Evidence map›Paper›PMID 35013238›Full record

ArticleNature communications2022

Helical structure motifs made searchable for functional peptide design.

Cheng-Yu Tsai, Emmanuel Oluwatobi Salawu, Hongchun Li, Guan-Yu Lin, Ting-Yu Kuo, Liyin Voon, Adarsh Sharma, Kai-Di Hu, Yi-Yun Cheng, Sobha Sahoo and 11 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. AI-assisted design of a VEGFR2 agonistic peptide that promotes angiogenesis and wound repair.Protein science : a publication of the Protein Society · 2026
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  11. The Role ofInternational journal of molecular sciences · 2022
    Review
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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

21 authors at 6 institutions in 3 countries.

Cheng-Yu Tsai *Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.ORCID http://orcid.org/0000-0001-6150-4577
Emmanuel Oluwatobi Salawu *Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.ORCID http://orcid.org/0000-0002-4977-0917
Hongchun Li *Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.
Guan-Yu Lin *Institute of Molecular and Cellular Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.ORCID http://orcid.org/0000-0001-6644-6695
Ting-Yu Kuo *Institute of Molecular and Cellular Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.
Liyin Voon *Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.
Adarsh SharmaInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.ORCID http://orcid.org/0000-0001-5374-8248
Kai-Di HuInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.
Yi-Yun ChengPraexisio Taiwan Inc., New Taipei, 221425, Taiwan.
Sobha SahooInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.ORCID http://orcid.org/0000-0001-9273-341X
Lutimba StuartInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.
Chih-Wei ChenInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.
Yuan-Yu ChangInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.
Yu-Lin LuInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.ORCID http://orcid.org/0000-0002-7775-1801
Simai KeInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.ORCID http://orcid.org/0000-0002-6972-1012
Christopher Llynard D OrtizInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan.ORCID http://orcid.org/0000-0002-3114-7369
Bai-Shan FangCollege of Chemistry and Chemical Engineering, Xiamen University, 361005, Xiamen, China.
Chen-Chi WuDepartment of Otolaryngology, National Taiwan University Hospital, Taipei, 100225, Taiwan.ORCID http://orcid.org/0000-0002-5047-2204
Chung-Yu LanInstitute of Molecular and Cellular Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan. cylan@life.nthu.edu.tw.ORCID http://orcid.org/0000-0002-1533-3049
Hua-Wen FuInstitute of Molecular and Cellular Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan. hwfu@life.nthu.edu.tw.ORCID http://orcid.org/0000-0002-6346-2785
Lee-Wei YangInstitute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu, 300044, Taiwan. lwyang@life.nthu.edu.tw.ORCID http://orcid.org/0000-0002-3971-6386
National Tsing Hua University · TWAmazon (United States) · USNational Taiwan University · TWNational Taiwan University Hospital · TWUniversity of Pittsburgh · USXiamen University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The systematic design of functional peptides has technological and therapeutic applications. However, there is a need for pattern-based search engines that help locate desired functional motifs in primary sequences regardless of their evolutionary conservation. Existing databases such as The Protein Secondary Structure database (PSS) no longer serves the community, while the Dictionary of Protein Secondary Structure (DSSP) annotates the secondary structures when tertiary structures of proteins are provided. Here, we extract 1.7 million helices from the PDB and compile them into a database (Therapeutic Peptide Design database; TP-DB) that allows queries of compounded patterns to facilitate the identification of sequence motifs of helical structures. We show how TP-DB helps us identify a known purification-tag-specific antibody that can be repurposed into a diagnostic kit for Helicobacter pylori. We also show how the database can be used to design a new antimicrobial peptide that shows better Candida albicans clearance and lower hemolysis than its template homologs. Finally, we demonstrate how TP-DB can suggest point mutations in helical peptide blockers to prevent a targeted tumorigenic protein-protein interaction. TP-DB is made available at http://dyn.life.nthu.edu.tw/design/ .

Indexed as

SoftwareAmino AcidsAmino Acid SequenceAnimalsAntimicrobial PeptidesAntineoplastic AgentsDatabases, ProteinDrug DesignHumansMolecular Dynamics SimulationMutagenesis, Site-DirectedProtein BindingProtein Conformation, alpha-HelicalRecombinant ProteinsStructure-Activity RelationshipAmino AcidsAntimicrobial PeptidesAntineoplastic AgentsRecombinant Proteins

Identifiers

PMID35013238
PMCPMC8748493
OpenAlexW4205095214

What OpenQuestion holds

Textmetadata
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.