Evidence map›Paper›PMID 28516012›Full record

ReviewIntrinsically disordered proteins

Extracting structural information from charge-state distributions of intrinsically disordered proteins by non-denaturing electrospray-ionization mass spectrometry.

Lorenzo Testa, Stefania Brocca, Carlo Santambrogio, Annalisa D'Urzo, Johnny Habchi, Sonia Longhi, Vladimir N Uversky, Rita Grandori

Abstract readReview
In one paragraph

Review in Intrinsically disordered proteins. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
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  3. Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  14. Review
  15. Nanobody-aided crystallization of the transcription regulator PaaR2 from Escherichia coli O157:H7.Acta crystallographica. Section F, Structural biology communications · 2021
    Article
  16. Article
  17. Article
  18. Review
  19. Article
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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

8 authors.

Lorenzo TestaDepartment of Biotechnology and Biosciences; University of Milano-Bicocca; Milan, Italy.
Stefania BroccaDepartment of Biotechnology and Biosciences; University of Milano-Bicocca; Milan, Italy.
Carlo SantambrogioDepartment of Biotechnology and Biosciences; University of Milano-Bicocca; Milan, Italy.
Annalisa D'UrzoDepartment of Biotechnology and Biosciences; University of Milano-Bicocca; Milan, Italy.
Johnny HabchiAix-Marseille Université; CNRS, Architecture et Fonction des Macromolécules Biologiques (AFMB); Marseille, France.
Sonia LonghiAix-Marseille Université; CNRS, Architecture et Fonction des Macromolécules Biologiques (AFMB); Marseille, France.
Vladimir N UverskyDepartment of Molecular Medicine; College of Medicine; University of South Florida; Tampa, FL USA.
Rita GrandoriDepartment of Biotechnology and Biosciences; University of Milano-Bicocca; Milan, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) exert key biological functions but tend to escape identification and characterization due to their high structural dynamics and heterogeneity. The possibility to dissect conformational ensembles by electrospray-ionization mass spectrometry (ESI-MS) offers an attracting possibility to develop a signature for this class of proteins based on their peculiar ionization behavior. This review summarizes available data on charge-state distributions (CSDs) obtained for IDPs by non-denaturing ESI-MS, with reference to globular or chemically denatured proteins. The results illustrate the contributions that direct ESI-MS analysis can give to the identification of new putative IDPs and to their conformational investigation.

Indexed as

charge-state distributionscharge-to-mass relationIDP compactionintrinsically folded structural unitsnative mass spectrometryprotein foldingproteomicsSic1solvent-accessible surface areaα-synuclein

Identifiers

PMID28516012
PMCPMC5424789

What OpenQuestion holds

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Registered trials

None linked

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.