Evidence map›Paper›PMID 29679287›Full record

ArticleJournal of the American Society for Mass Spectrometry2019

The First MS-Cleavable, Photo-Thiol-Reactive Cross-Linker for Protein Structural Studies.

Claudio Iacobucci, Christine Piotrowski, Anne Rehkamp, Christian H Ihling, Andrea Sinz

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Preserving Single Cells in Space and Time for Analytical Assays.Trends in analytical chemistry : TRAC · 2020
    Article
  6. Article
  7. Review
  8. Review
  9. Rapid Mapping of Protein Interactions Using Tag-Transfer Photocrosslinkers.Angewandte Chemie (International ed. in English) · 2018
    Article
  10. Article
  11. Article
  12. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Claudio IacobucciDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle (Saale), Germany. iacobucci.claudio@gmail.com.
Christine PiotrowskiDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle (Saale), Germany.
Anne RehkampDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle (Saale), Germany.
Christian H IhlingDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle (Saale), Germany.
Andrea SinzDepartment of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Charles Tanford Protein Center, Martin Luther University Halle-Wittenberg, Kurt-Mothes-Str. 3a, 06120, Halle (Saale), Germany. andrea.sinz@pharmazie.uni-halle.de.ORCID http://orcid.org/0000-0003-1521-4899

Funding

Alexander von Humboldt-Stiftung Postdoctoral fellowshipDeutsche Forschungsgemeinschaft Si 867/15-2
6 · The paper itself

Abstract

Cleavable cross-linkers are gaining increasing importance for chemical cross-linking/mass spectrometry (MS) as they permit a reliable and automated data analysis in structural studies of proteins and protein assemblies. Here, we introduce 1,3-diallylurea (DAU) as the first CID-MS/MS-cleavable, photo-thiol-reactive cross-linker. DAU is a commercially available, inexpensive reagent that efficiently undergoes an anti-Markovnikov hydrothiolation with cysteine residues in the presence of a radical initiator upon UV-A irradiation. Radical cysteine cross-linking proceeds via an orthogonal "click reaction" and yields stable alkyl sulfide products. DAU reacts at physiological pH and cross-linking reactions with peptides, and proteins can be performed at temperatures as low as 4 °C. The central urea bond is efficiently cleaved upon collisional activation during tandem MS experiments generating characteristic product ions. This improves the reliability of automated cross-link identification. Different radical initiators have been screened for the cross-linking reaction of DAU using the thiol-containing compounds cysteine and glutathione. Our concept has also been exemplified for the biologically relevant proteins bMunc13-2 and retinal guanylyl cyclase-activating protein-2. Graphical abstract ᅟ.

Indexed as

Allyl CompoundsCross-Linking ReagentsCysteineGlutathioneGuanylate Cyclase-Activating ProteinsHydrogen-Ion ConcentrationNerve Tissue ProteinsProteinsReproducibility of ResultsSpectrometry, Mass, Electrospray IonizationSulfhydryl CompoundsTandem Mass SpectrometryUreaAllyl CompoundsCross-Linking ReagentsCysteineGlutathioneGuanylate Cyclase-Activating ProteinsNerve Tissue ProteinsProteinsSulfhydryl CompoundsUnc13b protein, ratUrea1,3-diallylureaCross-linkingProtein structureTandem mass spectrometryThiols

Identifiers

What OpenQuestion holds

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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.