Evidence map›Paper›PMID 25970732›Full record

ReviewProtein science : a publication of the Protein Society2015

Chemical cross-linking and native mass spectrometry: A fruitful combination for structural biology.

Andrea Sinz, Christian Arlt, Dror Chorev, Michal Sharon

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
10.9field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 129 citations in OpenAlex.

  1. Article
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  9. A Treatment to Cure Diabetes Using Plant-Based Drug Discovery.Evidence-based complementary and alternative medicine : eCAM · 2022
    Article
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  17. Structural dynamics of the human COP9 signalosome revealed by cross-linking mass spectrometry and integrative modeling.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. Review
  19. Plant-Derived Bioactive Peptides: A Treatment to Cure Diabetes.International journal of peptide research and therapeutics · 2020
    Review
  20. Review
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

4 authors at 2 institutions in 2 countries.

Andrea SinzDepartment of Pharmaceutical Chemistry & Bioanalytics, Institute of Pharmacy, Martin-Luther University Halle-Wittenberg, D-06120, Halle, Germany.
Christian ArltDepartment of Pharmaceutical Chemistry & Bioanalytics, Institute of Pharmacy, Martin-Luther University Halle-Wittenberg, D-06120, Halle, Germany.
Dror ChorevDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot, 76100, Israel.
Michal SharonDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot, 76100, Israel.
Martin Luther University Halle-Wittenberg · DEWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mass spectrometry (MS) is becoming increasingly popular in the field of structural biology for analyzing protein three-dimensional-structures and for mapping protein-protein interactions. In this review, the specific contributions of chemical crosslinking and native MS are outlined to reveal the structural features of proteins and protein assemblies. Both strategies are illustrated based on the examples of the tetrameric tumor suppressor protein p53 and multisubunit vinculin-Arp2/3 hybrid complexes. We describe the distinct advantages and limitations of each technique and highlight synergistic effects when both techniques are combined. Integrating both methods is especially useful for characterizing large protein assemblies and for capturing transient interactions. We also point out the future directions we foresee for a combination of in vivo crosslinking and native MS for structural investigation of intact protein assemblies.

Indexed as

AnimalsCross-Linking ReagentsHumansMass SpectrometryModels, MolecularProtein ConformationProtein Interaction MappingProteinsProteomicsTumor Suppressor Protein p53Cross-Linking ReagentsProteinsTumor Suppressor Protein p53chemical cross-linkingnative mass spectrometryprotein 3D structureprotein-protein interactions

Identifiers

PMID25970732
PMCPMC4534171
OpenAlexW2163756713

What OpenQuestion holds

Textmetadata
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.