Evidence map›Paper›PMID 25995273›Full record

ArticleMolecular & cellular proteomics : MCP2015

Tissue-Specific Glycosylation at the Glycopeptide Level.

Katalin F Medzihradszky, Krista Kaasik, Robert J Chalkley

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed, 1 pooled it
7.2field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 1 synthesis or guideline pooled it, 122 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Mass Spectrometry-Based Comparative Analysis ofACS chemical neuroscience · 2025
    Article
  11. Article
  12. Glycosylation in kidney diseases.Precision clinical medicine · 2025
    Review
  13. Article
  14. Article
  15. Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

15 more citing papers are in PubMed but not listed here.

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.

Katalin F MedzihradszkyFrom the ‡Department of Pharmaceutical Chemistry, School of Pharmacy, University of California San Francisco, 600 16th Street Genentech Hall, N474A, Box 2240, San Francisco, California 94158-2517 folkl@cgl.ucsf.edu.
Krista KaasikFrom the ‡Department of Pharmaceutical Chemistry, School of Pharmacy, University of California San Francisco, 600 16th Street Genentech Hall, N474A, Box 2240, San Francisco, California 94158-2517.
Robert J ChalkleyFrom the ‡Department of Pharmaceutical Chemistry, School of Pharmacy, University of California San Francisco, 600 16th Street Genentech Hall, N474A, Box 2240, San Francisco, California 94158-2517.
University of California, San Francisco · US

Funding

Bio-Organic Biomedical Mass Spectromy ResourceP41GM103481 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BURLINGAME, ALMA L · 2012 to 2015
$6.4M
Howard Hughes Medical InstituteNIGMS NIH HHS P41 GM103481PHS HHS NIGMS 8P41GM103481
6 · The paper itself

Abstract

This manuscript describes the enrichment and mass spectrometric analysis of intact glycopeptides from mouse liver, which yielded site-specific N- and O-glycosylation data for ∼ 130 proteins. Incorporation of different sialic acid variants in both N- and O-linked glycans was observed, and the importance of using both collisional activation and electron transfer dissociation for glycopeptide analysis was illustrated. The N-glycan structures of predicted lysosomal, endoplasmic reticulum (ER), secreted and transmembrane proteins were compared. The data suggest that protein N-glycosylation differs depending on cellular location. The glycosylation patterns of several mouse liver and mouse brain glycopeptides were compared. Tissue-specific differences in glycosylation were observed between sites within the same protein: Some sites displayed a similar spectrum of glycan structures in both tissues, whereas for others no overlap was observed. We present comparative brain/liver glycosylation data on 50 N-glycosylation sites from 34 proteins and 13 O-glycosylation sites from seven proteins.

Indexed as

Organ SpecificityAnimalsBrainEndoplasmic ReticulumGlycopeptidesGlycosylationLiverLysosomesMembrane ProteinsMiceGlycopeptidesMembrane Proteins

Identifiers

PMID25995273
PMCPMC4528240
OpenAlexW2167584554

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.