Evidence map›Paper›PMID 28855581›Full record

ArticleScientific reports2017

Elucidation of potential sites for antibody engineering by fluctuation editing.

Saeko Yanaka, Yoshitaka Moriwaki, Kouhei Tsumoto, Kenji Sugase

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. 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
2.8field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

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  11. Structure-guided design fine-tunes pharmacokinetics, tolerability, and antitumor profile of multispecific frizzled antibodies.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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

4 authors at 3 institutions in 1 country.

Saeko YanakaBioorganic Research Institute, Suntory Foundation for Life Sciences, Kyoto, Japan.
Yoshitaka MoriwakiDepartment of Biotechnology and Agricultural Bioinformatics Research Unit, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.
Kouhei TsumotoDepartment of Bioengineering, Graduate School of Engineering, The University of Tokyo, Tokyo, Japan.
Kenji SugaseBioorganic Research Institute, Suntory Foundation for Life Sciences, Kyoto, Japan. sugase@moleng.kyoto-u.ac.jp.
The University of Tokyo · JPNational Institutes of Natural Sciences · JPSuntory Foundation for Life Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Target-specific monoclonal antibodies can be routinely acquired, but the sequences of naturally acquired antibodies are not always affinity-matured and methods that increase antigen affinity are desirable. Most biophysical studies have focused on the complementary determining region (CDR), which directly contacts the antigen; however, it remains difficult to increase the affinity as much as desired. While strategies to alter the CDR to increase antibody affinity are abundant, those that target non-CDR regions are scarce. Here we describe a new method, designated fluctuation editing, which identifies potential mutation sites and engineers a high-affinity antibody based on conformational fluctuations observed by NMR relaxation dispersion. Our data show that relaxation dispersion detects important fluctuating residues that are not located in the CDR and that increase antigen-antibody affinity by point mutation. The affinity-increased mutants are shown to fluctuate less in their free form and to form a more packed structure in their antigen-bound form.

Indexed as

Binding SitesProtein EngineeringProtein Interaction Domains and MotifsAmino Acid SequenceAntibodies, MonoclonalAntibody AffinityAntigensComplementarity Determining RegionsHumansImmunoglobulin Fab FragmentsModels, MolecularMutationProtein ConformationProtein StabilityQuantitative Structure-Activity RelationshipThermodynamicsAntibodies, MonoclonalAntigensComplementarity Determining RegionsImmunoglobulin Fab Fragments

Identifiers

PMID28855581
PMCPMC5577056
OpenAlexW2750032024

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.