Evidence map›Paper›PMID 32413515›Full record

ArticleGenomics, proteomics & bioinformatics2020

Procleave: Predicting Protease-specific Substrate Cleavage Sites by Combining Sequence and Structural Information.

Fuyi Li, Andre Leier, Quanzhong Liu, Yanan Wang, Dongxu Xiang, Tatsuya Akutsu, Geoffrey I Webb, A Ian Smith, Tatiana Marquez-Lago, Jian Li and 1 more

Open access · goldAbstract readEvaluation Study
In one paragraph

Article in Genomics, proteomics & bioinformatics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed, 1 pooled it
6.1field-weighted citation impact, top 3% 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

71 citing papers in PubMed, 1 synthesis or guideline pooled it, 145 citations in OpenAlex.

  1. Pooled it
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  6. The rise and future of peptide-based antimicrobials.Journal of microbiology (Seoul, Korea) · 2026
    Review
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  19. Investigating Protein-Protein Interactions of Autophagy-Involved TNIP1.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  20. Article

11 more citing papers are in PubMed but not listed here.

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

11 authors at 5 institutions in 4 countries.

Fuyi LiBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC 3800, Australia; Monash Centre for Data Science, Faculty of Information Technology, Monash University, Melbourne, VIC 3800, Australia.
Andre LeierSchool of Medicine, University of Alabama at Birmingham, Birmingham, AL 35233, USA.
Quanzhong LiuCollege of Information Engineering, Northwest A&F University, Yangling 712100, China.
Yanan WangBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC 3800, Australia; Monash Centre for Data Science, Faculty of Information Technology, Monash University, Melbourne, VIC 3800, Australia.
Dongxu XiangBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC 3800, Australia; College of Information Engineering, Northwest A&F University, Yangling 712100, China.
Tatsuya AkutsuBioinformatics Center, Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
Geoffrey I WebbMonash Centre for Data Science, Faculty of Information Technology, Monash University, Melbourne, VIC 3800, Australia.
A Ian SmithBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC 3800, Australia; ARC Centre of Excellence in Advanced Molecular Imaging, Monash University, Melbourne, VIC 3800, Australia.
Tatiana Marquez-LagoSchool of Medicine, University of Alabama at Birmingham, Birmingham, AL 35233, USA. Electronic address: tmarquezlago@uabmc.edu.
Jian LiBiomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC 3800, Australia. Electronic address: Jian.Li@monash.edu.
Jiangning SongBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC 3800, Australia; Monash Centre for Data Science, Faculty of Information Technology, Monash University, Melbourne, VIC 3800, Australia; ARC Centre of Excellence in Advanced Molecular Imaging, Monash University, Melbourne, VIC 3800, Australia. Electronic address: Jiangning.Song@monash.edu.
Australian Regenerative Medicine Institute · AUUniversity of Alabama at Birmingham · USKyoto University · JPMonash University · AUNorthwest A&F University · CN

Funding

New Tricks for 'Old' Drugs: PK/PD of Polymyxin Nonantibiotic CombinationsR01AI111965 · NIAID · MONASH UNIVERSITY · PI LI, JIAN · 2014 to 2018
$4.3M
NIAID NIH HHS R01 AI111965
6 · The paper itself

Abstract

Proteases are enzymes that cleave and hydrolyse the peptide bonds between two specific amino acid residues of target substrate proteins. Protease-controlled proteolysis plays a key role in the degradation and recycling of proteins, which is essential for various physiological processes. Thus, solving the substrate identification problem will have important implications for the precise understanding of functions and physiological roles of proteases, as well as for therapeutic target identification and pharmaceutical applicability. Consequently, there is a great demand for bioinformatics methods that can predict novel substrate cleavage events with high accuracy by utilizing both sequence and structural information. In this study, we present Procleave, a novel bioinformatics approach for predicting protease-specific substrates and specific cleavage sites by taking into account both their sequence and 3D structural information. Structural features of known cleavage sites were represented by discrete values using a LOWESS data-smoothing optimization method, which turned out to be critical for the performance of Procleave. The optimal approximations of all structural parameter values were encoded in a conditional random field (CRF) computational framework, alongside sequence and chemical group-based features. Here, we demonstrate the outstanding performance of Procleave through extensive benchmarking and independent tests. Procleave is capable of correctly identifying most cleavage sites in the case study. Importantly, when applied to the human structural proteome encompassing 17,628 protein structures, Procleave suggests a number of potential novel target substrates and their corresponding cleavage sites of different proteases. Procleave is implemented as a webserver and is freely accessible at http://procleave.erc.monash.edu/.

Indexed as

SoftwareAlgorithmsBenchmarkingCatalytic DomainComputational BiologyHumansPeptide HydrolasesProtein ConformationProteolysisProteomeStructure-Activity RelationshipSubstrate SpecificityPeptide HydrolasesProteomeCleavage site predictionConditional random fieldMachine learningProteaseStructural determinants

Identifiers

PMID32413515
PMCPMC7393547
OpenAlexW3024086681

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.