ArticleNature methods2011
Visualizing a one-way protein encounter complex by ultrafast single-molecule mixing.
Article in Nature methods, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 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
59 citing papers in PubMed.
- Differences in α-synuclein conformational states in physiologically relevant pH/NaThe Analyst · 2026Article
- Time-Resolved Single-Molecule FRET Reveals Length-Dependent Nucleosome Decompaction by Poly(ADP-ribose).bioRxiv : the preprint server for biology · 2026Article
- Single-Molecule Techniques for Probing the Conformation, Dynamics and Interactions of Intrinsically Disordered Proteins.Biophysics reviews · 2025Article
- Quantitative analysis methods for free diffusion single-molecule FRET experiments.Current opinion in structural biology · 2025Review
- Advances in microfluidic mixers for time-resolved structural biology with X-rays.Biophysical reviews · 2025Review
- Integrated In-Plane Nanofluidic Devices for Resistive-Pulse Sensing.Annual review of analytical chemistry (Palo Alto, Calif.) · 2024Review
- Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Rapid droplet-based mixing for single-molecule spectroscopy.Nature methods · 2023Article
- Trends in Single-Molecule Total Internal Reflection Fluorescence Imaging and Their Biological Applications with Lab-on-a-Chip Technology.Sensors (Basel, Switzerland) · 2023Review
- Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model.bioRxiv : the preprint server for biology · 2023Article
- Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates.Angewandte Chemie (International ed. in English) · 2023Article
- Single-Molecule Two-Color Coincidence Detection of Unlabeled alpha-Synuclein Aggregates.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Article
- Choosing the Probe for Single-Molecule Fluorescence Microscopy.International journal of molecular sciences · 2022Review
- Module-Fluidics: Building Blocks for Spatio-Temporal Microenvironment Control.Micromachines · 2022Article
- The structural heterogeneity of α-synuclein is governed by several distinct subpopulations with interconversion times slower than milliseconds.Structure (London, England : 1993) · 2021Article
- FRET-based dynamic structural biology: Challenges, perspectives and an appeal for open-science practices.eLife · 2021Review
- Microfluidic approaches for the analysis of protein-protein interactions in solution.Biophysical reviews · 2020Review
- The liquid state of FG-nucleoporins mimics permeability barrier properties of nuclear pore complexes.The Journal of cell biology · 2020Article
- Single-molecule detection on a portable 3D-printed microscope.Nature communications · 2019Article
- Single-molecule fluorescence studies of intrinsically disordered proteins and liquid phase separation.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
Corrections and comments
- Commented on by
Authors and funding
6 authors.
Funding
Abstract
We combined rapid microfluidic mixing with single-molecule fluorescence resonance energy transfer to study the folding kinetics of the intrinsically disordered human protein α-synuclein. The time-resolution of 0.2 ms revealed initial collapse of the unfolded protein induced by binding with lipid mimics and subsequent rapid formation of transient structures in the encounter complex. The method also enabled analysis of rapid dissociation and unfolding of weakly bound complexes triggered by massive dilution.
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.