Evidence map›Paper›PMID 30393918›Full record

ArticleAngewandte Chemie (International ed. in English)2018

Rapid Mapping of Protein Interactions Using Tag-Transfer Photocrosslinkers.

Jim E Horne, Martin Walko, Antonio N Calabrese, Mark A Levenstein, David J Brockwell, Nikil Kapur, Andrew J Wilson, Sheena E Radford

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Review
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  14. The Application of Fluorine-Containing Reagents in Structural Proteomics.Angewandte Chemie (International ed. in English) · 2020
    Review
  15. Review
  16. Article
  17. Mapping low-affinity/high-specificity peptide-protein interactions using ligand-footprinting mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. 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.

Jim E HorneSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0001-5260-2634
Martin WalkoSchool of Chemistry, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0002-7160-6136
Antonio N CalabreseSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0003-2437-7761
Mark A LevensteinSchool of Chemistry, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0002-2309-3743
David J BrockwellSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0002-0802-5937
Nikil KapurSchool of Mechanical Engineering, University of Leeds, Leeds, LS2 9JT, UK.
Andrew J WilsonSchool of Chemistry, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0001-9852-6366
Sheena E RadfordSchool of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0002-3079-8039

Funding

W METRO-MINNEAPOLIS COMMUNITY CLINICAL ONCOLOGY PROGRAMU10CA035267 · NCI · PARK NICOLLET INSTITUTE · PI LEACH, JOSEPH · 1985 to 2014
$23.2M
Biotechnology and Biological Sciences Research Council BB/K000659/1Biotechnology and Biological Sciences Research Council BB/M011151/1Biotechnology and Biological Sciences Research Council BB/M01151/1Biotechnology and Biological Sciences Research Council BB/M012573/1Biotechnology and Biological Sciences Research Council BB/N007603/1Biotechnology and Biological Sciences Research Council BB/P000037/1European Research Council 322408Wellcome Trust 208385/Z/17/Z
6 · The paper itself

Abstract

Analysing protein complexes by chemical crosslinking-mass spectrometry (XL-MS) is limited by the side-chain reactivities and sizes of available crosslinkers, their slow reaction rates, and difficulties in crosslink enrichment, especially for rare, transient or dynamic complexes. Here we describe two new XL reagents that incorporate a methanethiosulfonate (MTS) group to label a reactive cysteine introduced into the bait protein, and a residue-unbiased diazirine-based photoactivatable XL group to trap its interacting partner(s). Reductive removal of the bait transfers a thiol-containing fragment of the crosslinking reagent onto the target that can be alkylated and located by MS sequencing and exploited for enrichment, enabling the detection of low abundance crosslinks. Using these reagents and a bespoke UV LED irradiation platform, we show that maximum crosslinking yield is achieved within 10 seconds. The utility of this "tag and transfer" approach is demonstrated using a well-defined peptide/protein regulatory interaction (BID

Indexed as

Protein Interaction MapsCross-Linking ReagentsCysteineMass SpectrometryMesylatesMolecular StructurePhotochemical ProcessesProteinsCross-Linking ReagentsCysteineMesylatesmethanethiosulfonateProteinschemical crosslinkingdiazo compoundsmass spectrometryphotoaffinity labelingprotein-protein interactions

Identifiers

PMID30393918
PMCPMC6348423

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.