Evidence map›Paper›PMID 26535604›Full record

ArticleJournal of proteome research2015

Comprehensive Cross-Linking Mass Spectrometry Reveals Parallel Orientation and Flexible Conformations of Plant HOP2-MND1.

Evelyn Rampler, Thomas Stranzl, Zsuzsanna Orban-Nemeth, David Maria Hollenstein, Otto Hudecz, Peter Schlögelhofer, Karl Mechtler

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2015. 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 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  3. Review
  4. Review
  5. Article
  6. Crosslinking mass spectrometry: A link between structural biology and systems biology.Protein science : a publication of the Protein Society · 2021
    Review
  7. Review
  8. Article
  9. Quantitative Cross-Linking of Proteins and Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Tools for 3D Interactome Visualization.Journal of proteome research · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Evelyn RamplerInstitute of Molecular Pathology , Dr.-Bohr-Gasse 7, 1030 Vienna, Austria.
Thomas StranzlInstitute of Molecular Pathology , Dr.-Bohr-Gasse 7, 1030 Vienna, Austria.
Zsuzsanna Orban-NemethInstitute of Molecular Pathology , Dr.-Bohr-Gasse 7, 1030 Vienna, Austria.
David Maria Hollenstein
Otto HudeczInstitute of Molecular Biotechnology, Austrian Academy of Sciences , Dr.-Bohr-Gasse 3, 1030 Vienna, Austria.
Peter Schlögelhofer
Karl MechtlerInstitute of Molecular Pathology , Dr.-Bohr-Gasse 7, 1030 Vienna, Austria.
Research Institute of Molecular Pathology · ATInstitute of Molecular Biotechnology · AT

Funding

Austrian Science Fund FWF F 3408Austrian Science Fund FWF F 3411Austrian Science Fund FWF I 1468Austrian Science Fund FWF P 24685Austrian Science Fund FWF TRP 308
6 · The paper itself

Abstract

The HOP2-MND1 heterodimer is essential for meiotic homologous recombination in plants and other eukaryotes and promotes the repair of DNA double-strand breaks. We investigated the conformational flexibility of HOP2-MND1, important for understanding the mechanistic details of the heterodimer, with chemical cross-linking in combination with mass spectrometry (XL-MS). The final XL-MS workflow encompassed the use of complementary cross-linkers, quenching, digestion, size exclusion enrichment, and HCD-based LC-MS/MS detection prior to data evaluation. We applied two different homobifunctional amine-reactive cross-linkers (DSS and BS(2)G) and one zero-length heterobifunctional cross-linker (EDC). Cross-linked peptides of four biological replicates were analyzed prior to 3D structure prediction by protein threading and protein-protein docking for cross-link-guided molecular modeling. Miniaturization of the size-exclusion enrichment step reduced the required starting material, led to a high amount of cross-linked peptides, and allowed the analysis of replicates. The major interaction site of HOP2-MND1 was identified in the central coiled-coil domains, and an open colinear parallel arrangement of HOP2 and MND1 within the complex was predicted. Moreover, flexibility of the C-terminal capping helices of both complex partners was observed, suggesting the coexistence of a closed complex conformation in solution.

Indexed as

Arabidopsis ProteinsCarbodiimidesChromatography, GelCross-Linking ReagentsModels, MolecularMultiprotein ComplexesPhosphotransferasesProtein ConformationProtein MultimerizationSuccinimidesTandem Mass SpectrometryWorkflow1-ethyl-3-(3-(diethylamino)propyl)carbodiimideAHP2 protein, ArabidopsisArabidopsis ProteinsCarbodiimidesCross-Linking Reagentsdisuccinimidyl suberateMND1 protein, ArabidopsisMultiprotein ComplexesPhosphotransferasesSuccinimidesBS2Gcomparative modelingcross-linkingDSSEDCHOP2–MND1SECXL−MS

Identifiers

PMID26535604
PMCPMC6207341
OpenAlexW2263727490

What OpenQuestion holds

Textmetadata
LicenceTDM
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.