Evidence map›Paper›PMID 34288809›Full record

ReviewmAbs

The therapeutic potential of sialylated Fc domains of human IgG.

Richard J Pleass

Open access · goldAbstract readReviewVideo-Audio Media
In one paragraph

Review in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Immunoglobulin GFrontiers in immunology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Serum immunoglobulin and the threshold of Fc receptor-mediated immune activation.Biochimica et biophysica acta. General subjects · 2023
    Review
  10. Article
  11. 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

1 author at 1 institution in 1 country.

Richard J PleassDepartment of Tropical Disease Biology, Tropical Disease Biology, Liverpool School of Tropical Medicine, Liverpool, UK.ORCID 0000-0001-7438-8296
Liverpool School of Tropical Medicine · GB

Funding

Wellcome Trust 208938/Z/17/Z
6 · The paper itself

Abstract

Pathogens frequently use multivalent binding to sialic acid to infect cells or to modulate immunity through interactions with human sialic acid-binding immunoglobulin-type lectins (Siglecs). Molecules that interfere with these interactions could be of interest as diagnostics, anti-infectives or as immune modulators. This review describes the development of molecular scaffolds based on the crystallizable fragment (Fc) region of immunoglobulin (Ig) G that deliver high-avidity binding to innate immune receptors, including sialic acid-dependent receptors. The ways in which the sialylated Fc may be engineered as immune modulators that mimic the anti-inflammatory properties of intravenous polyclonal Ig or as blockers of sialic-acid-dependent infectivity by viruses are also discussed.

Indexed as

Immunoglobulin Fc FragmentsImmunoglobulin GN-Acetylneuraminic AcidAnimalsGlycosylationHumansSialic Acid Binding Immunoglobulin-like LectinsImmunoglobulin Fc FragmentsImmunoglobulin GN-Acetylneuraminic AcidSialic Acid Binding Immunoglobulin-like LectinsFcIgGinfluenzasialic acidSiglecvirus

Identifiers

PMID34288809
PMCPMC8296966
OpenAlexW3183755046

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.