ReviewBrain research2016
Immunoprecipitation and mass spectrometry defines an extensive RBM45 protein-protein interaction network.
Review in Brain research, 2016. 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
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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
33 citing papers in PubMed, 70 citations in OpenAlex.
- Multi-omics-driven precision medicine.iMeta · 2026Review
- RBM45 Preferential Binding to mThe journal of physical chemistry. B · 2026Article
- RBM45 reprograms lipid metabolism promoting hepatocellular carcinoma via Rictor and ACSL1/ACSL4.Oncogene · 2024Article
- The Influence of Lipid Microdomain Heterogeneity on Protein-Protein Interactions: Proteomic Analysis of Co-Immunoprecipitated Binding Partners of P450 1A2 and P450 3A in Rat Liver Microsomes.Drug metabolism and disposition: the biological fate of chemicals · 2023Article
- Emerging Trends in the Field of Inflammation and Proteinopathy in ALS/FTD Spectrum Disorder.Biomedicines · 2023Review
- Syndecan-4 Mediates the Cellular Entry of Adeno-Associated Virus 9.International journal of molecular sciences · 2023Article
- G Protein-Coupled Receptor 37L1 Modulates Epigenetic Changes in Human Renal Proximal Tubule Cells.International journal of molecular sciences · 2022Article
- RBM45 is an mCell reports · 2022Article
- Editorial: New challenges and future perspectives in neurodegeneration.Frontiers in neuroscience · 2022Article
- Nuclear translocation of vitellogenin in the honey bee (Apidologie · 2022Article
- Defining the Caprin-1 Interactome in Unstressed and Stressed Conditions.Journal of proteome research · 2021Article
- Structural basis for RNA recognition by the N-terminal tandem RRM domains of human RBM45.Nucleic acids research · 2021Article
- Isolating and Analyzing Protein Containing Granules from Cells.Current protocols · 2021Article
- Protein Interaction Network Biology in Neuroscience.Proteomics · 2021Review
- Matrin 3 in neuromuscular disease: physiology and pathophysiology.JCI insight · 2021Review
- Intron retention is a robust marker of intertumoral heterogeneity in pancreatic ductal adenocarcinoma.NPJ genomic medicine · 2020Article
- Plasmodium falciparum DDX55 is a nucleocytoplasmic protein and a 3'-5' direction-specific DNA helicase.Protoplasma · 2020Article
- RBM45 associates with nuclear stress bodies and forms nuclear inclusions during chronic cellular stress and in neurodegenerative diseases.Acta neuropathologica communications · 2020Article
- Eukaryotic expression, Co-IP and MS identify BMPR-1B protein-protein interaction network.Biological research · 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
9 authors at 2 institutions in 1 country.
Funding
Abstract
The pathological accumulation of RNA-binding proteins (RBPs) within inclusion bodies is a hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). RBP aggregation results in both toxic gain and loss of normal function. Determining the protein binding partners and normal functions of disease-associated RBPs is necessary to fully understand molecular mechanisms of RBPs in disease. Herein, we characterized the protein-protein interactions (PPIs) of RBM45, a RBP that localizes to inclusions in ALS/FTLD. Using immunoprecipitation coupled to mass spectrometry (IP-MS), we identified 132 proteins that specifically interact with RBM45 within HEK293 cells. Select PPIs were validated by immunoblot and immunocytochemistry, demonstrating that RBM45 associates with a number of other RBPs primarily via RNA-dependent interactions in the nucleus. Analysis of the biological processes and pathways associated with RBM45-interacting proteins indicates enrichment for nuclear RNA processing/splicing via association with hnRNP proteins and cytoplasmic RNA translation via eiF2 and eiF4 pathways. Moreover, several other ALS-linked RBPs, including TDP-43, FUS, Matrin-3, and hnRNP-A1, interact with RBM45, consistent with prior observations of these proteins within intracellular inclusions in ALS/FTLD. Taken together, our results define a PPI network for RBM45, suggest novel functions for this protein, and provide new insights into the contributions of RBM45 to neurodegeneration in ALS/FTLD. This article is part of a Special Issue entitled SI:RNA Metabolism in Disease.
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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.