Evidence map›Paper›PMID 27975143›Full record

ReviewHistochemistry and cell biology2017

Sialylation of N-glycans: mechanism, cellular compartmentalization and function.

Gaurang P Bhide, Karen J Colley

Open access · bronzeAbstract readReview
In one paragraph

Review in Histochemistry and cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
10.8field-weighted citation impact, top 1% 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

126 citing papers in PubMed, 227 citations in OpenAlex.

  1. Trial
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  16. CD21Frontiers in immunology · 2025
    Article
  17. Article
  18. Review
  19. Article
  20. SerumBiomolecules · 2024
    Article

66 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

2 authors at 1 institution in 1 country.

Gaurang P BhideDepartment of Biochemistry and Molecular Genetics, College of Medicine, The University of Illinois at Chicago, 900 S. Ashland Avenue, MC669, Chicago, IL, 60607, USA.
Karen J ColleyDepartment of Biochemistry and Molecular Genetics, College of Medicine, The University of Illinois at Chicago, 900 S. Ashland Avenue, MC669, Chicago, IL, 60607, USA. karenc@uic.edu.
University of Illinois Chicago · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sialylated N-glycans play essential roles in the immune system, pathogen recognition and cancer. This review approaches the sialylation of N-glycans from three perspectives. The first section focuses on the sialyltransferases that add sialic acid to N-glycans. Included in the discussion is a description of these enzymes' glycan acceptors, conserved domain organization and sequences, molecular structure and catalytic mechanism. In addition, we discuss the protein interactions underlying the polysialylation of a select group of adhesion and signaling molecules. In the second section, the biosynthesis of sialic acid, CMP-sialic acid and sialylated N-glycans is discussed, with a special emphasis on the compartmentalization of these processes in the mammalian cell. The sequences and mechanisms maintaining the sialyltransferases and other glycosylation enzymes in the Golgi are also reviewed. In the final section, we have chosen to discuss processes in which sialylated glycans, both N- and O-linked, play a role. The first part of this section focuses on sialic acid-binding proteins including viral hemagglutinins, Siglecs and selectins. In the second half of this section, we comment on the role of sialylated N-glycans in cancer, including the roles of β1-integrin and Fas receptor N-glycan sialylation in cancer cell survival and drug resistance, and the role of these sialylated proteins and polysialic acid in cancer metastasis.

Indexed as

AnimalsCellsHumansNeoplasmsPolysaccharidesSelectinsSialic Acid Binding Immunoglobulin-like LectinsSialic AcidsPolysaccharidespolysialic acidSelectinsSialic Acid Binding Immunoglobulin-like LectinsSialic AcidsGolgiPolysialic acidSelectinsSialic acidSialyltransferaseSiglecs

Identifiers

PMID27975143
PMCPMC7088086
OpenAlexW2564847909

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.