Evidence map›Paper›PMID 36671521›Full record

ArticleBiomolecules2023

Prediction of Protein Function from Tertiary Structure of the Active Site in Heme Proteins by Convolutional Neural Network.

Hiroko X Kondo, Hiroyuki Iizuka, Gen Masumoto, Yuichi Kabaya, Yusuke Kanematsu, Yu Takano

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Computational Exploration of Minimum Energy Reaction Pathway of NInternational journal of molecular sciences · 2023
    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 at 6 institutions in 1 country.

Hiroko X KondoFaculty of Engineering, Kitami Institute of Technology, 165 Koen-cho, Kitami 090-8507, Japan.ORCID 0000-0002-0782-9677
Hiroyuki IizukaGraduate School of Information Science and Technology, Hokkaido University, Kita 14, Nishi 9, Kitaku, Sapporo 060-0814, Japan.
Gen MasumotoInformation Systems Division, RIKEN Information R&D and Strategy Headquarters, 2-1 Hirosawa, Wako 351-0198, Japan.ORCID 0000-0002-8906-0952
Yuichi KabayaFaculty of Engineering, Kitami Institute of Technology, 165 Koen-cho, Kitami 090-8507, Japan.
Yusuke KanematsuGraduate School of Information Sciences, Hiroshima City University, 3-4-1 Ozukahigashi Asaminamiku, Hiroshima 731-3194, Japan.ORCID 0000-0003-3546-3198
Yu TakanoGraduate School of Information Sciences, Hiroshima City University, 3-4-1 Ozukahigashi Asaminamiku, Hiroshima 731-3194, Japan.ORCID 0000-0002-4165-8672
Hiroshima City University · JPHiroshima University · JPHokkaido University · JPKitami Institute of Technology · JPRIKEN · JPRIKEN Center for Biosystems Dynamics Research · JP

Funding

Japan Society for the Promotion of Science 19H02752Japan Society for the Promotion of Science 19K06589Japan Society for the Promotion of Science 21K14741Japan Society for the Promotion of Science 22H04813Japan Society for the Promotion of Science 22K06164Ministry of Education, Culture, Sports, Science and Technology 20H05883
6 · The paper itself

Abstract

Structure-function relationships in proteins have been one of the crucial scientific topics in recent research. Heme proteins have diverse and pivotal biological functions. Therefore, clarifying their structure-function correlation is significant to understand their functional mechanism and is informative for various fields of science. In this study, we constructed convolutional neural network models for predicting protein functions from the tertiary structures of heme-binding sites (active sites) of heme proteins to examine the structure-function correlation. As a result, we succeeded in the classification of oxygen-binding protein (OB), oxidoreductase (OR), proteins with both functions (OB-OR), and electron transport protein (ET) with high accuracy. Although the misclassification rate for OR and ET was high, the rates between OB and ET and between OB and OR were almost zero, indicating that the prediction model works well between protein groups with quite different functions. However, predicting the function of proteins modified with amino acid mutation(s) remains a challenge. Our findings indicate a structure-function correlation in the active site of heme proteins. This study is expected to be applied to the prediction of more detailed protein functions such as catalytic reactions.

Indexed as

HemeproteinsAmino AcidsBinding SitesCatalytic DomainNeural Networks, ComputerAmino AcidsHemeproteinsactive site conformationconvolutional neural networkmachine learningstructure–function correlation

Identifiers

PMID36671521
PMCPMC9855806
OpenAlexW4313893898

What OpenQuestion holds

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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.