Evidence map›Paper›PMID 36699363›Full record

ArticleBioinformatics advances2022

AbAdapt: an adaptive approach to predicting antibody-antigen complex structures from sequence.

Ana Davila, Zichang Xu, Songling Li, John Rozewicki, Jan Wilamowski, Sergei Kotelnikov, Dima Kozakov, Shunsuke Teraguchi, Daron M Standley

Abstract read
In one paragraph

Article in Bioinformatics advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Review
  2. Improving B-cell epitope prediction.Drug discovery today · 2025
    Review
  3. Article
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  8. Article
  9. Review
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  14. How can we discover developable antibody-based biotherapeutics?Frontiers in molecular biosciences · 2023
    Review
  15. Improved Antibody-Specific Epitope Prediction Using AlphaFold and AbAdapt.Chembiochem : a European journal of chemical biology · 2022
    Article
  16. Review
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

9 authors.

Ana DavilaResearch Institute for Microbial Diseases, Department of Genome Informatics, Osaka University, Suita 565-0871, Japan.ORCID https://orcid.org/0000-0002-2076-6842
Zichang XuResearch Institute for Microbial Diseases, Department of Genome Informatics, Osaka University, Suita 565-0871, Japan.ORCID https://orcid.org/0000-0003-1940-6898
Songling LiResearch Institute for Microbial Diseases, Department of Genome Informatics, Osaka University, Suita 565-0871, Japan.
John RozewickiResearch Institute for Microbial Diseases, Department of Genome Informatics, Osaka University, Suita 565-0871, Japan.
Jan WilamowskiResearch Institute for Microbial Diseases, Department of Genome Informatics, Osaka University, Suita 565-0871, Japan.
Sergei KotelnikovDepartment of Applied Mathematics and Statistics, Stony Brook University, Stony Brook, NY 11794-5252, USA.ORCID https://orcid.org/0000-0001-9400-101X
Dima KozakovDepartment of Applied Mathematics and Statistics, Stony Brook University, Stony Brook, NY 11794-5252, USA.
Shunsuke TeraguchiResearch Institute for Microbial Diseases, Department of Genome Informatics, Osaka University, Suita 565-0871, Japan.
Daron M StandleyResearch Institute for Microbial Diseases, Department of Genome Informatics, Osaka University, Suita 565-0871, Japan.ORCID https://orcid.org/0000-0003-4078-0817

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Motivation: The scoring of antibody-antigen docked poses starting from unbound homology models has not been systematically optimized for a large and diverse set of input sequences. Results: To address this need, we have developed AbAdapt, a webserver that accepts antibody and antigen sequences, models their 3D structures, predicts epitope and paratope, and then docks the modeled structures using two established docking engines (Piper and Hex). Each of the key steps has been optimized by developing and training new machine-learning models. The sequences from a diverse set of 622 antibody-antigen pairs with known structure were used as inputs for leave-one-out cross-validation. The final set of cluster representatives included at least one 'Adequate' pose for 550/622 (88.4%) of the queries. The median (interquartile range) ranks of these 'Adequate' poses were 22 (5-77). Similar results were obtained on a holdout set of 100 unrelated antibody-antigen pairs. When epitopes were repredicted using docking-derived features for specific antibodies, the median ROC AUC increased from 0.679 to 0.720 in cross-validation and from 0.694 to 0.730 in the holdout set. Availability and implementation: AbAdapt and related data are available at https://sysimm.org/abadapt/. Supplementary information: Supplementary data are available at

Identifiers

PMID36699363
PMCPMC9710585

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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.