Evidence map›Paper›PMID 39192607›Full record

ArticleDatabase : the journal of biological databases and curation2024

Autoinhibited Protein Database: a curated database of autoinhibitory domains and their autoinhibition mechanisms.

Daeahn Cho, Hyang-Mi Lee, Ji Ah Kim, Jae Gwang Song, Su-Hee Hwang, Bomi Lee, Jinsil Park, Kha Mong Tran, Jiwon Kim, Phuong Ngoc Lam Vo and 6 more

Abstract 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
–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

2 citing papers in PubMed.

  1. Article
  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

16 authors.

Daeahn ChoDepartment of Biomedical Engineering, Chung-Ang University, Seoul 06974, South Korea.ORCID 0009-0001-7229-3952
Hyang-Mi LeeDepartment of Biomedical Engineering, Chung-Ang University, Seoul 06974, South Korea.
Ji Ah KimDepartment of Biomedical Engineering, Chung-Ang University, Seoul 06974, South Korea.
Jae Gwang SongDepartment of Bio-integrated Science and Technology, College of Life Sciences, Sejong University, Seoul 05006, Republic of Korea.
Su-Hee HwangDepartment of Biomedical Engineering, Chung-Ang University, Seoul 06974, South Korea.
Bomi LeeDepartment of Bio-integrated Science and Technology, College of Life Sciences, Sejong University, Seoul 05006, Republic of Korea.
Jinsil ParkDepartment of Bio-integrated Science and Technology, College of Life Sciences, Sejong University, Seoul 05006, Republic of Korea.
Kha Mong TranDepartment of Biomedical Engineering, Chung-Ang University, Seoul 06974, South Korea.
Jiwon KimDepartment of Bio-integrated Science and Technology, College of Life Sciences, Sejong University, Seoul 05006, Republic of Korea.
Phuong Ngoc Lam VoDepartment of Biomedical Engineering, Chung-Ang University, Seoul 06974, South Korea.
Jooeun BaeDepartment of Bio-integrated Science and Technology, College of Life Sciences, Sejong University, Seoul 05006, Republic of Korea.
Teerapat PimtDepartment of Biomedical Engineering, Chung-Ang University, Seoul 06974, South Korea.
Kangseok LeeDepartment of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea.
Jörg GsponerCenter for High-Throughput Biology, University of British Columbia, 2125 East Mall, Vancouver, BC V6T 1Z4, Canada.ORCID 0000-0003-3672-6594
Hyung Wook KimDepartment of Bio-integrated Science and Technology, College of Life Sciences, Sejong University, Seoul 05006, Republic of Korea.
Dokyun NaDepartment of Biomedical Engineering, Chung-Ang University, Seoul 06974, South Korea.ORCID 0000-0002-9107-7040

Funding

National Research Foundation of Korea (NRF) 2018R1A5A1025077 2021R1I1A1A01056588 2022M3A9B6082687
6 · The paper itself

Abstract

Autoinhibition, a crucial allosteric self-regulation mechanism in cell signaling, ensures signal propagation exclusively in the presence of specific molecular inputs. The heightened focus on autoinhibited proteins stems from their implication in human diseases, positioning them as potential causal factors or therapeutic targets. However, the absence of a comprehensive knowledgebase impedes a thorough understanding of their roles and applications in drug discovery. Addressing this gap, we introduce Autoinhibited Protein Database (AiPD), a curated database standardizing information on autoinhibited proteins. AiPD encompasses details on autoinhibitory domains (AIDs), their targets, regulatory mechanisms, experimental validation methods, and implications in diseases, including associated mutations and post-translational modifications. AiPD comprises 698 AIDs from 532 experimentally characterized autoinhibited proteins and 2695 AIDs from their 2096 homologs, which were retrieved from 864 published articles. AiPD also includes 42 520 AIDs of computationally predicted autoinhibited proteins. In addition, AiPD facilitates users in investigating potential AIDs within a query sequence through comparisons with documented autoinhibited proteins. As the inaugural autoinhibited protein repository, AiPD significantly aids researchers studying autoinhibition mechanisms and their alterations in human diseases. It is equally valuable for developing computational models, analyzing allosteric protein regulation, predicting new drug targets, and understanding intervention mechanisms AiPD serves as a valuable resource for diverse researchers, contributing to the understanding and manipulation of autoinhibition in cellular processes. Database URL: http://ssbio.cau.ac.kr/databases/AiPD.

Indexed as

Databases, ProteinData CurationHumansProtein DomainsProteinsProteins

Identifiers

PMID39192607
PMCPMC11349611

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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.