Evidence map›Paper›PMID 32083467›Full record

ArticleAnalytical chemistry2020

Structural Analysis of the Glycoprotein Complex Avidin by Tandem-Trapped Ion Mobility Spectrometry-Mass Spectrometry (Tandem-TIMS/MS).

Fanny C Liu, Tyler C Cropley, Mark E Ridgeway, Melvin A Park, Christian Bleiholder

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
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  6. Review
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  10. A Conformation-Specific Approach to Native Top-down Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  11. Evaluation of a Commercial TIMS-Q-TOF Platform for Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  12. Article
  13. Top-down proteomics.Nature reviews. Methods primers · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Dissecting the structural heterogeneity of proteins by native mass spectrometry.Protein science : a publication of the Protein Society · 2023
    Review
  18. Article
  19. Article
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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

5 authors at 2 institutions in 1 country.

Fanny C LiuDepartment of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida 32306-4390, United States.ORCID 0000-0003-1403-7114
Tyler C CropleyDepartment of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida 32306-4390, United States.ORCID 0000-0003-2804-2555
Mark E RidgewayBruker Daltonics Inc., 40 Manning Road, Billerica, Massachusetts 01821, United States.
Melvin A ParkBruker Daltonics Inc., 40 Manning Road, Billerica, Massachusetts 01821, United States.
Christian BleiholderDepartment of Chemistry and Biochemistry, Florida State University, Tallahassee, Florida 32306-4390, United States.ORCID 0000-0002-4211-1388
Florida State University · USBruker (United States) · US

Funding

Elucidating the structural heterogeneity of differentially modified protein systems by tandem-ion mobility spectrometry / mass spectrometry methods.R01GM135682 · NIGMS · FLORIDA STATE UNIVERSITY · PI BLEIHOLDER, CHRISTIAN · 2019 to 2022
$1.3M
NIGMS NIH HHS R01 GM135682
6 · The paper itself

Abstract

Glycoproteins play a central role in many biological processes including disease mechanisms. Nevertheless, because glycoproteins are heterogeneous entities, it remains unclear how glycosylation modulates the protein structure and function. Here, we assess the ability of tandem-trapped ion mobility spectrometry-mass spectrometry (tandem-TIMS/MS) to characterize the structure and sequence of the homotetrameric glycoprotein avidin. We show that (1) tandem-TIMS/MS retains native-like avidin tetramers with deeply buried solvent particles; (2) applying high activation voltages in the interface of tandem-TIMS results in collision-induced dissociation (CID) of avidin tetramers into compact monomers, dimers, and trimers with cross sections consistent with X-ray structures and reports from surface-induced dissociation (SID); (3) avidin oligomers are best described as heterogeneous ensembles with (essentially) random combinations of monomer glycoforms; (4) native top-down sequence analysis of the avidin tetramer is possible by CID in tandem-TIMS. Overall, our results demonstrate that tandem-TIMS/MS has the potential to correlate individual proteoforms to variations in protein structure.

Indexed as

AvidinIon Mobility SpectrometryProtein ConformationTandem Mass SpectrometryAvidin

Identifiers

PMID32083467
PMCPMC7339587
OpenAlexW3008534761

What OpenQuestion holds

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Registered trials

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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.