Evidence map›Paper›PMID 26193081›Full record

ArticleScientific reports2015

Formation and reshuffling of disulfide bonds in bovine serum albumin demonstrated using tandem mass spectrometry with collision-induced and electron-transfer dissociation.

Ine Rombouts, Bert Lagrain, Katharina A Scherf, Marlies A Lambrecht, Peter Koehler, Jan A Delcour

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
5.1field-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

25 citing papers in PubMed, 96 citations in OpenAlex.

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  19. From Protein Features to Sensing Surfaces.Sensors (Basel, Switzerland) · 2018
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Ine RomboutsLaboratory of Food Chemistry and Biochemistry, Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 20, box 2463, B-3001 Leuven, Belgium.
Bert LagrainLaboratory of Food Chemistry and Biochemistry, Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 20, box 2463, B-3001 Leuven, Belgium.
Katharina A ScherfDeutsche Forschungsanstalt für Lebensmittelchemie, Leibniz Institut, Lise-Meitner-Straβe 34, D-85354 Freising, Germany.
Marlies A LambrechtLaboratory of Food Chemistry and Biochemistry, Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 20, box 2463, B-3001 Leuven, Belgium.
Peter KoehlerDeutsche Forschungsanstalt für Lebensmittelchemie, Leibniz Institut, Lise-Meitner-Straβe 34, D-85354 Freising, Germany.
Jan A DelcourLaboratory of Food Chemistry and Biochemistry, Leuven Food Science and Nutrition Research Centre (LFoRCe), KU Leuven, Kasteelpark Arenberg 20, box 2463, B-3001 Leuven, Belgium.
KU Leuven · BELeibniz-Institute for Food Systems Biology at the Technical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thermolysin hydrolyzates of freshly isolated, extensively stored (6 years, 6 °C, dry) and heated (60 min, 90 °C, in excess water) bovine serum albumin (BSA) samples were analyzed with liquid chromatography (LC) electrospray ionization (ESI) tandem mass spectrometry (MS/MS) using alternating electron-transfer dissociation (ETD) and collision-induced dissociation (CID). The positions of disulfide bonds and free thiol groups in the different samples were compared to those deduced from the crystal structure of native BSA. Results revealed non-enzymatic posttranslational modifications of cysteine during isolation, extensive dry storage, and heating. Heat-induced extractability loss of BSA was linked to the impact of protein unfolding on the involvement of specific cysteine residues in intermolecular and intramolecular thiol-disulfide interchange and thiol oxidation reactions. The here developed approach holds promise for exploring disulfide bond formation and reshuffling in various proteins under conditions relevant for chemical, biochemical, pharmaceutical and food processing.

Indexed as

ElectronsAmino Acid SequenceAnimalsCattleChromatography, GelChromatography, High Pressure LiquidCysteineDisulfidesHot TemperatureMolecular Sequence DataPeptidesProtein AggregatesSerum Albumin, BovineTandem Mass SpectrometryCysteineDisulfidesPeptidesProtein AggregatesSerum Albumin, Bovine

Identifiers

PMID26193081
PMCPMC4507448
OpenAlexW1009584036

What OpenQuestion holds

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LicenceCC BY
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.