ArticleBMC bioinformatics2007
UbiProt: a database of ubiquitylated proteins.
Article in BMC bioinformatics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 62 citations in OpenAlex.
- Precision Profiling of the Cardiovascular Post-Translationally Modified Proteome.Journal of cardiovascular development and disease · 2026Review
- An atlas of posttranslational modifications on RNA binding proteins.Nucleic acids research · 2022Article
- Mini-review: Recent advances in post-translational modification site prediction based on deep learning.Computational and structural biotechnology journal · 2022Review
- Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions.Journal of enzyme inhibition and medicinal chemistry · 2020Review
- Advances on Plant Ubiquitylome-From Mechanism to Application.International journal of molecular sciences · 2020Review
- iPTMnet: an integrated resource for protein post-translational modification network discovery.Nucleic acids research · 2018Article
- Investigation and identification of functional post-translational modification sites associated with drug binding and protein-protein interactions.BMC systems biology · 2017Article
- CIPPN: computational identification of protein pupylation sites by using neural network.Oncotarget · 2017Article
- Mapping Biological Networks from Quantitative Data-Independent Acquisition Mass Spectrometry: Data to Knowledge Pipelines.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Comprehensive database of human E3 ubiquitin ligases: application to aquaporin-2 regulation.Physiological genomics · 2016Article
- Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system.Nature communications · 2016Article
- dbPTM 2016: 10-year anniversary of a resource for post-translational modification of proteins.Nucleic acids research · 2016Article
- Regulation of translesion DNA synthesis: Posttranslational modification of lysine residues in key proteins.DNA repair · 2015Review
- Characterization and identification of ubiquitin conjugation sites with E3 ligase recognition specificities.BMC bioinformatics · 2015Article
- SysPTM 2.0: an updated systematic resource for post-translational modification.Database : the journal of biological databases and curation · 2014Article
- Article
- DbPTM 3.0: an informative resource for investigating substrate site specificity and functional association of protein post-translational modifications.Nucleic acids research · 2013Article
- SNObase, a database for S-nitrosation modification.Protein & cell · 2012Article
- E3Net: a system for exploring E3-mediated regulatory networks of cellular functions.Molecular & cellular proteomics : MCP · 2012Article
- PupDB: a database of pupylated proteins.BMC bioinformatics · 2012Article
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 at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPost-translational protein modification with ubiquitin, or ubiquitylation, is one of the hottest topics in a modern biology due to a dramatic impact on diverse metabolic pathways and involvement in pathogenesis of severe human diseases. A great number of eukaryotic proteins was found to be ubiquitylated. However, data about particular ubiquitylated proteins are rather disembodied. DESCRIPTION: To fill a general need for collecting and systematizing experimental data concerning ubiquitylation we have developed a new resource, UbiProt Database, a knowledge base of ubiquitylated proteins. The database contains retrievable information about overall characteristics of a particular protein, ubiquitylation features, related ubiquitylation and de-ubiquitylation machinery and literature references reflecting experimental evidence of ubiquitylation. UbiProt is available at http://ubiprot.org.ru for free.
conclusionUbiProt Database is a public resource offering comprehensive information on ubiquitylated proteins. The resource can serve as a general reference source both for researchers in ubiquitin field and those who deal with particular ubiquitylated proteins which are of their interest. Further development of the UbiProt Database is expected to be of common interest for research groups involved in studies of the ubiquitin system.
Indexed as
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.