Evidence map›Paper›PMID 23210856›Full record

ArticleAnalytical chemistry2013

Simple approach to assign disulfide connectivity using extracted ion chromatograms of electron transfer dissociation spectra.

Daniel F Clark, Eden P Go, Heather Desaire

Abstract read
In one paragraph

Article in Analytical chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Mass Spectrometry-Based Disulfide Mapping of Lysyl Oxidase-like 2.International journal of molecular sciences · 2022
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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

3 authors.

Daniel F ClarkDepartment of Chemistry, University of Kansas, Lawrence, Kansas 66045, USA.
Eden P Go
Heather Desaire

Funding

Development of a rapid glycosylation profiling system using mass spectrometry datR01GM103547 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI DESAIRE, HEATHER R · 2012 to 2017
$1.8M
Characterization of PTMs on Env to support HIV vaccine developmentR01AI094797 · NIAID · UNIVERSITY OF KANSAS LAWRENCE · PI DESAIRE, HEATHER R · 2012 to 2015
$1.4M
Development of a rapid glycosylation profiling system using mass spec dataR01RR026061 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI DESAIRE, HEATHER R · 2009 to 2011
$935k
NCRR NIH HHS R01 RR026061NIAID NIH HHS R01 AI094797NIAID NIH HHS R01AI094797NIGMS NIH HHS R01 GM103547NIGMS NIH HHS R01GM103547
6 · The paper itself

Abstract

Increasing interest in production of protein-based pharmaceuticals (biotherapeutics) is accompanied by an increased need for verification of protein folding and correct disulfide bonding. Recombinant protein expression may produce aberrant disulfide bonds and could result in safety concerns or decreased efficacy. Thus, the thorough analysis of disulfide bonding is a necessity for protein therapeutics. The use of electron transfer dissociation (ETD) facilitates this analysis because disulfide bonds are preferentially cleaved when subjected to ETD. Here, we make use of this well-characterized reaction to assign disulfide bonding networks by coupling the use of extracted ion chromatograms (XICs) of cysteine-containing peptides with ETD analysis to produce an efficient assignment approach for disulfide bonding. This method can be used to assign a disulfide pattern in a de novo fashion, to detect disulfide shuffling, and to provide information on heterogeneity, when more than one disulfide bonding pattern is present. The method was applied for assigning the disulfide-bonding network of a recombinant monomer of the HIV envelope protein gp120. It was found that one region of the protein, the V1/V2 loops, had significant heterogeneity in the disulfide bonds.

Indexed as

CysteineDisulfidesElectron TransportHIV Envelope Protein gp120IonsPeptidesRecombinant ProteinsTandem Mass SpectrometryCysteineDisulfidesHIV Envelope Protein gp120IonsPeptidesRecombinant Proteins

Identifiers

PMID23210856
PMCPMC3607449

What OpenQuestion holds

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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.