Evidence map›Paper›PMID 20176268›Full record

ReviewThe Journal of allergy and clinical immunology2010

Structure and function of immunoglobulins.

Harry W Schroeder, Lisa Cavacini

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of allergy and clinical immunology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 813 papers.

0numbers the graph read from it
0cells of the map it votes in
813citing papers in PubMed
43.8field-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

813 citing papers in PubMed, 1,836 citations in OpenAlex.

  1. Characterization of immunoglobulin loci inNAR genomics and bioinformatics · 2026
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753 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 2 institutions in 2 countries.

Harry W SchroederDivision of Clinical Immunology and Rheumatology, Department of Medicine, University of Alabama at Birmingham, Birmingham, AL 35294-2182, USA. hwsj@uab.edu
Lisa Cavacini
Hadassah Medical Center · ILUniversity of Alabama at Birmingham Hospital · US

Funding

The role of Immunoglobulin CDRH3 in Autoimmune DiseaseR01AI048115 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SCHROEDER, HARRY WILLIAM · 2000 to 2010
$3.1M
HLA Region and KIR Genomics in Common Variable Immune DeficiencyU01AI090902 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SCHROEDER, HARRY WILLIAM · 2010 to 2014
$2.9M
Role of IG CDR-H3 in Responses to HIV VaccinesR01AI090742 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SCHROEDER, HARRY WILLIAM · 2010 to 2013
$1.5M
Role of immunoglobulin CDR-H3 in heterosubtypic immunity to influenza virusR21AI088498 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SCHROEDER, HARRY WILLIAM · 2010 to 2011
$401k
NIAID NIH HHS R01 AI048115NIAID NIH HHS R01 AI090742NIAID NIH HHS R21 AI088498NIAID NIH HHS U01 AI090902
6 · The paper itself

Abstract

Immunoglobulins are heterodimeric proteins composed of 2 heavy and 2 light chains. They can be separated functionally into variable domains that bind antigens and constant domains that specify effector functions, such as activation of complement or binding to Fc receptors. The variable domains are created by means of a complex series of gene rearrangement events and can then be subjected to somatic hypermutation after exposure to antigen to allow affinity maturation. Each variable domain can be split into 3 regions of sequence variability termed the complementarity-determining regions (CDRs) and 4 regions of relatively constant sequence termed the framework regions. The 3 CDRs of the heavy chain are paired with the 3 CDRs of the light chain to form the antigen-binding site, as classically defined. The constant domains of the heavy chain can be switched to allow altered effector function while maintaining antigen specificity. There are 5 main classes of heavy chain constant domains. Each class defines the IgM, IgG, IgA, IgD, and IgE isotypes. IgG can be split into 4 subclasses, IgG1, IgG2, IgG3, and IgG4, each with its own biologic properties, and IgA can similarly be split into IgA1 and IgA2.

Indexed as

ImmunoglobulinsAnimalsAntigen-Antibody ReactionsGene Rearrangement, B-LymphocyteGlycosylationHumansImmunity, CellularImmunity, HumoralImmunity, InnateOrgan SpecificityProtein MultimerizationReceptors, FcSignal TransductionStructure-Activity RelationshipImmunoglobulinsReceptors, Fc

Identifiers

PMID20176268
PMCPMC3670108
OpenAlexW1963778872

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.