Evidence map›Paper›PMID 28627758›Full record

ArticleProteomics. Clinical applications2017

Spectral library-based glycopeptide analysis-detection of circulating galectin-3 binding protein in pancreatic cancer.

Eslam N Nigjeh, Ru Chen, Yasuko Allen-Tamura, Randall E Brand, Teresa A Brentnall, Sheng Pan

Open access · greenAbstract read
In one paragraph

Article in Proteomics. Clinical applications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 30% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 25 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. The Role of Data-Independent Acquisition for Glycoproteomics.Molecular & cellular proteomics : MCP · 2021
    Review
  14. Review
  15. Surfaceome profiling enables isolation of cancer-specific exosomal cargo in liquid biopsies from pancreatic cancer patients.Annals of oncology : official journal of the European Society for Medical Oncology · 2018
    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

6 authors at 2 institutions in 1 country.

Eslam N NigjehDepartment of Medicine, University of Washington, Seattle, WA, USA.
Ru ChenDepartment of Medicine, University of Washington, Seattle, WA, USA.
Yasuko Allen-TamuraDepartment of Medicine, University of Washington, Seattle, WA, USA.
Randall E BrandDepartment of Medicine, University of Pittsburgh, Pittsburgh, PA, USA.
Teresa A BrentnallDepartment of Medicine, University of Washington, Seattle, WA, USA.
Sheng PanDepartment of Medicine, University of Washington, Seattle, WA, USA.ORCID 0000-0003-3500-9745
University of Washington · USUniversity of Pittsburgh · US

Funding

Early detection of pancreatic cancer in diabeticsR01CA180949 · NCI · UNIVERSITY OF WASHINGTON · PI CHEN, RU, PAN, SHENG · 2014 to 2018
$2.9M
Quantitative glycoproteomics for pancreatic cancer studiesK25CA137222 · NCI · UNIVERSITY OF WASHINGTON · PI PAN, SHENG · 2010 to 2014
$612k
Aberrant Glycosylation Signature in Pancreatic CancerR21CA149772 · NCI · UNIVERSITY OF WASHINGTON · PI BRENTNALL, TERESA A, PAN, SHENG · 2011 to 2012
$396k
NCI NIH HHS K25 CA137222NCI NIH HHS R01 CA180949NCI NIH HHS R21 CA149772
6 · The paper itself

Abstract

purposePancreatic ductal adenocarcinoma (PDAC) is a lethal disease characterized by its late diagnosis, poor prognosis and rapid development of drug resistance. Using the data-independent acquisition (DIA) technique, the authors applied a spectral library-based proteomic approach to analyze N-glycosylated peptides in human plasma, in the context of pancreatic cancer study. EXPERIMENTAL

designThe authors extended the application of DIA to the quantification of N-glycosylated peptides enriched from plasma specimens from a clinically well-defined cohort that consists of patients with early stage PDAC, chronic pancreatitis and healthy subjects.

resultsThe analytical platform was evaluated in light of its robustness for quantitative analysis of large-scale clinical specimens. The authors analysis indicated that the level of N-glycosylated peptides derived from galectin-3 binding proteins (LGALS3BP) were frequently elevated in plasma from PDAC patients, concurrent with the altered N-glycosylation of LGALS3BP observed in the tumor tissue. CONCLUSION AND CLINICAL RELEVANCE: The glycosylation form of LGALS3BP influences its function in the galectin network, which profoundly involves in cancer progression, immune response and drug resistance. As one of the major binding ligands of galectin network, discovery of site specific N-glycosylation changes of LGALS3BP in association of PDAC may provide useful clues to facilitate cancer detection or phenotype stratification.

Indexed as

Peptide LibraryProteomicsAdenocarcinomaAntigens, NeoplasmBiomarkers, TumorCarrier ProteinsExtracellular Matrix ProteinsGlycoproteinsGlycosylationHumansPancreatic NeoplasmsAntigens, NeoplasmBiomarkers, TumorCarrier ProteinsExtracellular Matrix ProteinsGlycoproteinsLGALS3BP protein, humanPeptide LibraryGalectin-3 binding proteins (LGALS3BP)GlycoproteomicsMass spectrometrypancreatic cancerPlasmaProteomics

Identifiers

PMID28627758
PMCPMC5880677
OpenAlexW2632058739

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.