Evidence map›Paper›PMID 35656889›Full record

ArticleJournal of computational chemistry2022

Sparse group selection and analysis of function-related residue for protein-state recognition.

Fangyun Bai, Kin Ming Puk, Jin Liu, Hongyu Zhou, Peng Tao, Wenyong Zhou, Shouyi Wang

Abstract read
In one paragraph

Article in Journal of computational chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

7 authors.

Fangyun BaiDepartment of Management Science and Engineering, Tongji University, Shanghai, China.ORCID 0000-0003-3138-6500
Kin Ming PukDepartment of Industrial, Manufacturing and Systems Engineering, University of Texas at Arlington, Arlington, Texas, USA.ORCID 0000-0002-6432-101X
Jin LiuDepartment of Pharmaceutical Sciences, University of North Texas System College of Pharmacy, University of North Texas Health Science Center, Fort Worth, Texas, USA.ORCID 0000-0002-1067-4063
Hongyu ZhouDepartment of Chemistry, Center for Scientific Computation, Center for Drug Discovery, Design, and Delivery (CD4), Southern Methodist University, Dallas, Texas, USA.
Peng TaoDepartment of Chemistry, Center for Scientific Computation, Center for Drug Discovery, Design, and Delivery (CD4), Southern Methodist University, Dallas, Texas, USA.ORCID 0000-0002-2488-0239
Wenyong ZhouDepartment of Management Science and Engineering, Tongji University, Shanghai, China.ORCID 0000-0001-7507-4002
Shouyi WangDepartment of Industrial, Manufacturing and Systems Engineering, University of Texas at Arlington, Arlington, Texas, USA.ORCID 0000-0001-6366-3619

Funding

Probing Hidden Conformational Space and Dynamical States of Circadian Clock Proteins through Rigid Residue Scan and Machine LearningR15GM122013 · NIGMS · SOUTHERN METHODIST UNIVERSITY · PI TAO, PENG · 2018 to 2023
$800k
National Science Foundation 1434401National Science Foundation 1537504NIGMS NIH HHS R15 GM122013Southern Methodist University Dissertation Fellowship
6 · The paper itself

Abstract

Machine learning methods have helped to advance wide range of scientific and technological field in recent years, including computational chemistry. As the chemical systems could become complex with high dimension, feature selection could be critical but challenging to develop reliable machine learning based prediction models, especially for proteins as bio-macromolecules. In this study, we applied sparse group lasso (SGL) method as a general feature selection method to develop classification model for an allosteric protein in different functional states. This results into a much improved model with comparable accuracy (Acc) and only 28 selected features comparing to 289 selected features from a previous study. The Acc achieves 91.50% with 1936 selected feature, which is far higher than that of baseline methods. In addition, grouping protein amino acids into secondary structures provides additional interpretability of the selected features. The selected features are verified as associated with key allosteric residues through comparison with both experimental and computational works about the model protein, and demonstrate the effectiveness and necessity of applying rigorous feature selection and evaluation methods on complex chemical systems.

Indexed as

Machine LearningProteinsAlgorithmsProteinsclassificationfeature selectionfunction-related residuesprotein statessparse group lasso

Identifiers

PMID35656889
PMCPMC9248267

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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.