Evidence map›Paper›PMID 27830529›Full record

ArticleJournal of the American Society for Mass Spectrometry2017

Influence of Alkylammonium Acetate Buffers on Protein-Ligand Noncovalent Interactions Using Native Mass Spectrometry.

Xiaoyu Zhuang, Agni F M Gavriilidou, Renato Zenobi

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
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  4. Hydration (HJournal of the American Chemical Society · 2025
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  9. Review
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  11. Collision-Induced Unfolding Is Sensitive to the Polarity of Proteins and Protein Complexes.Journal of the American Society for Mass Spectrometry · 2019
    Article
  12. Article
  13. Review
  14. 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

3 authors at 2 institutions in 2 countries.

Xiaoyu ZhuangDepartment of Chemistry and Applied Biosciences, ETH Zurich, CH-8093, Zurich, Switzerland.
Agni F M GavriilidouDepartment of Chemistry and Applied Biosciences, ETH Zurich, CH-8093, Zurich, Switzerland.
Renato ZenobiDepartment of Chemistry and Applied Biosciences, ETH Zurich, CH-8093, Zurich, Switzerland. zenobi@org.chem.ethz.ch.
ETH Zurich · CHChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We investigate the influence of three volatile alkylammonium acetate buffers on binding affinities for protein-ligand interactions determined by native electrospray ionization-mass spectrometry (ESI-MS). Four different types of proteins were chosen for this study. A charge-reduction effect was observed for all the cases studied, in comparison to the ions formed in ammonium acetate solution. When increasing the collision energy, the complexes of trypsin and the ligand were found to be more stable when sprayed from alkylammonium acetate buffers than from ammonium acetate. The determined dissociation constant (K

Indexed as

AcetatesBuffersCarbonic Anhydrase IIChlorothiazideLactoglobulinsLauric AcidsLigandsMuramidaseProteinsSpectrometry, Mass, Electrospray IonizationSulfonesTrypsin4-(2-aminoethyl)benzenesulfonylfluorideAcetatesammonium acetateBuffersCarbonic Anhydrase IIChlorothiazideLactoglobulinslauric acidLauric AcidsLigandsMuramidaseProteinsSulfonesTrypsinAlkylammonium saltsCharge reductionNative mass spectrometryNoncovalent interactions

Identifiers

PMID27830529
OpenAlexW2554429273

What OpenQuestion holds

Textmetadata
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.