Evidence map›Paper›PMID 34302810›Full record

ArticleThe Journal of biological chemistry2021

Solution structures of human myeloma IgG3 antibody reveal extended Fab and Fc regions relative to the other IgG subclasses.

Valentina A Spiteri, Margaret Goodall, James Doutch, Robert P Rambo, Jayesh Gor, Stephen J Perkins

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

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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

6 authors.

Valentina A SpiteriDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom.
Margaret GoodallInstitute for Biomedical Research, University of Birmingham, Birmingham, United Kingdom.
James DoutchISIS Facility, STFC Rutherford Appleton Laboratory, Harwell Campus, Didcot, Oxfordshire, United Kingdom.
Robert P RamboDiamond Light Source Ltd, Harwell Science and Innovation Campus, Didcot, Oxfordshire, United Kingdom.
Jayesh GorDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom.
Stephen J PerkinsDepartment of Structural and Molecular Biology, Division of Biosciences, University College London, London, United Kingdom. Electronic address: s.perkins@ucl.ac.uk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human immunoglobulin G subclass 3 (IgG3) possesses a uniquely long hinge region that separates its Fab antigen-binding and Fc receptor-binding regions. Owing to this hinge length, the molecular structure of full-length IgG3 remains elusive, and the role of the two conserved Fc glycosylation sites are unknown. To address these issues, we subjected glycosylated and deglycosylated human myeloma IgG3 to multidisciplinary solution structure studies. Using analytical ultracentrifugation, the elongated structure of IgG3 was determined from the reduced sedimentation coefficients s

Indexed as

Amino Acid SequenceChromatography, LiquidGlycosylationHumansImmunoglobulin Fab FragmentsImmunoglobulin GMass SpectrometryMolecular Dynamics SimulationMultiple MyelomaMyeloma ProteinsNeutronsProtein ConformationReceptors, FcScattering, Small AngleSequence Homology, Amino AcidUltracentrifugationImmunoglobulin Fab FragmentsImmunoglobulin Gmyeloma immunoglobulinsMyeloma ProteinsReceptors, Fcanalytical ultracentrifugationantibody modelinghuman IgG subclassessmall-angle neutron scatteringsmall angle X-ray scattering

Identifiers

PMID34302810
PMCPMC8371214

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Registered trials

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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.