ArticleRNA (New York, N.Y.)2014
The prolyl isomerase, FKBP25, interacts with RNA-engaged nucleolin and the pre-60S ribosomal subunit.
Article in RNA (New York, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 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
20 citing papers in PubMed, 41 citations in OpenAlex.
- Genetic validation ofeLife · 2023Article
- Cyclophilin anaCyp40 regulates photosystem assembly and phycobilisome association in a cyanobacterium.Nature communications · 2022Article
- Article
- FKBP25 Regulates Meiotic Apparatus During Mouse Oocyte Maturation.Frontiers in cell and developmental biology · 2021Article
- FKBP25 participates in DNA double-strand break repair.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2020Article
- Ligand-induced disorder-to-order transitions characterized by structural proteomics and molecular dynamics simulations.Journal of proteomics · 2020Article
- Histone Chaperone Paralogs Have Redundant, Cooperative, and Divergent Functions in Yeast.Genetics · 2019Article
- The anti-tumor diterpene oridonin is a direct inhibitor of Nucleolin in cancer cells.Scientific reports · 2018Article
- The prolyl isomerase FKBP25 regulates microtubule polymerization impacting cell cycle progression and genomic stability.Nucleic acids research · 2018Article
- Canonical and Noncanonical Actions of Arabidopsis Histone Deacetylases in Ribosomal RNA Processing.The Plant cell · 2018Article
- The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module.Nucleic acids research · 2017Article
- Solving protein structures using short-distance cross-linking constraints as a guide for discrete molecular dynamics simulations.Science advances · 2017Article
- Basic surface features of nuclear FKBPs facilitate chromatin binding.Scientific reports · 2017Article
- FKBP12 enhances sensitivity to chemotherapy-induced cancer cell apoptosis by inhibiting MDM2.Oncogene · 2017Article
- Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin.Nucleic acids research · 2016Article
- Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506.Protein science : a publication of the Protein Society · 2016Article
- LARP6 Meets Collagen mRNA: Specific Regulation of Type I Collagen Expression.International journal of molecular sciences · 2016Review
- Prolyl isomerases in gene transcription.Biochimica et biophysica acta · 2015Review
- Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.Biomolecules · 2015Review
- Cyclophilin J is a novel peptidyl-prolyl isomerase and target for repressing the growth of hepatocellular carcinoma.PloS one · 2015Article
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
No grant is acknowledged in the PubMed record.
Abstract
Peptidyl-proline isomerases of the FK506-binding protein (FKBP) family belong to a class of enzymes that catalyze the cis-trans isomerization of prolyl-peptide bonds in proteins. A handful of FKBPs are found in the nucleus, implying that the isomerization of proline in nuclear proteins is enzymatically controlled. FKBP25 is a nuclear protein that has been shown to associate with chromatin modifiers and transcription factors. In this study, we performed the first proteomic characterization of FKBP25 and found that it interacts with numerous ribosomal proteins, ribosomal processing factors, and a small selection of chromatin modifiers. In agreement with previous reports, we found that nucleolin is a major FKBP25-interacting protein and demonstrated that this interaction is dependent on rRNA. FKBP25 interacts with the immature large ribosomal subunit in nuclear extract but does not associate with mature ribosomes, implicating this FKBP's action in ribosome biogenesis. Despite engaging nascent 60S ribosomes, FKBP25 does not affect steady-state levels of rRNAs or its pre-rRNA intermediates. We conclude that FKBP25 is likely recruited to preribosomes to chaperone one of the protein components of the ribosome large subunit.
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.