ReviewACS chemical biology2015
Structural basis for regulation of RNA-binding proteins by phosphorylation.
Review in ACS chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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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
30 citing papers in PubMed, 65 citations in OpenAlex.
- Impact of Gemin5 in protein synthesis: phosphoresidues of the dimerization domain regulate ribosome binding.RNA biology · 2025Article
- SARS-CoV-2 RNA-binding protein suppresses extracellular miRNA release.RNA biology · 2025Article
- Arginine demethylation of Serine/Arginine-rich splicing factor 1 enhances miRNA enrichment in small extracellular vesicles derived from pancreatic ductal adenocarcinoma cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Alternative Splicing in the Heart: The Therapeutic Potential of Regulating the Regulators.International journal of molecular sciences · 2024Review
- Article
- Phosphorylation of the compartmentalized PKA substrate TAF15 regulates RNA-protein interactions.Cellular and molecular life sciences : CMLS · 2024Article
- A cyclin D1 intrinsically disordered domain accesses modified histone motifs to govern gene transcription.Oncogenesis · 2024Article
- Development and Applications of Chimera Platforms for Tyrosine Phosphorylation.ACS central science · 2023Article
- Uridylation of the histone mRNA stem-loop weakens binding interactions with SLBP while maintaining interactions with 3'hExo.RNA biology · 2023Article
- Cdk1-mediated threonine phosphorylation of Sam68 modulates its RNA binding, alternative splicing activity and cellular functions.Nucleic acids research · 2022Article
- Phosphorylation of the smooth muscle master splicing regulator RBPMS regulates its splicing activity.Nucleic acids research · 2022Article
- mMolecules and cells · 2022Review
- Interplay between A-to-I Editing and Splicing of RNA: A Potential Point of Application for Cancer Therapy.International journal of molecular sciences · 2022Review
- An atlas of posttranslational modifications on RNA binding proteins.Nucleic acids research · 2022Article
- Targeting transcription cycles in cancer.Nature reviews. Cancer · 2022Review
- Stem-loop binding protein and metal carcinogenesis.Seminars in cancer biology · 2021Review
- Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases.Life (Basel, Switzerland) · 2021Review
- Identification of Nrl1 Domains Responsible for Interactions with RNA-Processing Factors and Regulation of Nrl1 Function by Phosphorylation.International journal of molecular sciences · 2021Article
- Systematic Identification of Protein Phosphorylation-Mediated Interactions.Journal of proteome research · 2021Article
- Opportunities and Challenges in Global Quantification of RNA-Protein InteractionFrontiers in molecular biosciences · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Ribonucleoprotein complexes involved in pre-mRNA splicing and mRNA decay are often regulated by phosphorylation of RNA-binding proteins. Cells use phosphorylation-dependent signaling pathways to turn on and off gene expression. Not much is known about how phosphorylation-dependent signals transmitted by exogenous factors or cell cycle checkpoints regulate RNA-mediated gene expression at the atomic level. Several human diseases are linked to an altered phosphorylation state of an RNA binding protein. Understanding the structural response to the phosphorylation "signal" and its effect on ribonucleoprotein assembly provides mechanistic understanding, as well as new information for the design of novel drugs. In this review, I highlight recent structural studies that reveal the mechanisms by which phosphorylation can regulate protein-protein and protein-RNA interactions in ribonucleoprotein complexes.
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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.