ArticleArXiv2026
Label-free Imaging of Single-Biomolecule Structure and Interaction by Stimulated Raman Photothermal Encoded Scattering.
Article in ArXiv, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
Current single molecule methods either rely on fluorescence or lack chemical information. Here we report stimulated Raman photothermal encoded scattering (SRPSCAT) microscopy for quantitative bond-selective imaging of single-biomolecule structures and interactions in native environments. In this approach, scattering of the target molecule is modulated by the deposited energy from stimulated Raman gain and loss processes, thereby encoding vibrational spectroscopic information. Leveraging single-molecule sensitivity of interferometric scattering, SRPSCAT can map single proteins with chemical specificity, determine their mass, and distinguish protein secondary structures based on their Raman fingerprints. Furthermore, single protein binding kinetics are quantified and the conformational dynamics of single de novo designed allosteric proteins are observed. Together, these results highlight the potential of SRPSCAT for label-free structural, functional and dynamic analysis at the single-molecule level.
Identifiers
41994174PMC13082132What 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.