ArticleBMC research notes2009
A comprehensive resource for integrating and displaying protein post-translational modifications.
Article in BMC research notes, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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.
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.
Who cites it
33 citing papers in PubMed.
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- Considerations on Structural Vaccinology and Epitope Screening of Calcium-Dependent Protein Kinases 8 as a Potential Vaccine Target AgainstInterdisciplinary perspectives on infectious diseases · 2025Article
- Sialic Acid-Binding Protein-1 (SABP1) ofJournal of parasitology research · 2025Article
- In silico evaluation of Toxoplasma gondii rhoptry neck proteins (TgRONs) for potential immunogenic epitopes.EXCLI journal · 2025Article
- In Silico-Based Investigation of the Immunogenicity and Biochemical Attributes ofJournal of parasitology research · 2025Article
- Article
- PreliminaryRecent advances in inflammation & allergy drug discovery · 2025Article
- KinPred-RNA-kinase activity inference and cancer type classification using machine learning on RNA-seq data.iScience · 2024Article
- In Silico Analysis of the ROP29 Protein as a Vaccine Candidate AgainstJournal of parasitology research · 2024Article
- CHDbase: A Comprehensive Knowledgebase for Congenital Heart Disease-related Genes and Clinical Manifestations.Genomics, proteomics & bioinformatics · 2023Article
- Current status of PTMs structural databases: applications, limitations and prospects.Amino acids · 2022Review
- Incorporating support vector machine with sequential minimal optimization to identify anticancer peptides.BMC bioinformatics · 2021Article
- A large-scale investigation and identification of methicillin-resistant Staphylococcus aureus based on peaks binning of matrix-assisted laser desorption ionization-time of flight MS spectra.Briefings in bioinformatics · 2021Article
- Bioinformatics analysis of calcium-dependent protein kinase 4 (CDPK4) as Toxoplasma gondii vaccine target.BMC research notes · 2021Article
- Immunoinformatic Analysis of Calcium-Dependent Protein Kinase 7 (CDPK7) Showed Potential Targets forJournal of parasitology research · 2021Article
- Immunoinformatic analysis of immunogenic B- and T-cell epitopes of MIC4 protein to designing a vaccine candidate againstClinical and experimental vaccine research · 2021Article
- Article
- Antigenic properties of dense granule antigen 12 protein using bioinformatics tools in order to improve vaccine design againstClinical and experimental vaccine research · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundProtein Post-Translational Modification (PTM) plays an essential role in cellular control mechanisms that adjust protein physical and chemical properties, folding, conformation, stability and activity, thus also altering protein function.
findingsdbPTM (version 1.0), which was developed previously, aimed on a comprehensive collection of protein post-translational modifications. In this update version (dbPTM2.0), we developed a PTM database towards an expert system of protein post-translational modifications. The database comprehensively collects experimental and predictive protein PTM sites. In addition, dbPTM2.0 was extended to a knowledge base comprising the modified sites, solvent accessibility of substrate, protein secondary and tertiary structures, protein domains, protein intrinsic disorder region, and protein variations. Moreover, this work compiles a benchmark to construct evaluation datasets for computational study to identifying PTM sites, such as phosphorylated sites, glycosylated sites, acetylated sites and methylated sites.
conclusionThe current release not only provides the sequence-based information, but also annotates the structure-based information for protein post-translational modification. The interface is also designed to facilitate the access to the resource. This effective database is now freely accessible at http://dbPTM.mbc.nctu.edu.tw/.
Identifiers
What OpenQuestion holds
Registered trials
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.