Evidence map›Paper›PMID 39231922›Full record

ArticleNature communications2024

Single-molecule digital sizing of proteins in solution.

Georg Krainer, Raphael P B Jacquat, Matthias M Schneider, Timothy J Welsh, Jieyuan Fan, Quentin A E Peter, Ewa A Andrzejewska, Greta Šneiderienė, Magdalena A Czekalska, Hannes Ausserwoeger and 10 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

20 authors.

Georg Krainer *Institute of Molecular Biosciences (IMB), University of Graz, Humboldtstraße 50, 8010, Graz, Austria. georg.krainer@uni-graz.at.ORCID 0000-0002-9626-7636
Raphael P B Jacquat *Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0002-8661-9722
Matthias M Schneider *Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0002-1894-1859
Timothy J Welsh *Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Jieyuan Fan *Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Quentin A E PeterCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Ewa A AndrzejewskaCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0002-1421-5569
Greta ŠneiderienėCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0002-4585-5091
Magdalena A CzekalskaCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0002-4494-4463
Hannes AusserwoegerCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0003-0762-8872
Lin ChaiCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
William E ArterCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.
Kadi L SaarCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0002-5926-3628
Therese W HerlingCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0002-1332-3090
Titus M FranzmannCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307, Dresden, Germany.ORCID 0000-0002-4281-7209
Vasilis KosmoliaptsisDepartment of Surgery, University of Cambridge, Addenbrooke's Hospital, Hills Road, Cambridge, CB2 0QQ, UK.ORCID 0000-0001-7298-1387
Simon AlbertiCenter for Molecular and Cellular Bioengineering, Biotechnology Center, Technische Universität Dresden, Tatzberg 47/49, 01307, Dresden, Germany.ORCID 0000-0003-4017-6505
F Ulrich HartlDepartment of Cellular Biochemistry, Max-Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.ORCID 0000-0002-7941-135X
Steven F LeeYusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK.ORCID 0000-0003-4492-5139
Tuomas P J KnowlesCentre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, UK. tpjk2@cam.ac.uk.ORCID 0000-0002-7879-0140

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The physical characterization of proteins in terms of their sizes, interactions, and assembly states is key to understanding their biological function and dysfunction. However, this has remained a difficult task because proteins are often highly polydisperse and present as multicomponent mixtures. Here, we address this challenge by introducing single-molecule microfluidic diffusional sizing (smMDS). This approach measures the hydrodynamic radius of single proteins and protein assemblies in microchannels using single-molecule fluorescence detection. smMDS allows for ultrasensitive sizing of proteins down to femtomolar concentrations and enables affinity profiling of protein interactions at the single-molecule level. We show that smMDS is effective in resolving the assembly states of protein oligomers and in characterizing the size of protein species within complex mixtures, including fibrillar protein aggregates and nanoscale condensate clusters. Overall, smMDS is a highly sensitive method for the analysis of proteins in solution, with wide-ranging applications in drug discovery, diagnostics, and nanobiotechnology.

Indexed as

ProteinsSingle Molecule ImagingDiffusionHydrodynamicsMicrofluidic Analytical TechniquesMicrofluidicsSolutionsProteinsSolutions

Identifiers

PMID39231922
PMCPMC11375031

What OpenQuestion holds

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Registered trials

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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.