single molecule spectrum dynamics imaging with 3D target-locking tracking.Nature communications · 2025Article
- Advancing Single-Molecule Biophysics: Next-Generation Organic Fluorophores with Tailored Labeling Strategies.Chemical & biomedical imaging · 2025Review
- ATP plays a structural role in Hsp90 function.Nature communications · 2025Article
- Recent advances in detection techniques for vitamin analysis: A comprehensive review.Food chemistry: X · 2025Review
- The known unknowns of the Hsp90 chaperone.eLife · 2024Review
- The dynamic triage interplay of Hsp90 with its chaperone cycle and client binding.Nature communications · 2024Article
- Artificial Intelligence-Guided Gut-Microenvironment-Triggered Imaging Sensor Reveals Potential Indicators of Parkinson's Disease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- The Onset of Molecule-Spanning Dynamics in Heat Shock Protein Hsp90.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function.Essays in biochemistry · 2023Article
- Nucleotide exchange is sufficient for Hsp90 functions in vivo.Nature communications · 2023Article
- Review of FRET biosensing and its application in biomolecular detection.American journal of translational research · 2023Review
- Visualizing the transiently populated closed-state of human HSP90 ATP binding domain.Nature communications · 2022Article
- A dual-responsive doxorubicin-indoximod conjugate for programmed chemoimmunotherapy.RSC chemical biology · 2022Article
- Advances towards Understanding the Mechanism of Action of the Hsp90 Complex.Biomolecules · 2022Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many proteins are molecular machines, whose function is dependent on multiple conformational changes that are initiated and tightly controlled through biochemical stimuli. Their mechanistic understanding calls for spectroscopy that can probe simultaneously such structural coordinates. Here we present two-colour fluorescence microscopy in combination with photoinduced electron transfer (PET) probes as a method that simultaneously detects two structural coordinates in single protein molecules, one colour per coordinate. This contrasts with the commonly applied resonance energy transfer (FRET) technique that requires two colours per coordinate. We demonstrate the technique by directly and simultaneously observing three critical structural changes within the Hsp90 molecular chaperone machinery. Our results reveal synchronicity of conformational motions at remote sites during ATPase-driven closure of the Hsp90 molecular clamp, providing evidence for a cooperativity mechanism in the chaperone's catalytic cycle. Single-molecule PET fluorescence microscopy opens up avenues in the multi-dimensional exploration of protein dynamics and allosteric mechanisms.
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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.