Evidence map›Paper›PMID 20012955›Full record

ArticleImmunogenetics2010

Structural correlates of mouse IgA allotypes.

Julia M Phillips-Quagliata

Abstract read
PubMed Publisher
In one paragraph

Article in Immunogenetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 85% 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

2 citing papers in PubMed, 1 citations in OpenAlex.

  1. Article
  2. 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

1 author at 1 institution in 1 country.

Julia M Phillips-QuagliataDepartment of Pathology, New York University School of Medicine, New York, NY 10016, USA. phillj01@med.nyu.edu
New York University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A set of mouse IgAs containing amino acids differing amongst the six alpha-chain allotypes was constructed by mutating an S107-IgA plasmid and transfecting it into a non-producer myeloma cell line along with a kappa-chain plasmid. The secreted IgAs were examined for their possession of a covalent bond between alpha- and light (L)-chains and for their ability to bind to three anti-allotypic monoclonal antibodies, HIS-M2, HY-15, and HY-16. IgA of the Igh-2(a) allotype was found to be unique in its total lack of a covalent bond between alpha and L: -chains, formation of which apparently depends on the presence of an "extra" Cys in the hinges of all of the other five allotypes. The allotypic epitopes are associated with identifiable amino acids in the Calpha1 region of the molecule. Binding to HIS-M2 requires Ala 216 whereas binding to HY-15 requires Pro 216 and Asp 222. Binding to Hy-16 requires Arg 183 and either Pro 216 or Ser 216 but not Ala 216. However, binding to HY-16 by all of the IgAs produced by transfectants is impaired by defective glycosylation in the transfected myeloma and is only revealed after deglycosylation.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsAntibodies, MonoclonalEpitopesGlycosylationImmunoglobulin AMiceMice, Inbred BALB CMice, Inbred C57BLMolecular Sequence DataProtein IsoformsSequence AlignmentSpecies SpecificityAntibodies, MonoclonalEpitopesImmunoglobulin AProtein Isoforms

Identifiers

PMID20012955
OpenAlexW2032911579

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.