Evidence map›Paper›PMID 29031045›Full record

ArticleMolecular immunology2017

Structural characterization of the Man5 glycoform of human IgG3 Fc.

Ishan S Shah, Scott Lovell, Nurjahan Mehzabeen, Kevin P Battaile, Thomas J Tolbert

Open access · greenAbstract read
In one paragraph

Article in Molecular immunology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Constant domain polymorphisms influence monoclonal antibody stability and dynamics.Protein science : a publication of the Protein Society · 2023
    Article
  5. Article
  6. Article
  7. Staphylococcal protein A inhibits complement activation by interfering with IgG hexamer formation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
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

5 authors at 2 institutions in 1 country.

Ishan S ShahDepartment of Pharmaceutical Chemistry, University of Kansas, Lawrence, KS, USA.
Scott LovellProtein Structure Laboratory, Del Shankel Structural Biology Center, University of Kansas, Lawrence, KS, USA.
Nurjahan MehzabeenProtein Structure Laboratory, Del Shankel Structural Biology Center, University of Kansas, Lawrence, KS, USA.
Kevin P BattaileIMCA-CAT, Hauptman-Woodward Medical Research Institute, Argonne, IL, USA.
Thomas J TolbertDepartment of Pharmaceutical Chemistry, University of Kansas, Lawrence, KS, USA. Electronic address: tolbert@ku.edu.
University of Kansas · USHauptman-Woodward Medical Research Institute · US

Funding

Protein Structure Laboratory P30GM110761 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI HANZLIK, ROBERT P · 2014 to 2018
$5.6M
The Role of Glycosylation in Regulating Immune ResponsesR01GM090080 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI TOLBERT, THOMAS J · 2010 to 2013
$1.1M
NIGMS NIH HHS P30 GM110761NIGMS NIH HHS R01 GM090080
6 · The paper itself

Abstract

Immunoglobulin G (IgG) consists of four subclasses in humans: IgG1, IgG2, IgG3 and IgG4, which are highly conserved but have unique differences that result in subclass-specific effector functions. Though IgG1 is the most extensively studied IgG subclass, study of other subclasses is important to understand overall immune function and for development of new therapeutics. When compared to IgG1, IgG3 exhibits a similar binding profile to Fcγ receptors and stronger activation of complement. All IgG subclasses are glycosylated at N297, which is required for Fcγ receptor and C1q complement binding as well as maintaining optimal Fc conformation. We have determined the crystal structure of homogenously glycosylated human IgG3 Fc with a GlcNAc

Indexed as

Crystallography, X-RayGlycoproteinsGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GMannoseGlycoproteinsImmunoglobulin Fc FragmentsImmunoglobulin GMannoseFc receptorGlycosylationHigh mannoseImmunoglobulin GX-ray crystal structure

Identifiers

PMID29031045
PMCPMC5694352
OpenAlexW2762727349

What OpenQuestion holds

Textmetadata
LicenceTDM
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.