Evidence map›Paper›PMID 38752317›Full record

ArticleChemical communications (Cambridge, England)2024

A native mass spectrometry approach to qualitatively elucidate interfacial epitopes of transient protein-protein interactions.

Clinton G L Veale, Abir Chakraborty, Richwell Mhlanga, Fernando Albericio, Beatriz G de la Torre, Adrienne L Edkins, David J Clarke

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chemical communications (Cambridge, England), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Article
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

7 authors.

Clinton G L VealeDepartment of Chemistry, University of Cape Town, Rondebosch, Cape Town 7701, South Africa. clinton.veale@uct.ac.za.ORCID http://orcid.org/0000-0002-4043-7106
Abir ChakrabortyThe Biomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, South Africa.ORCID http://orcid.org/0000-0002-3131-0808
Richwell MhlangaThe Biomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, South Africa.
Fernando AlbericioSchool of Chemistry and Physics, University of KwaZulu-Natal, Westville, South Africa.ORCID http://orcid.org/0000-0002-8946-0462
Beatriz G de la TorreSchool of Laboratory Medicine and Medical Sciences, College of Health Sciences, University of KwaZulu-Natal, South Africa.ORCID http://orcid.org/0000-0001-8521-9172
Adrienne L EdkinsThe Biomedical Biotechnology Research Unit (BioBRU), Department of Biochemistry and Microbiology, Rhodes University, Makhanda, South Africa.
David J ClarkeEaStCHEM School of Chemistry, University of Edinburgh, Joseph Black Building, David Brewster Road, Edinburgh EH93FJ, UK. dave.clarke@ed.ac.uk.ORCID http://orcid.org/0000-0002-3741-2952

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Native mass spectrometric analysis of TPR2A and GrpE with unpurified peptides derived from limited proteolysis of their respective PPI partners (HSP90 C-terminus and DnaK) facilitated efficient, qualitative identification of interfacial epitopes involved in transient PPI formation. Application of this approach can assist in elucidating interfaces of currently uncharacterised transient PPIs.

Indexed as

EpitopesMass SpectrometryHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPeptidesProtein BindingEpitopesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsPeptides

Identifiers

PMID38752317
PMCPMC11139139

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.