Evidence map›Paper›PMID 29191832›Full record

ArticleThe Journal of biological chemistry2018

Molecular characterization of human anti-hinge antibodies derived from single-cell cloning of normal human B cells.

Tao Huang, Mary Mathieu, Sophia Lee, Xinhua Wang, Yee Seir Kee, Jack J Bevers, Claudio Ciferri, Alberto Estavez, Manda Wong, Nancy Y Chiang and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

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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

12 authors at 2 institutions in 3 countries.

Tao HuangFrom the Antibody Engineering Department and.
Mary MathieuFrom the Antibody Engineering Department and.
Sophia LeeFrom the Antibody Engineering Department and.
Xinhua WangFrom the Antibody Engineering Department and.
Yee Seir KeeFrom the Antibody Engineering Department and.
Jack J BeversFrom the Antibody Engineering Department and.
Claudio CiferriStructural Biology Department-Cryo-EM Unit, Genentech, South San Francisco, California 94080.
Alberto EstavezStructural Biology Department-Cryo-EM Unit, Genentech, South San Francisco, California 94080.
Manda WongStructural Biology Department-Cryo-EM Unit, Genentech, South San Francisco, California 94080.
Nancy Y ChiangFrom the Antibody Engineering Department and.
Gerald NakamuraFrom the Antibody Engineering Department and.
Randall J BrezskiFrom the Antibody Engineering Department and brezski.randall@gene.com.
Recombinant Antibody Technology (United Kingdom) · GBInstitute for Structural Research · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Anti-hinge antibodies (AHAs) are an autoantibody subclass that, following proteolytic cleavage, recognize cryptic epitopes exposed in the hinge regions of immunoglobulins (Igs) and do not bind to the intact Ig counterpart. AHAs have been postulated to exacerbate chronic inflammatory disorders such as inflammatory bowel disease and rheumatoid arthritis. On the other hand, AHAs may protect against invasive microbial pathogens and cancer. However, despite more than 50 years of study, the origin and specific B cell compartments that express AHAs remain elusive. Recent research on serum AHAs suggests that they arise during an active immune response, in contrast to previous proposals that they derive from the preexisting immune repertoire in the absence of antigenic stimuli. We report here the isolation and characterization of AHAs from memory B cells, although anti-hinge-reactive B cells were also detected in the naive B cell compartment. IgG AHAs cloned from a single human donor exhibited restricted specificity for protease-cleaved F(ab')

Indexed as

Antibodies, MonoclonalAutoantibodiesB-LymphocytesEnzyme-Linked Immunosorbent AssayFlow CytometryHumansImmunoglobulin GMatrix Metalloproteinase 3Matrix Metalloproteinase 7Antibodies, MonoclonalAutoantibodiesImmunoglobulin GMatrix Metalloproteinase 3Matrix Metalloproteinase 7antibody engineeringautoimmunityimmunogenicityimmunoglobulin G (IgG)monoclonal antibody

Identifiers

PMID29191832
PMCPMC5777262
OpenAlexW2774350129

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.