ArticleG3 (Bethesda, Md.)2019
iProteinDB: An Integrative Database of
Article in G3 (Bethesda, Md.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed.
- Proteome-wide prediction of the functional impact of missense variants with ProteoCast.Nature communications · 2026Article
- Diverse oncogenes use common mechanisms to drive growth of major forms of human cancer.Science advances · 2025Article
- An integrative systems-biology approach defines mechanisms of Alzheimer's disease neurodegeneration.Nature communications · 2025Article
- Cross-Species Epitope Sequence Analysis for Discovery of Existing Antibodies Useful for Phospho-Specific Protein Detection in Model Species.International journal of molecular sciences · 2025Article
- FlyRNAi.org 2025 update-expanded resources for new technologies and species.Nucleic acids research · 2025Article
- CESA: Cross-species Epitope Sequence Analysis for discovery of existing antibodies useful for phospho-specific protein detection in model species.bioRxiv : the preprint server for biology · 2024Article
- An image-based RNAi screen identifies the EGFR signaling pathway as a regulator of Imp RNP granules.Journal of cell science · 2024Article
- A force-sensitive mutation reveals a non-canonical role for dynein in anaphase progression.The Journal of cell biology · 2024Article
- Regulation of centrosome size by the cell-cycle oscillator in Drosophila embryos.The EMBO journal · 2024Article
- Article
- An AMPK phosphoregulated RhoGEF feedback loop tunes cortical flow-driven amoeboid migration in vivo.Science advances · 2022Article
- SUMOylation of Dorsal attenuates Toll/NF-κB signaling.Genetics · 2022Article
- Extended disordered regions of ribosome-associated NAC proteins paralogs belong only to the germline in Drosophila melanogaster.Scientific reports · 2022Article
- The phospho-docking protein 14-3-3 regulates microtubule-associated proteins in oocytes including the chromosomal passenger Borealin.PLoS genetics · 2022Article
- Article
- FlyRNAi.org-the database of the Drosophila RNAi screening center and transgenic RNAi project: 2021 update.Nucleic acids research · 2021Article
- Phosphoinositide Recognition Sites Are Blocked by Metabolite Attachment.Frontiers in cell and developmental biology · 2021Article
- STRIPAK regulates Slik localization to control mitotic morphogenesis and epithelial integrity.The Journal of cell biology · 2020Article
- Post-translational modifications of Drosophila melanogaster HOX protein, Sex combs reduced.PloS one · 2020Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors.
Funding
Abstract
Post-translational modification (PTM) serves as a regulatory mechanism for protein function, influencing their stability, interactions, activity and localization, and is critical in many signaling pathways. The best characterized PTM is phosphorylation, whereby a phosphate is added to an acceptor residue, most commonly serine, threonine and tyrosine in metazoans. As proteins are often phosphorylated at multiple sites, identifying those sites that are important for function is a challenging problem. Considering that any given phosphorylation site might be non-functional, prioritizing evolutionarily conserved phosphosites provides a general strategy to identify the putative functional sites. To facilitate the identification of conserved phosphosites, we generated a large-scale phosphoproteomics dataset from
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.