Evidence map›Paper›PMID 22327427›Full record

ReviewmAbs

Disulfide bond structures of IgG molecules: structural variations, chemical modifications and possible impacts to stability and biological function.

Hongcheng Liu, Kimberly May

Open access · goldAbstract readReview
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 207 papers.

0numbers the graph read from it
0cells of the map it votes in
207citing papers in PubMed
17.2field-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

207 citing papers in PubMed, 465 citations in OpenAlex.

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147 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 1 country.

Hongcheng LiuMerck Research Laboratories, Union, NJ, USA. hongcheng.liu@merck.com
Kimberly May
Merck & Co., Inc., Rahway, NJ, USA (United States) · USUniversity of South Carolina Union · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The disulfide bond structures established decades ago for immunoglobulins have been challenged by findings from extensive characterization of recombinant and human monoclonal IgG antibodies. Non-classical disulfide bond structure was first identified in IgG4 and later in IgG2 antibodies. Although, cysteine residues should be in the disulfide bonded states, free sulfhydryls have been detected in all subclasses of IgG antibodies. In addition, disulfide bonds are susceptible to chemical modifications, which can further generate structural variants such as IgG antibodies with trisulfide bond or thioether linkages. Trisulfide bond formation has also been observed for IgG of all subclasses. Degradation of disulfide bond through β-elimination generates free sulfhydryls disulfide and dehydroalanine. Further reaction between free sulfhydryl and dehydroalanine leads to the formation of a non-reducible cross-linked species. Hydrolysis of the dehydroalanine residue contributes substantially to antibody hinge region fragmentation. The effect of these disulfide bond variations on antibody structure, stability and biological function are discussed in this review.

Indexed as

Antibodies, MonoclonalDisulfidesHumansImmunoglobulin GProtein IsoformsRecombinant ProteinsAntibodies, MonoclonalDisulfidesImmunoglobulin GProtein IsoformsRecombinant Proteins

Identifiers

PMID22327427
PMCPMC3338938
OpenAlexW1555361166

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.