Evidence map›Paper›PMID 41100667›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2025

A protein dynamics-based deep learning model enhances predictions of fitness and epistasis.

Ngoc Huynh, I Can Kazan, Jin Lu, Bethany Kolbaba-Kartchner, Jeremy H Mills, S Banu Ozkan

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. A protein dynamics-based deep learning model enhances predictions of fitness and epistasis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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.

Ngoc Huynh *Center for Biological Physics, Arizona State University, Tempe, AZ 85287.ORCID 0009-0005-1065-2090
I Can Kazan *Center for Biological Physics, Arizona State University, Tempe, AZ 85287.ORCID 0000-0003-2593-4179
Jin Lu *Center for Biological Physics, Arizona State University, Tempe, AZ 85287.
Bethany Kolbaba-KartchnerCenter for Biological Physics, Arizona State University, Tempe, AZ 85287.
Jeremy H MillsCenter for Biological Physics, Arizona State University, Tempe, AZ 85287.ORCID 0000-0003-2017-1846
S Banu OzkanCenter for Biological Physics, Arizona State University, Tempe, AZ 85287.ORCID 0000-0002-9351-3758

Funding

Gordon and Betty Moore Foundation (GBMF) AWD00034439NSF (NSF) 1901709
6 · The paper itself

Abstract

Deep learning has advanced our ability to assess the effects that individual mutations have on protein function; however, predicting the complex interplay between two or more mutations remains challenging. Here, we seek to address this challenge by building a deep learning framework that incorporates information related to protein dynamics. Namely, we build a neural network architecture using a physics-based metric called the Asymmetric Dynamic Coupling Index (DCI

Indexed as

beta-LactamasesDeep LearningEpistasis, GeneticProteinsMutationNeural Networks, Computerbeta-Lactamasesbeta-lactamase TEM-1Proteinsallosterydeep learningepistasisprotein dynamics

Identifiers

PMID41100667
PMCPMC12557479

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.