Evidence map›Paper›PMID 30688442›Full record

ArticleAnalytical chemistry2019

Surface-Induced Dissociation of Noncovalent Protein Complexes in an Extended Mass Range Orbitrap Mass Spectrometer.

Zachary L VanAernum, Joshua D Gilbert, Mikhail E Belov, Alexander A Makarov, Stevan R Horning, Vicki H Wysocki

Abstract read
In one paragraph

Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing 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

62 citing papers in PubMed.

  1. Article
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  6. Other Techniques.Advances in biochemical engineering/biotechnology · 2026
    Review
  7. Article
  8. Design of a yeast SUMO tag to eliminate internal translation initiation.Protein science : a publication of the Protein Society · 2025
    Article
  9. Article
  10. Article
  11. Review
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  20. Article

2 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

6 authors.

Zachary L VanAernumORCID 0000-0002-0956-3956
Joshua D Gilbert
Mikhail E BelovThermo Fisher Scientific , 28199 Bremen , Germany.
Alexander A MakarovThermo Fisher Scientific , 28199 Bremen , Germany.
Stevan R HorningThermo Fisher Scientific , 28199 Bremen , Germany.
Vicki H Wysocki

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2018 to 2022
$7.6M
NIGMS NIH HHS P41 GM128577
6 · The paper itself

Abstract

Native mass spectrometry continues to develop as a significant complement to traditional structural biology techniques. Within native mass spectrometry (MS), surface-induced dissociation (SID) has been shown to be a powerful activation method for the study of noncovalent complexes of biological significance. High-resolution mass spectrometers have become increasingly adapted to the analysis of high-mass ions and have demonstrated their importance in understanding how small mass changes can affect the overall structure of large biomolecular complexes. Herein we demonstrate the first adaptation of surface-induced dissociation in a modified high-mass-range, high-resolution Orbitrap mass spectrometer. The SID device was designed to be installed in the Q Exactive series of Orbitrap mass spectrometers with minimal disruption of standard functions. The performance of the SID-Orbitrap instrument has been demonstrated with several protein complex and ligand-bound protein complex systems ranging from 53 to 336 kDa. We also address the effect of ion source temperature on native protein-ligand complex ions as assessed by SID. Results are consistent with previous findings on quadrupole time-of-flight instruments and suggest that SID coupled to high-resolution MS is well-suited to provide information on the interface interactions within protein complexes and ligand-bound protein complexes.

Indexed as

IonsLigandsMass SpectrometryMultiprotein ComplexesProtein BindingSurface PropertiesTemperatureIonsLigandsMultiprotein Complexes

Identifiers

PMID30688442
PMCPMC6516482

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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.