Evidence map›Paper›PMID 32561732›Full record

ArticleNature communications2020

Mass spectrometry reveals the chemistry of formaldehyde cross-linking in structured proteins.

Tamar Tayri-Wilk, Moriya Slavin, Joanna Zamel, Ayelet Blass, Shon Cohen, Alex Motzik, Xue Sun, Deborah E Shalev, Oren Ram, Nir Kalisman

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
6.9field-weighted citation impact, top 2% of its field
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

68 citing papers in PubMed, 124 citations in OpenAlex.

  1. Review
  2. Article
  3. FFPE-CUTAC: A Single Assay, Multiple Layers.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
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  6. SpyCEP dismantles neutrophil immunity via disorder-driven chemokine remodeling and GAG targeting.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  13. Review
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  17. Review
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8 more citing papers are in PubMed but not listed here.

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

10 authors at 1 institution in 1 country.

Tamar Tayri-Wilk *Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
Moriya Slavin *Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
Joanna Zamel *Institute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
Ayelet BlassInstitute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
Shon CohenInstitute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
Alex MotzikInstitute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
Xue SunInstitute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.ORCID http://orcid.org/0000-0002-7971-4051
Deborah E ShalevWolfson Centre for Applied Structural Biology, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
Oren RamInstitute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel.
Nir KalismanInstitute of Life Sciences, The Hebrew University of Jerusalem, Jerusalem, 9190401, Israel. nirka@mail.huji.ac.il.ORCID http://orcid.org/0000-0003-1615-7136
Hebrew University of Jerusalem · IL

Funding

Israel Science Foundation (ISF) 1768/15
6 · The paper itself

Abstract

Whole-cell cross-linking coupled to mass spectrometry is one of the few tools that can probe protein-protein interactions in intact cells. A very attractive reagent for this purpose is formaldehyde, a small molecule which is known to rapidly penetrate into all cellular compartments and to preserve the protein structure. In light of these benefits, it is surprising that identification of formaldehyde cross-links by mass spectrometry has so far been unsuccessful. Here we report mass spectrometry data that reveal formaldehyde cross-links to be the dimerization product of two formaldehyde-induced amino acid modifications. By integrating the revised mechanism into a customized search algorithm, we identify hundreds of cross-links from in situ formaldehyde fixation of human cells. Interestingly, many of the cross-links could not be mapped onto known atomic structures, and thus provide new structural insights. These findings enhance the use of formaldehyde cross-linking and mass spectrometry for structural studies.

Indexed as

Amino AcidsCell Line, TumorCross-Linking ReagentsFormaldehydeHumansMass SpectrometryMolecular Docking SimulationProtein Interaction MappingProteinsAmino AcidsCross-Linking ReagentsFormaldehydeProteins

Identifiers

PMID32561732
PMCPMC7305180
OpenAlexW3036754088

What OpenQuestion holds

Textmetadata
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.