Evidence map›Paper›PMID 25151374›Full record

ArticleAdvances in neurobiology

Synthesis, Processing, and Function of N-glycans in N-glycoproteins.

Erhard Bieberich

Abstract read
In one paragraph

Article in Advances in neurobiology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
–field-weighted citation impact
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

93 citing papers in PubMed.

  1. Substrate Versatility of a Recombinant Bifidobacterial Endoglycosidase:International journal of molecular sciences · 2026
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  12. Identification and comparison ofFood chemistry: X · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

33 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

1 author.

Erhard BieberichDepartment of Neuroscience and Regenerative Medicine, Medical College of Georgia, Georgia Regents University, 1120 15th Street Room CA4012, Augusta, GA, 30912, USA, ebieberich@gru.edu.

Funding

Function of ceramide in neurodegenerative diseaseR01AG034389 · NIA · UNIVERSITY OF KENTUCKY · PI BIEBERICH, ERHARD · 2010 to 2020
$3.6M
NIA NIH HHS R01 AG034389
6 · The paper itself

Abstract

Many membrane-resident and secrected proteins, including growth factors and their receptors, are N-glycosylated. The initial N-glycan structure is synthesized in the endoplasmic reticulum (ER) as a branched structure on a lipid anchor (dolichol pyrophosphate) and then co-translationally, "en bloc" transferred and linked via N-acetylglucosamine to asparagine within a specific N-glycosylation acceptor sequence of the nascent recipient protein. In the ER and then the Golgi apparatus, the N-linked glycan structure is modified by hydrolytic removal of sugar residues ("trimming") followed by re-glycosylation with additional sugar residues ("processing") such as galactose, fucose, or sialic acid to form complex N-glycoproteins. While the sequence of the reactions leading to biosynthesis, "en bloc" transfer and processing of N-glycans is well investigated, it is still not completely understood how N-glycans affect the biological fate and function of N-glycoproteins. This review discusses the biology of N-glycoprotein synthesis, processing, and function with specific reference to the physiology and pathophysiology of the nervous system.

Identifiers

PMID25151374
PMCPMC4236024

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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.