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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Splicing factor proline/glutamine-rich

polypyrimidine tract-binding protein-associated splicing factor, PTB-associated splicing factor, SFPQ
Top mentioned proteins: non-O, PTB, fibrillin-1, CAN, ACID
Papers on polypyrimidine tract-binding protein-associated splicing factor
The proteomic profile of deleted in breast cancer 1 (DBC1) interactions points to a multi-faceted regulation of gene expression.
Cristea et al., Princeton, United States. In Mol Cell Proteomics, Jan 2016
Strikingly, we discovered that DBC1 associates with proteins that regulate the circadian cycle, including DDX5, DHX9, and SFPQ.
TRAP150 interacts with the RNA-binding domain of PSF and antagonizes splicing of numerous PSF-target genes in T cells.
Lynch et al., Philadelphia, United States. In Nucleic Acids Res, Nov 2015
PSF (a.k.a.
PSF/SFPQ is a very common gene fusion partner in TFE3 rearrangement-associated perivascular epithelioid cell tumors (PEComas) and melanotic Xp11 translocation renal cancers: clinicopathologic, immunohistochemical, and molecular characteristics suggesting classification as a distinct entity.
Zhou et al., Hefei, China. In Am J Surg Pathol, Sep 2015
PSF-TFE3 fusion genes were confirmed by reverse transcription polymerase chain reaction in cases (7/7) in which a novel PSF-TFE3 fusion point was identified.
Characterization of DNA binding and pairing activities associated with the native SFPQ·NONO DNA repair protein complex.
Dynan et al., Augusta, United States. In Biochem Biophys Res Commun, Sep 2015
We have previously shown that a complex of SFPQ (PSF) and NONO (p54(nrb)) cooperates with Ku protein at an early step of NHEJ, forming a committed preligation complex and stimulating end-joining activity by 10-fold or more.
PSF: nuclear busy-body or nuclear facilitator?
Lynch et al., Philadelphia, United States. In Wiley Interdiscip Rev Rna, Jul 2015
PTB-associated splicing factor (PSF) is an abundant and essential nucleic acid-binding protein that participates in a wide range of gene regulatory processes and cellular response pathways.
Dichotomy of Genetic Abnormalities in PEComas With Therapeutic Implications.
Antonescu et al., New York City, United States. In Am J Surg Pathol, Jun 2015
Combined RNA sequencing and fluorescence in situ hybridization analysis identified 9 (23%) TFE3 gene-rearranged tumors, with 3 cases showing an SFPQ/PSF-TFE3 fusion and 1 case showing a novel DVL2-TFE3 gene fusion.
PTB-associated splicing factor inhibits IGF-1-induced VEGF upregulation in a mouse model of oxygen-induced retinopathy.
Li et al., Tianjin, China. In Cell Tissue Res, May 2015
Here, we show that the polypyrimidine tract-binding protein-associated splicing factor (PSF) is a potential negative regulator of VEGF expression induced by IGF stimulation.
Arginine methylation and citrullination of splicing factor proline- and glutamine-rich (SFPQ/PSF) regulates its association with mRNA.
Dickman et al., Sheffield, United Kingdom. In Rna, Mar 2015
Splicing factor proline- and glutamine-rich (SFPQ) also commonly known as polypyrimidine tract-binding protein-associated-splicing factor (PSF) and its binding partner non-POU domain-containing octamer-binding protein (NONO/p54nrb), are highly abundant, multifunctional nuclear proteins.
The PTB-Associated Splicing Factor/Peroxisome Proliferator-Activated Receptor Gamma Axis Regulates Autophagosome Formation in Human Pancreatic Cancer Cells.
Matsuda et al., Nagasaki, Japan. In Biores Open Access, 2014
Our previous study suggested that PTB-associated splicing factor (PSF) is a PPARγ-interacting protein and growth regulator of colon cancer cells.
Molecular genetics and cellular features of TFE3 and TFEB fusion kidney cancers.
Linehan et al., Bethesda, United States. In Nat Rev Urol, 2014
The recently published findings of The Cancer Genome Atlas Network reported that five of the 416 surveyed clear cell RCC tumours (1.2%) harboured SFPQ-TFE3 fusions, providing further evidence for the importance of gene fusions.
Proteomic identification of PSF and p54(nrb) as TopBP1-interacting proteins.
Hänel et al., Jena, Germany. In J Cell Biochem, 2012
Localisation of TopBP1 at DNA damage sites was noticed as early as 5 s following damage induction, whereas p54(nrb) and PSF localised there after 20 s.
Human PSF concentrates DNA and stimulates duplex capture in DMC1-mediated homologous pairing.
Kurumizaka et al., Tokyo, Japan. In Nucleic Acids Res, 2012
The results suggested that PSF may function as an activator for the meiosis-specific recombinase DMC1.
Tau-mediated nuclear depletion and cytoplasmic accumulation of SFPQ in Alzheimer's and Pick's disease.
Götz et al., Sydney, Australia. In Plos One, 2011
In Alzheimer's disease, Pick's disease, and Frontotemporal Lobar Degeneration Tau-mediates nuclear depletion and cytoplasmic accumulation of SFPQ.
PSF controls expression of histone variants and cellular viability in thymocytes.
Lynch et al., Philadelphia, United States. In Biochem Biophys Res Commun, 2011
PSF contributes to the stability of a subset of histone genes and that loss of H2AE expression in the PSF-deficient thymocytes uniquely contributes to an increase in thymic apoptosis.
The splicing factor proline-glutamine rich (SFPQ/PSF) is involved in influenza virus transcription.
Ortín et al., Madrid, Spain. In Plos Pathog, 2011
results indicate that SFPQ/PSF is a host factor essential for influenza virus transcription that increases the efficiency of viral mRNA polyadenylation
A molecular mechanism for circadian clock negative feedback.
Weitz et al., Boston, United States. In Science, 2011
analysis indicates PSF within the PER complex recruits SIN3A, a scaffold for assembly of transcriptional inhibitory complexes, and the PER complex thereby rhythmically delivers histone deacetylases to the Per1 promoter, which repress Per1 transcription
ABL1 fusion genes in hematological malignancies: a review.
De Braekeleer et al., Brest, France. In Eur J Haematol, 2011
Both fusion genes (SFPQ-ABL1 and RCSD1-ABL1) characterized by a break in intron 4 of ABL1 are associated with B-cell ALL, as the chimeric proteins lacked the SH2 domain of ABL1.
Lamond et al., Australia. In Cold Spring Harb Perspect Biol, 2010
They are RNA-protein structures formed by the interaction between a long nonprotein-coding RNA species, NEAT1/Men epsilon/beta, and members of the DBHS (Drosophila Behavior Human Splicing) family of proteins: P54NRB/NONO, PSPC1, and PSF/SFPQ.
Hacking RNA: Hakai promotes tumorigenesis by enhancing the RNA-binding function of PSF.
Gorospe et al., A Coruña, Spain. In Cell Cycle, 2009
Recently, Hakai was also found to interact with PSF (PTB-associated splicing factor).
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