Evidence map›Paper›PMID 19240272›Full record

ArticleGlycobiology2009

Structural analysis of N-glycans from gull egg white glycoproteins and egg yolk IgG.

Noriko Suzuki, Tseng-Hsiung Su, Sze-Wei Wu, Kazuo Yamamoto, Kay-Hooi Khoo, Yuan C Lee

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed, 32 citations in OpenAlex.

  1. Identification and comparison ofFood chemistry: X · 2025
    Article
  2. Article
  3. Article
  4. Glycosylation at an evolutionary nexus: the brittle starThe Journal of biological chemistry · 2020
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
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 4 institutions in 3 countries.

Noriko SuzukiDepartment of Biology, The Johns Hopkins University, Baltimore, MD 21218, USA. nrsuzuki@k.u-tokyo.ac.jp
Tseng-Hsiung Su
Sze-Wei Wu
Kazuo Yamamoto
Kay-Hooi Khoo
Yuan C Lee
Institute of Biological Chemistry, Academia Sinica · TWJohns Hopkins University · USNational Taiwan University · TWThe University of Tokyo · JP

Funding

CHEMISTRY AND BIOCHEMISTRY OF GLYCOCONJUGATESR01DK009970 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI LEE, YUAN CHUAN · 1986 to 2005
$2.2M
CHEMISTRY AND BIOCHEMISTRY OF GLYCOCONJUGATESR37DK009970 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI LEE, YUAN CHUAN · 1987 to 1994
–
NIDDK NIH HHS DK09970
6 · The paper itself

Abstract

We previously showed that the expression of (Gal alpha 1-4Gal)-bearing glycoproteins among birds is related to their phylogeny. However, precise structures of (Gal alpha 1-4Gal)-containing N-glycans were only known for pigeon egg white glycoproteins and IgG. To compare structural features of (Gal alpha 1-4Gal)-containing N-glycans from other species, we analyzed N-glycans of gull egg white (GEW)-glycoproteins, ovomucoid, and ovotransferrin, and gull egg yolk IgG by HPLC, mass spectrometry (MS), and MS/MS analyses. GEW-glycoproteins included neutral, monosialyl, and disialyl N-glycans, and some of them contained Gal alpha 1-4Gal sequences. Bi-, tri-, and tetra-antennary oligosaccharides that lacked bisecting GlcNAc were the major core structures, and incomplete alpha-galactosylation and sialylation as well as the presence of diLacNAc on the branches generated microheterogeneity of the N-glycan structures. Moreover, unlike pigeon egg white glycoproteins, the major sialylation in GEW-glycoproteins is alpha2,3-, but not alpha2,6-linked sialic acids (NeuAc). In addition to the complex-type oligosaccharide, hybrid-type oligosaccharides that lack bisecting GlcNAc were also abundant in GEW-glycoproteins. Gull egg yolk IgG also contained Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequences, but unlike pigeon IgG, no Gal alpha 1-4Gal beta 1-4Gal beta 1-4GlcNAc beta 1- sequence was detected. Bi- and tri-antennary complex-type oligosaccharides with bisecting GlcNAc and with core fucosylation as well as high-mannose-type oligosaccharides were the major structures in gull IgG. Our data indicated that some N-glycans from both GEW-glycoproteins and gull IgG contain the Gal alpha 1-4Gal beta 1-4GlcNAc beta 1- sequence, but the ratio of alpha-Gal-capped residues to non-alpha-Gal-capped residues in the nonreducing termini of N-glycans is much lower than that in those of pigeon glycoproteins.

Indexed as

CharadriiformesAnimalsEgg WhiteEgg YolkGlycoproteinsImmunoglobulin GMass SpectrometryPolysaccharidesSpecies SpecificityTime FactorsGlycoproteinsImmunoglobulin GPolysaccharides

Identifiers

PMID19240272
PMCPMC2688389
OpenAlexW2142494552

What OpenQuestion holds

Textmetadata
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.