Evidence map›Paper›PMID 38557634›Full record

ArticleDatabase : the journal of biological databases and curation2024

ProNet DB: a proteome-wise database for protein surface property representations and RNA-binding profiles.

Junkang Wei, Jin Xiao, Siyuan Chen, Licheng Zong, Xin Gao, Yu Li

Open access · goldAbstract read
In one paragraph

Article in Database : the journal of biological databases and curation, 2024. 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
0.5field-weighted citation impact, top 38% 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, 2 citations in OpenAlex.

  1. Antibody-drug conjugate engineering: from design to efficacy and safety.Signal transduction and targeted therapy · 2026
    Review
  2. 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 3 institutions in 3 countries.

Junkang WeiDepartment of Computer Science and Engineering (CSE), The Chinese University of Hong Kong (CUHK), Chung Chi Rd, Ma Liu Shui, Hong Kong SAR 999077, China.ORCID 0000-0001-5666-2140
Jin XiaoDepartment of Computer Science and Engineering (CSE), The Chinese University of Hong Kong (CUHK), Chung Chi Rd, Ma Liu Shui, Hong Kong SAR 999077, China.
Siyuan ChenComputer Science Program, Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955, Kingdom of Saudi Arabia.ORCID 0000-0002-2382-2248
Licheng ZongDepartment of Computer Science and Engineering (CSE), The Chinese University of Hong Kong (CUHK), Chung Chi Rd, Ma Liu Shui, Hong Kong SAR 999077, China.ORCID 0000-0001-5418-005X
Xin GaoComputer Science Program, Computer, Electrical and Mathematical Sciences and Engineering (CEMSE) Division, King Abdullah University of Science and Technology (KAUST), Thuwal 23955, Kingdom of Saudi Arabia.ORCID 0000-0002-7108-3574
Yu LiDepartment of Computer Science and Engineering (CSE), The Chinese University of Hong Kong (CUHK), Chung Chi Rd, Ma Liu Shui, Hong Kong SAR 999077, China.ORCID 0000-0002-3664-6722
Chinese University of Hong Kong · HKKing Abdullah University of Science and Technology · SABroad Institute · US

Funding

Chinese University of Hong KongInnovation and Technology Commission of the Hong Kong Special Administrative RegionOffice of Research Administration at King Abdullah University of Science and TechnologyResearch Grants Council of the Hong Kong Special Administrative RegionRMGS in CUHK
6 · The paper itself

Abstract

The rapid growth in the number of experimental and predicted protein structures and more complicated protein structures poses a significant challenge for computational biology in leveraging structural information and accurate representation of protein surface properties. Recently, AlphaFold2 released the comprehensive proteomes of various species, and protein surface property representation plays a crucial role in protein-molecule interaction predictions, including those involving proteins, nucleic acids and compounds. Here, we proposed the first extensive database, namely ProNet DB, that integrates multiple protein surface representations and RNA-binding landscape for 326 175 protein structures. This collection encompasses the 16 model organism proteomes from the AlphaFold Protein Structure Database and experimentally validated structures from the Protein Data Bank. For each protein, ProNet DB provides access to the original protein structures along with the detailed surface property representations encompassing hydrophobicity, charge distribution and hydrogen bonding potential as well as interactive features such as the interacting face and RNA-binding sites and preferences. To facilitate an intuitive interpretation of these properties and the RNA-binding landscape, ProNet DB incorporates visualization tools like Mol* and an Online 3D Viewer, allowing for the direct observation and analysis of these representations on protein surfaces. The availability of pre-computed features enables instantaneous access for users, significantly advancing computational biology research in areas such as molecular mechanism elucidation, geometry-based drug discovery and the development of novel therapeutic approaches. Database URL:  https://proj.cse.cuhk.edu.hk/aihlab/pronet/.

Indexed as

ProteomeRNABinding SitesDatabases, ProteinMembrane ProteinsSurface PropertiesMembrane ProteinsProteomeRNA

Identifiers

PMID38557634
PMCPMC10984565
OpenAlexW4393394975

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.