ArticleCellular and molecular life sciences : CMLS2005
Structural organization and cellular localization of tuftelin-interacting protein 11 (TFIP11).
Article in Cellular and molecular life sciences : CMLS, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- G-patch proteins: important regulators of pre-mRNA splicing and ribosome biogenesis.Frontiers in cell and developmental biology · 2026Review
- TFIP11 promotes replication fork reversal to preserve genome stability.Nature communications · 2024Article
- Comparative Analysis of Saliva and Plasma Proteins Patterns in Pregnant Cows-Preliminary Studies.Animals : an open access journal from MDPI · 2022Article
- Drosophila septin interacting protein 1 regulates neurogenesis in the early developing larval brain.Scientific reports · 2022Article
- Evolutionary Analysis of the Mammalian Tuftelin Sequence Reveals Features of Functional Importance.Journal of molecular evolution · 2017Article
- Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways.RNA biology · 2016Article
- STIP overexpression confers oncogenic potential to human non-small cell lung cancer cells by regulating cell cycle and apoptosis.Journal of cellular and molecular medicine · 2015Article
- STIP is a critical nuclear scaffolding protein linking USP7 to p53-Mdm2 pathway regulation.Oncotarget · 2015Article
- NTR1 is required for transcription elongation checkpoints at alternative exons in Arabidopsis.The EMBO journal · 2015Article
- Genes expressed in dental enamel development are associated with molar-incisor hypomineralization.Archives of oral biology · 2013Article
- Nuclear protein IK undergoes dynamic subcellular translocation and forms unique nuclear bodies during the cell cycle.Biomarker research · 2013Article
- Identification of a pH-responsive DNA region upstream of the transcription start site of human NBCe1-B.European journal of oral sciences · 2011Article
- Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly.Biochemical and biophysical research communications · 2009Article
- Differential protein expression in Spirometra erinacei according to its development in its final host.Parasitology research · 2009Article
- Differential gene expression in the perichondrium and cartilage of the neonatal mouse temporomandibular joint.Orthodontics & craniofacial research · 2009Article
- TFIP11 interacts with mDEAH9, an RNA helicase involved in spliceosome disassembly.International journal of molecular sciences · 2008Article
- Biomimetic systems for hydroxyapatite mineralization inspired by bone and enamel.Chemical reviews · 2008Review
- TFIP11, CCNL1 and EWSR1 Protein-protein Interactions, and Their Nuclear Localization.International journal of molecular sciences · 2008Article
- Spliceosomal small nuclear ribonucleoprotein particles repeatedly cycle through Cajal bodies.Molecular biology of the cell · 2008Article
- TRIM5 alpha cytoplasmic bodies are highly dynamic structures.Molecular biology of the cell · 2007Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Tuftelin-interacting protein (TFIP11) was first identified in a yeast two-hybrid screening as a protein interacting with tuftelin. The ubiquitous expression of TFIP11 suggested that it might have other functions in non-dental tissues. TFIP11 contains a G-patch, a protein domain believed to be involved in RNA binding. Using a green fluorescence protein tag, TFIP11 was found to locate in a novel subnuclear structure that we refer to as the TFIP body. An in vivo splicing assay demonstrated that TFIP11 is a novel splicing factor. TFIP11 diffuses from the TFIP body following RNase A treatment, suggesting that the retention of TFIP11 is RNA dependent. RNA polymerase II inhibitor (-amanitin and actinomycin D) treatment causes enlargement in size and decrease in number of TFIP bodies, suggesting that TFIP bodies perform a storage function rather than an active splicing function. The TFIP body may therefore represent a new subnuclear storage compartment for splicing components.
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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.