Evidence map›Paper›PMID 28444931›Full record

ArticleElectrophoresis2017

Study of structure-dependent chromatographic behavior of glycopeptides using reversed phase nanoLC.

Petr Kozlik, Radoslav Goldman, Miloslav Sanda

Open access · greenAbstract read
In one paragraph

Article in Electrophoresis, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

13 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Glycan-specific precipitation of glycopeptides in high organic content sample solvents used in HILIC.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2020
    Article
  10. Article
  11. The Journal of biological chemistry · 2019
    Article
  12. Review
  13. 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 1 institution in 2 countries.

Petr KozlikDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington, DC, USA.
Radoslav GoldmanDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington, DC, USA.
Miloslav SandaDepartment of Oncology, Lombardi Comprehensive Cancer Center, Georgetown University, Washington, DC, USA.ORCID 0000-0002-7735-3635
Georgetown University · US

Funding

Tissue Culture Shared ResourceP30CA051008 · NCI · GEORGETOWN UNIVERSITY · PI Louis M Weiner · 1990 to 2026
$71.5M
Glycans in Hepatocellular CarcinomaR01CA135069 · NCI · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2009 to 2019
$4.1M
Alliance of Glycobiologists for Detection of CancerU01CA168926 · NCI · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2012 to 2016
$2.0M
Basic Cancer Research in Cancer Health DisparitiesU01CA171146 · NCI · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2012 to 2016
$1.5M
SULF2 in HNSCCR21DE025732 · NIDCR · GEORGETOWN UNIVERSITY · PI GOLDMAN, RADOSLAV · 2016 to 2017
$428k
NCI NIH HHS P30 CA051008NCI NIH HHS R01 CA135069NCI NIH HHS U01 CA168926NCI NIH HHS U01 CA171146NIDCR NIH HHS R21 DE025732
6 · The paper itself

Abstract

Analysis of glycosylation is challenging due to micro- and macro-heterogeneity of the protein attachment. A combination of LC with MS/MS is one of the most powerful tools for glycopeptide analysis. In this work, we show the effect of various monosaccharide units on the retention time of glycopeptides. Retention behavior of several glycoforms of six peptides obtained from tryptic digest of haptoglobin, hemopexin, and sex hormone-binding globulin was studied on a reversed phase chromatographic column. We observed reduction of the retention time with increasing number of monosaccharide units of glycans attached to the same peptide backbone. Fucosylation of larger glycans provides less significant retention time shift than for smaller ones. Retention times of glycopeptides were expressed as relative retention times. These relative retention times were used for calculation of upper and lower limits of glycopeptide retention time windows under the reversed phase conditions. We then demonstrated on the case of a glycopeptide of haptoglobin that the predicted retention time window boosts confidence of identification and minimizes false-positive identification. Relative retention time, as a qualitative parameter, is expected to improve LC-MS/MS characterization of glycopeptides.

Indexed as

Chromatography, Reverse-PhaseGlycopeptidesGlycosylationHumansNanotechnologyPeptide FragmentsProteomicsSensitivity and SpecificityTrypsinGlycopeptidesPeptide FragmentsTrypsinGlycoform-dependent retention predictionGlycopeptide chromatographyGlycoproteomicsLC-MS/MSReversed phase chromatography

Identifiers

PMID28444931
PMCPMC5581245
OpenAlexW2607809077

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.