Evidence map›Paper›PMID 19857462›Full record

ArticleBiochemical and biophysical research communications2009

Identification of a novel nuclear localization signal and speckle-targeting sequence of tuftelin-interacting protein 11, a splicing factor involved in spliceosome disassembly.

Sissada Tannukit, Tara L Crabb, Klemens J Hertel, Xin Wen, David A Jans, Michael L Paine

Open access · greenAbstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed, 1 pooled it
0.5field-weighted citation impact, top 33% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.

  1. Pooled it
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  4. Review
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  7. Article
  8. Article
  9. DHX15 Is a Coreceptor for RLR Signaling That Promotes Antiviral Defense Against RNA Virus Infection.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2019
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  14. Unraveling the circadian clock in Arabidopsis.Plant signaling & behavior · 2013
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Sissada TannukitCenter for Craniofacial Molecular Biology, University of Southern California, 2250 Alcazar Street, CSA Rm103, Los Angeles, CA 90033-1004, USA.
Tara L Crabb
Klemens J Hertel
Xin Wen
David A Jans
Michael L Paine
University of Southern California · USUniversity of California, Irvine · USMonash University · AU

Funding

MECHANISMS OF ENHANCER DEPENDENT SPLICE SITE ACTIVATIONR01GM062287 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI HERTEL, KLEMENS J · 2001 to 2019
$4.8M
MOLECULAR MECHANISMS FOR EXTRACELLULAR PH CONTROL DURING AMELOGENESISR01DE019629 · NIDCR · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PAINE, MICHAEL LANSDELL · 2009 to 2014
$2.9M
TIP39KDA AND TOOTH FORMATIONR01DE014867 · NIDCR · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PAINE, MICHAEL LANSDELL · 2003 to 2007
$1.8M
NIDCR NIH HHS DE014867NIDCR NIH HHS R01 DE014867NIDCR NIH HHS R01 DE019629NIGMS NIH HHS GM062287NIGMS NIH HHS R01 GM062287
6 · The paper itself

Abstract

Tuftelin-interacting protein 11 (TFIP11) is a protein component of the spliceosome complex that promotes the release of the lariat-intron during late-stage splicing through a direct recruitment and interaction with DHX15/PRP43. Expression of TFIP11 is essential for cell and organismal survival. TFIP11 contains a G-patch domain, a signature motif of RNA-processing proteins that is responsible for TFIP11-DHX15 interactions. No other functional domains within TFIP11 have been described. TFIP11 is localized to distinct speckled regions within the cell nucleus, although excluded from the nucleolus. In this study sequential C-terminal deletions and mutational analyses have identified two novel protein elements in mouse TFIP11. The first domain covers amino acids 701-706 (VKDKFN) and is an atypical nuclear localization signal (NLS). The second domain is contained within amino acids 711-735 and defines TFIP11's distinct speckled nuclear localization. The identification of a novel TFIP11 nuclear speckle-targeting sequence (TFIP11-STS) suggests that this domain directly interacts with additional spliceosomal components. These data help define the mechanism of nuclear/nuclear speckle localization of the splicing factor TFIP11, with implications for it's function.

Indexed as

Amino Acid SequenceAnimalsCell LineCell NucleusHumansMiceMolecular Sequence DataNuclear Localization SignalsNuclear ProteinsProtein Structure, TertiaryRNA-Binding ProteinsRNA HelicasesRNA SplicingRNA Splicing FactorsSpliceosomesVesicular Transport ProteinsDhx15 protein, mouseNuclear Localization SignalsNuclear ProteinsRNA-Binding ProteinsRNA HelicasesRNA Splicing FactorsTFIP11 protein, humanTfip11 protein, mouseVesicular Transport Proteins

Identifiers

PMID19857462
PMCPMC2787706
OpenAlexW2150909798

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.