Evidence map›Paper›PMID 25943546›Full record

ArticleNucleic acids research2015

(PS)2: protein structure prediction server version 3.0.

Tsun-Tsao Huang, Jenn-Kang Hwang, Chu-Huang Chen, Chih-Sheng Chu, Chi-Wen Lee, Chih-Chieh Chen

Abstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
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  3. SeqCP: A sequence-based algorithm for searching circularly permuted proteins.Computational and structural biotechnology journal · 2023
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  11. Role of juvenile hormone receptorZoological research · 2021
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  17. Article
  18. Computational Analysis ofCancer informatics · 2020
    Article
  19. Article
  20. 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.

Tsun-Tsao HuangInstitute of Bioinformatics and Systems Biology, National Chiao Tung University, Hsinchu 30068, Taiwan Center for Bioinformatics Research, National Chiao Tung University, Hsinchu 30068, Taiwan.
Jenn-Kang HwangInstitute of Bioinformatics and Systems Biology, National Chiao Tung University, Hsinchu 30068, Taiwan Center for Bioinformatics Research, National Chiao Tung University, Hsinchu 30068, Taiwan Department of Biological Science and Technology, National Chiao Tung University, Hsinchu 30068, Taiwan Department of Bioinformatics and Medical Engineering, Asia University, Taichung 41354, Taiwan.
Chu-Huang ChenDepartment of Vascular and Medicinal Research, Texas Heart Institute, Houston, TX 77030, USA Center for Lipid Biosciences, Kaohsiung Medical University Hospital, Kaohsiung Medical University, Kaohsiung 80708, Taiwan L5 Research Center, China Medical University Hospital, China Medical University, Taichung 40402, Taiwan Section of Cardiovascular Research, Department of Medicine, Baylor College of Medicine, Houston, TX 77030, USA.
Chih-Sheng ChuCenter for Lipid Biosciences, Kaohsiung Medical University Hospital, Kaohsiung Medical University, Kaohsiung 80708, Taiwan Department of Internal Medicine, Kaohsiung Medical University Hospital, Kaohsiung Medical University, Kaohsiung 80708, Taiwan.
Chi-Wen LeeCenter for Bioinformatics Research, National Chiao Tung University, Hsinchu 30068, Taiwan Department of Biological Science and Technology, National Chiao Tung University, Hsinchu 30068, Taiwan.
Chih-Chieh ChenCenter for Lipid Biosciences, Kaohsiung Medical University Hospital, Kaohsiung Medical University, Kaohsiung 80708, Taiwan Center for Lipid and Glycomedicine Research, Kaohsiung Medical University, Kaohsiung 80708, Taiwan Institute of Medical Science and Technology, National Sun Yat-sen University, Kaohsiung 80424, Taiwan chieh.bi91g@nctu.edu.tw.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein complexes are involved in many biological processes. Examining coupling between subunits of a complex would be useful to understand the molecular basis of protein function. Here, our updated (PS)(2) web server predicts the three-dimensional structures of protein complexes based on comparative modeling; furthermore, this server examines the coupling between subunits of the predicted complex by combining structural and evolutionary considerations. The predicted complex structure could be indicated and visualized by Java-based 3D graphics viewers and the structural and evolutionary profiles are shown and compared chain-by-chain. For each subunit, considerations with or without the packing contribution of other subunits cause the differences in similarities between structural and evolutionary profiles, and these differences imply which form, complex or monomeric, is preferred in the biological condition for the subunit. We believe that the (PS)(2) server would be a useful tool for biologists who are interested not only in the structures of protein complexes but also in the coupling between subunits of the complexes. The (PS)(2) is freely available at http://ps2v3.life.nctu.edu.tw/.

Indexed as

SoftwareInternetModels, MolecularMultiprotein ComplexesProtein ConformationSequence Analysis, ProteinMultiprotein Complexes

Identifiers

PMID25943546
PMCPMC4489310

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LicenceCC BY-NC
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Registered trials

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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.