Evidence map›Paper›PMID 26391079›Full record

ArticleNature chemistry2015

Latent analysis of unmodified biomolecules and their complexes in solution with attomole detection sensitivity.

Emma V Yates, Thomas Müller, Luke Rajah, Erwin J De Genst, Paolo Arosio, Sara Linse, Michele Vendruscolo, Christopher M Dobson, Tuomas P J Knowles

Abstract read
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In one paragraph

Article in Nature chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

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  16. The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

9 authors.

Emma V YatesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Thomas MüllerDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Luke RajahDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Erwin J De GenstDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Paolo ArosioDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Sara LinseDepartment of Biochemistry and Structural Biology, Lund University, Lund SE221 00, Sweden.
Michele VendruscoloDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Christopher M DobsonDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Tuomas P J KnowlesDepartment of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G1002272Wellcome Trust
6 · The paper itself

Abstract

The study of biomolecular interactions is central to an understanding of function, malfunction and therapeutic modulation of biological systems, yet often involves a compromise between sensitivity and accuracy. Many conventional analytical steps and the procedures required to facilitate sensitive detection, such as the incorporation of chemical labels, are prone to perturb the complexes under observation. Here we present a 'latent' analysis approach that uses chemical and microfluidic tools to reveal, through highly sensitive detection of a labelled system, the behaviour of the physiologically relevant unlabelled system. We implement this strategy in a native microfluidic diffusional sizing platform, allowing us to achieve detection sensitivity at the attomole level, determine the hydrodynamic radii of biomolecules that vary by over three orders of magnitude in molecular weight, and study heterogeneous mixtures. We illustrate these key advantages by characterizing a complex of an antibody domain in the solution phase and under physiologically relevant conditions.

Indexed as

Limit of DetectionMicrofluidicsNucleic AcidsProteinsNucleic AcidsProteins

Identifiers

PMID26391079

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.