Evidence map›Paper›PMID 42136527›Full record

ArticleNucleic acids research2026

PythiaStudio: a one-stop protein engineering platform powered by Pythia model suite.

Jinyuan Sun, Kelun Shi, Han Li, Yinglu Cui, Luoyi Wang, Bian Wu

Abstract read
In one paragraph

Article in Nucleic acids research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Jinyuan SunState Key Laboratory of Microbial Diversity and Innovative Utilization, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0000-0003-3456-0332
Kelun ShiState Key Laboratory of Microbial Diversity and Innovative Utilization, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0009-0003-9063-4006
Han LiIndependent Researcher.
Yinglu CuiState Key Laboratory of Microbial Diversity and Innovative Utilization, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0000-0002-2147-5879
Luoyi WangState Key Laboratory of Microbial Diversity and Innovative Utilization, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Bian WuState Key Laboratory of Microbial Diversity and Innovative Utilization, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.ORCID 0000-0002-6524-2049

Funding

Beijing Municipal Science & Technology Project, China Z241100007724009Chinese Academy of Sciences XDB0810000Fundamental Research Funds for the Central Universities buctrc202539National Key Research and Development Program of China 2023YFA0916000National Natural Science Foundation of China 32225002National Natural Science Foundation of China 32422001Youth Innovation Promotion Association, CAS 2022086
6 · The paper itself

Abstract

Predicting how mutations affect protein stability and protein-protein binding affinity is crucial for protein engineering and drug development. Although several computational tools have been developed for these tasks, they often require specialized expertise and are difficult to integrate into unified workflows. Here, we present PythiaStudio (https://pythiastudio.wulab.xyz), a comprehensive web platform that integrates our recently developed Pythia, Pythia-PPI, and Pythia-Pocket models with complementary protein analysis tools. The platform enables users to predict mutational effects on protein stability and protein-protein binding affinity, ligand binding pocket, through an intuitive interface. Additional features include fitness and structure prediction. PythiaStudio provides interactive visualization tools, including mutation heatmaps, sortable result tables, and structure viewers. Importantly, the platform offers an integrated engineering workflow that combines stability and fitness predictions to guide rational protein design. We demonstrate the utility of this workflow through multiple cases, including different glycoside hydrolases and amidases. In these cases, the two-step computational redesign strategy successfully improved both thermostability and catalytic activity. PythiaStudio democratizes access to state-of-the-art deep learning-based protein engineering methods, enabling researchers without computational expertise to perform sophisticated protein engineering.

Indexed as

Protein EngineeringSoftwareAmidohydrolasesBinding SitesGlycoside HydrolasesInternetModels, MolecularMutationProtein BindingProtein StabilityAmidohydrolasesGlycoside Hydrolases

Identifiers

PMID42136527
PMCPMC13355049

What OpenQuestion holds

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LicenceCC BY
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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.