ArticleNucleic acids research2003
The human Imp3 and Imp4 proteins form a ternary complex with hMpp10, which only interacts with the U3 snoRNA in 60-80S ribonucleoprotein complexes.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 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
55 citing papers in PubMed, 77 citations in OpenAlex.
- Detection of quantitative trait loci and genetic correlations of lipid reserves and production traits in aging laying hens.Poultry science · 2026Article
- RIBEX: predicting and explaining RNA binding across structured and intrinsically disordered regions (IDR)-rich proteins.Bioinformatics (Oxford, England) · 2026Article
- Mapping Spatiotemporal Metabolic Perturbations in Alloxan-Induced Diabetic Rat Kidneys Using Spatial Metabolomics and Proteomic Integration.Metabolites · 2026Article
- Article
- It Takes a Village of Chromatin Remodelers to Regulate rDNA Expression.International journal of molecular sciences · 2025Review
- Identification of Novel lncRNAs Related to Colorectal Cancer Through Bioinformatics Analysis.BioMed research international · 2025Article
- The RRP9-JUN axis promotes breast cancer progression via the AKT signalling pathway.Biology direct · 2024Article
- Article
- Ribosome biogenesis factors-from names to functions.The EMBO journal · 2023Review
- Mitochondrial DNA methylation is a predictor of immunotherapy response and prognosis in breast cancer: scRNA-seq and bulk-seq data insights.Frontiers in immunology · 2023Article
- ATRX proximal protein associations boast roles beyond histone deposition.PLoS genetics · 2021Article
- Article
- Smoking, DNA Methylation, and Breast Cancer: A Mendelian Randomization Study.Frontiers in oncology · 2021Article
- Loss of BRMS2 induces cell growth inhibition and translation capacity reduction in colorectal cancer cells.American journal of cancer research · 2021Article
- Ribosome Biogenesis in Plants: From Functional 45S Ribosomal DNA Organization to Ribosome Assembly Factors.The Plant cell · 2019Review
- Uncovering the assembly pathway of human ribosomes and its emerging links to disease.The EMBO journal · 2019Review
- Sas10 controls ribosome biogenesis by stabilizing Mpp10 and delivering the Mpp10-Imp3-Imp4 complex to nucleolus.Nucleic acids research · 2019Article
- Overexpression of a Brix Domain-Containing Ribosome Biogenesis Factor ARPF2 and its Interactor ARRS1 Causes Morphological Changes and Lifespan Extension inFrontiers in plant science · 2018Article
- Interaction network of the ribosome assembly machinery from a eukaryotic thermophile.Protein science : a publication of the Protein Society · 2017Article
- Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome.PloS one · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Ribosome biogenesis requires a vast number of trans-acting factors many of which are required for the chemical modification and processing of the pre-rRNA component. The U3 snoRNP complex is required for the early cleavage steps in pre-rRNA processing. We have cloned cDNAs encoding the human and mouse homologs of the yeast U3 snoRNP-associated proteins Imp3 and Imp4. Both human proteins localize to nucleoli and interact with the U3 snoRNA. The results of complementation experiments show that, in contrast to mouse Imp4, mouse Imp3 can partially alleviate the growth defect of the corresponding yeast null strain, indicating that the role of Imp3 in pre-rRNA processing is evolutionarily conserved. The results of density gradient centrifugation experiments show that, in contrast to hU3-55K, the human Imp3 and Imp4 proteins predominantly interact with the U3 snoRNA in 60-80S ribonucleoprotein complexes. In addition, we have found that hImp3, hImp4 and hMpp10 can form a stable hetero-trimeric complex in vitro, which is generated by direct interactions of both hImp3 and hImp4 with hMpp10. The analysis of hImp3 and hImp4 mutants indicated that their binding to hMpp10 correlates with their nucleolar accumulation, strongly suggesting that the formation of the ternary complex of hImp3, hImp4 and hMpp10 is required for their association with nucleolar components.
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.