Evidence map›Paper›PMID 25242457›Full record

ArticleStructure (London, England : 1993)2014

Mass spec studio for integrative structural biology.

Martial Rey, Vladimir Sarpe, Kyle M Burns, Joshua Buse, Charles A H Baker, Marc van Dijk, Linda Wordeman, Alexandre M J J Bonvin, David C Schriemer

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. Article
  2. Article
  3. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. The structural influence of the oncogenic driver mutation N642H in the STAT5B SH2 domain.Protein science : a publication of the Protein Society · 2025
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. All-in-One Pseudo-MSJournal of the American Society for Mass Spectrometry · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Chaperone requirements for de novo folding ofMolecular biology of the cell · 2022
    Article
  19. Article
  20. Article
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

9 authors.

Martial ReyDepartment of Biochemistry and Molecular Biology and Southern Alberta Cancer Research Institute, University of Calgary, Calgary, AB T2N 4N1, Canada.
Vladimir SarpeDepartment of Biochemistry and Molecular Biology and Southern Alberta Cancer Research Institute, University of Calgary, Calgary, AB T2N 4N1, Canada.
Kyle M BurnsDepartment of Biochemistry and Molecular Biology and Southern Alberta Cancer Research Institute, University of Calgary, Calgary, AB T2N 4N1, Canada.
Joshua BuseDepartment of Biochemistry and Molecular Biology and Southern Alberta Cancer Research Institute, University of Calgary, Calgary, AB T2N 4N1, Canada.
Charles A H BakerCultivated Code, Inc., Calgary, AB T2L 2H3, Canada.
Marc van DijkBijvoet Center for Biomolecular Research, Faculty of Science-Chemistry, Utrecht University, Padualaan 8, Utrecht CH 3584, the Netherlands.
Linda WordemanDepartment of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195-7290, USA.
Alexandre M J J BonvinBijvoet Center for Biomolecular Research, Faculty of Science-Chemistry, Utrecht University, Padualaan 8, Utrecht CH 3584, the Netherlands.
David C SchriemerDepartment of Biochemistry and Molecular Biology and Southern Alberta Cancer Research Institute, University of Calgary, Calgary, AB T2N 4N1, Canada. Electronic address: dschriem@ucalgary.ca.

Funding

Microtubule Dynamics and Chromosome SegregationR01GM069429 · NIGMS · UNIVERSITY OF WASHINGTON · PI WORDEMAN, LINDA · 2004 to 2020
$5.6M
NIGMS NIH HHS R01 GM069429
6 · The paper itself

Abstract

The integration of biophysical data from multiple sources is critical for developing accurate structural models of large multiprotein systems and their regulators. Mass spectrometry (MS) can be used to measure the insertion location for a wide range of topographically sensitive chemical probes, and such insertion data provide a rich, but disparate set of modeling restraints. We have developed a software platform that integrates the analysis of label-based MS and tandem MS (MS(2)) data with protein modeling activities (Mass Spec Studio). Analysis packages can mine any labeling data from any mass spectrometer in a proteomics-grade manner, and link labeling methods with data-directed protein interaction modeling using HADDOCK. Support is provided for hydrogen/deuterium exchange (HX) and covalent labeling chemistries, including novel acquisition strategies such as targeted HX-MS(2) and data-independent HX-MS(2). The latter permits the modeling of highly complex systems, which we demonstrate by the analysis of microtubule interactions.

Indexed as

SoftwareBinding SitesDeuteriumHydrogenMacrolidesMass SpectrometryModels, MolecularMolecular Docking SimulationProtein ConformationProteomicsTandem Mass SpectrometryTubulinDeuteriumHydrogenlaulimalideMacrolidesTubulin

Identifiers

PMID25242457
PMCPMC4391204

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.