Evidence map›Paper›PMID 22881839›Full record

ArticleAnalytical chemistry2012

Solution additives that desalt protein ions in native mass spectrometry.

Tawnya G Flick, Catherine A Cassou, Terrence M Chang, Evan R Williams

Abstract read
In one paragraph

Article in Analytical chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

31 citing papers in PubMed, 72 citations in OpenAlex.

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  14. Addition of Serine Enhances Protein Analysis by DESI-MS.Journal of the American Society for Mass Spectrometry · 2019
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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

4 authors at 1 institution in 1 country.

Tawnya G FlickDepartment of Chemistry, University of California, Berkeley, California 94720-1460, United States.
Catherine A Cassou
Terrence M Chang
Evan R Williams
University of California, Berkeley · US

Funding

Development of Single Particle Analyzer of Mass and Mobility (SPAMM)R01GM096097 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM096097NIGMS NIH HHS R01GM096097
6 · The paper itself

Abstract

The presence of many salts, such as sodium chloride, can adversely affect the performance of native electrospray ionization mass spectrometry for the analysis of proteins and protein complexes by reducing the overall molecular ion abundances and distributing signal for any given charge state into many cationized forms with various numbers of adducts attached. Several solution additives, such as ammonium bromide, ammonium iodide, and NaSbF(6), can significantly lower the extent of sodium ion adduction to the molecular ions of proteins and protein complexes. For ubiquitin, addition of 25 mM ammonium bromide or ammonium iodide into aqueous solutions also containing 1.0 mM NaCl results in a factor of 72 and 56 increase, respectively, in the relative abundances of the fully protonated molecular ions compared to when these additives are not present. The effectiveness of this method for reducing sodium ion adduction is related to the low proton affinity (PA) values of the anions. Anions with very low PA also have a propensity to adduct as an acid molecule, but these adducts can be readily dissociated from the molecular ions either by activation in the source or subsequently by collisional activation in the mass spectrometer. This method of reducing sodium ion adduction to proteins is simple and requires no experimental modifications, making it an attractive alternative to other methods for desalting proteins prior to mass spectrometry analysis.

Indexed as

Spectrometry, Mass, Electrospray IonizationBromidesIonsProteinsQuaternary Ammonium CompoundsSodium ChlorideSolutionsUbiquitinammonium bromideBromidesIonsProteinsQuaternary Ammonium CompoundsSodium ChlorideSolutionsUbiquitin

Identifiers

PMID22881839
PMCPMC3433631
OpenAlexW2089432560

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.