Evidence map›Paper›PMID 20858014›Full record

ArticleJournal of proteome research2010

Sialylated Lewis x antigen bearing glycoproteins in human plasma.

Wonryeon Cho, Kwanyoung Jung, Fred E Regnier

Abstract read
In one paragraph

Article in Journal of proteome research, 2010. 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
0.9field-weighted citation impact, top 26% 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, 26 citations in OpenAlex.

  1. Article
  2. Anti-Glycan Autoantibodies Induced byFrontiers in immunology · 2020
    Article
  3. Article
  4. Article
  5. Vitronectin: a promising breast cancer serum biomarker for early diagnosis of breast cancer in patients.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  6. Article
  7. Capturing and identification of differentially expressed fucome by a gel free and label free approach.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2015
    Article
  8. Article
  9. Article
  10. Targeting deeper the human serum fucome by a liquid-phase multicolumn platform in combination with combinatorial peptide ligand libraries.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2014
    Article
  11. Article
  12. The emerging importance of α-L-fucose in human breast cancer: a review.American journal of translational research · 2011
    Article
  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 1 country.

Wonryeon ChoDepartment of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
Kwanyoung Jung
Fred E Regnier
Purdue University West Lafayette · US

Funding

APT: the Analytical Proteomics TeamU24CA126480 · NCI · PURDUE UNIVERSITY · PI REGNIER, FRED E · 2006 to 2010
$6.4M
NCI NIH HHS U24 CA126480NCI NIH HHS U24-CA-126480
6 · The paper itself

Abstract

Recent studies have shown that antibodies targeting Lewis x (Le(x)) antigen are a valuable tool in the isolation and identification of glycoproteins in plasma. A focus of this study was to determine whether sialylated Lewis x (sLe(x)) antigen carrying glycoproteins occur in human plasma and whether an antibody targeting this antigen could be used to isolate and identify glycoproteins bearing this antigen. An additional objective was to determine the degree to which proteins conjugated to Le(x) and sLe(x) antigens are similar in structure. A specific anti-sLe(x) antibody (anti-sLe(x)Ab), CHO-131, immobilized in an immunoaffinity column was used to select a set of specific sLe(x) bearing proteins from human plasma, after which they were identified by either of two analytical strategies. One approach was to further resolve the affinity selected proteins by reversed phase chromatography (RPC), tryptic digest the RPC fractions, and identify peptide fragments by MALDI-MS/MS. The second was to tryptic digest the affinity selected protein fraction, further resolve the tryptic fragments by RPC, and identify peptides from RPC fractions by MALDI-MS/MS. Histidine-rich glycoprotein, plasminogen, apolipoprotein A-I, vitronectin, proteoglycan-4, clusterin, Ig gamma-2 chain C region, Ig mu chain C region, and interalpha-trypsin inhibitor heavy chain H4 were found to change three folds or more in association with breast cancer. Fifty percent of the glycoproteins carrying either sLe(x) antigen from CHO-131 selection, Le(x) antigen from selection with TG-1 antibody, or both were found to be changed three folds or more in concentration in breast cancer plasma relative to controls.

Indexed as

Antibodies, MonoclonalBreast NeoplasmsFemaleGlycoproteinsHumansLewis X AntigenNeoplasm ProteinsProtein ConformationAntibodies, MonoclonalGlycoproteinsLewis X AntigenNeoplasm Proteins

Identifiers

PMID20858014
PMCPMC2976037
OpenAlexW2093521345

What OpenQuestion holds

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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.