Evidence map›Paper›PMID 29131144›Full record

ArticleNature chemical biology2018

Top-down characterization of endogenous protein complexes with native proteomics.

Owen S Skinner, Nicole A Haverland, Luca Fornelli, Rafael D Melani, Luis H F Do Vale, Henrique S Seckler, Peter F Doubleday, Luis F Schachner, Kristina Srzentić, Neil L Kelleher and 1 more

Abstract read
In one paragraph

Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
8.9field-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

97 citing papers in PubMed, 164 citations in OpenAlex.

  1. Article
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  8. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Capillary Electrophoresis-Mass Spectrometry for Top-Down Proteomics.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  19. Article
  20. Native Proteomics by Capillary Zone Electrophoresis-Mass Spectrometry.Angewandte Chemie (International ed. in English) · 2024
    Article

37 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

11 authors at 1 institution in 2 countries.

Owen S SkinnerDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
Nicole A HaverlandDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
Luca FornelliDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
Rafael D MelaniDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.ORCID http://orcid.org/0000-0002-0349-235X
Luis H F Do ValeDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
Henrique S SecklerDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
Peter F DoubledayDepartment of Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.
Luis F SchachnerDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
Kristina SrzentićDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
Neil L KelleherDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.ORCID http://orcid.org/0000-0002-8815-3372
Philip D ComptonDepartment of Chemistry, Northwestern University, Evanston, Illinois, USA.
Northwestern University · US

Funding

TR&D 7: Cell Specific ProteomicsP41GM108569 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2015 to 2024
$13.6M
Chemistry of Life Processes Predoctoral Training ProgramT32GM105538 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2013 to 2022
$2.7M
NIGMS NIH HHS P41 GM108569NIGMS NIH HHS T32 GM105538
6 · The paper itself

Abstract

Protein complexes exhibit great diversity in protein membership, post-translational modifications and noncovalent cofactors, enabling them to function as the actuators of many important biological processes. The exposition of these molecular features using current methods lacks either throughput or molecular specificity, ultimately limiting the use of protein complexes as direct analytical targets in a wide range of applications. Here, we apply native proteomics, enabled by a multistage tandem MS approach, to characterize 125 intact endogenous complexes and 217 distinct proteoforms derived from mouse heart and human cancer cell lines in discovery mode. The native conditions preserved soluble protein-protein interactions, high-stoichiometry noncovalent cofactors, covalent modifications to cysteines, and, remarkably, superoxide ligands bound to the metal cofactor of superoxide dismutase 2. These data enable precise compositional analysis of protein complexes as they exist in the cell and demonstrate a new approach that uses MS as a bridge to structural biology.

Indexed as

Protein MultimerizationAnimalsCell Line, TumorHumansMiceMultiprotein ComplexesProtein ConformationProtein Processing, Post-TranslationalProtein SubunitsProteomicsTandem Mass SpectrometryMultiprotein ComplexesProtein Subunits

Identifiers

PMID29131144
PMCPMC5726920
OpenAlexW2768727863

What OpenQuestion holds

Textmetadata
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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.