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Polypyrimidine tract binding protein 1

PTB, Heterogeneous-Nuclear Ribonucleoprotein, Polypyrimidine Tract-Binding Protein
This gene belongs to the subfamily of ubiquitously expressed heterogeneous nuclear ribonucleoproteins (hnRNPs). The hnRNPs are RNA-binding proteins and they complex with heterogeneous nuclear RNA (hnRNA). These proteins are associated with pre-mRNAs in the nucleus and appear to influence pre-mRNA processing and other aspects of mRNA metabolism and transport. While all of the hnRNPs are present in the nucleus, some seem to shuttle between the nucleus and the cytoplasm. The hnRNP proteins have distinct nucleic acid binding properties. The protein encoded by this gene has four repeats of quasi-RNA recognition motif (RRM) domains that bind RNAs. This protein binds to the intronic polypyrimidine tracts that requires pre-mRNA splicing and acts via the protein degradation ubiquitin-proteasome pathway. It may also promote the binding of U2 snRNP to pre-mRNAs. This protein is localized in the nucleoplasm and it is also detected in the perinucleolar structure. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, HAD, V1a, ACID, AGE
Papers using PTB antibodies
Cleavage Map and Proteolytic Processing of the Murine Norovirus Nonstructural Polyprotein in Infected Cells.
Supplier
Ryu Wang-Shick, In PLoS ONE, 2005
... Antisera for western blot to hnRNP I (PTB) was purchased from Santa Cruz Biotechnology, mouse monoclonal antibodies to ...
Autoregulation of polypyrimidine tract binding protein by alternative splicing leading to nonsense-mediated decay
Supplier
Tarn Woan-Yuh et al., In The Journal of Cell Biology, 2003
... The His-tagged PTB expression vector was constructed by cloning the human PTB-coding region into pET-32a (QIAGEN).
Papers on PTB
The effects of SP110's associated genes on fresh cavitary pulmonary tuberculosis in Han Chinese population.
New
Deng et al., Shanghai, China. In Clin Exp Med, 23 Feb 2015
To investigate the effects of SP110 and its associated genes, i.e., MYBBP1A and RELA, on pathological progression of MTB infection, an association study with 424 patients of fresh pulmonary tuberculosis (PTB) and 424 healthy controls was performed.
Can microRNA profiling in maternal blood identify women at risk for preterm birth?
New
Brown et al., Philadelphia, United States. In Am J Obstet Gynecol, 21 Feb 2015
The objective of this study was to determine if miRNA profiles in maternal blood are different in women destined to have a preterm birth (PTB) compared to term.
Nuclear matrix protein Matrin3 regulates alternative splicing and forms overlapping regulatory networks with PTB.
New
Smith et al., San Carlos de Bariloche, Argentina. In Embo J, 19 Feb 2015
We identified Matrin3 by its interaction with the second RRM domain of the splicing regulator PTB.
Rhythmic Control of mRNA Stability Modulates Circadian Amplitude of Mouse Period3 mRNA.
New
Kim et al., South Korea. In J Neurochem, 10 Feb 2015
In this study, we identify three proteins - heterogeneous nuclear ribonucleoprotein (hnRNP) K, polypyrimidine tract-binding protein (PTB), and hnRNP D - that bind to mPer3 mRNA 3'-UTR.
A novel Pro197Glu substitution in acetolactate synthase (ALS) confers broad-spectrum resistance across ALS inhibitors.
New
Wang et al., Tai'an, China. In Pestic Biochem Physiol, 31 Jan 2015
A whole-plant experiment showed that the WRR04 population exhibited broad-spectrum resistance to tribenuron (SU, 318-fold), pyrithiobac sodium (PTB, > 197-fold), pyroxsulam (TP, 81-fold), florasulam (TP, > 36-fold) and imazethapyr (IMI, 11-fold).
The genesis of tyrosine phosphorylation.
Review
New
Hunter, Los Angeles, United States. In Cold Spring Harb Perspect Biol, May 2014
Like all types of protein phosphorylation, tyrosine phosphorylation serves to regulate proteins in multiple ways, including causing electrostatic repulsion and inducing allosteric transitions, but the most important function of phosphotyrosine (P.Tyr) is to serve as a docking site that promotes a specific interaction between a tyrosine phosphorylated protein and another protein that contains a P.Tyr-binding domain, such as an SH2 or PTB domain.
Preterm birth and its long-term effects: methylation to mechanisms.
Review
Smith et al., Atlanta, United States. In Biology (basel), 2013
This brief review explores the potential role of DNA methylation in preterm birth (PTB) and its possible long-term consequences and provides an overview of the physiological processes central to PTB and recent DNA methylation studies of PTB.
Genetic variation and RNA binding proteins: tools and techniques to detect functional polymorphisms.
Review
Fairbrother et al., Providence, United States. In Adv Exp Med Biol, 2013
The first characterizes a functional intronic SNP that deletes a high affinity PTB site using traditional low-throughput biochemical and functional assays.
Exploring preterm birth as a polymicrobial disease: an overview of the uterine microbiome.
Review
Bayatibojakhi et al., Perth, Australia. In Front Immunol, 2013
Infection is a leading cause of preterm birth (PTB).
PTB deficiency causes the loss of adherens junctions in the dorsal telencephalon and leads to lethal hydrocephalus.
GeneRIF
Yoshida et al., Tokyo, Japan. In Cereb Cortex, 2013
PTB depletion in the dorsal telencephalon is causally involved in the development of hydrocephalus. And PTB is important for the maintenance of Adherens Junctions in the neural stem cells of the dorsal telencephalon.
Temporal regulation of EGF signalling networks by the scaffold protein Shc1.
Impact
Pawson et al., Toronto, Canada. In Nature, 2013
Activated receptor tyrosine kinases, for example, engage scaffolds such as Shc1 that contain phosphotyrosine (pTyr)-binding (PTB) domains.
Direct conversion of fibroblasts to neurons by reprogramming PTB-regulated microRNA circuits.
Impact
Fu et al., Wuhan, China. In Cell, 2013
Here, we report that repression of a single RNA binding polypyrimidine-tract-binding (PTB) protein, which occurs during normal brain development via the action of miR-124, is sufficient to induce trans-differentiation of fibroblasts into functional neurons.
Evolutionary dynamics of gene and isoform regulation in Mammalian tissues.
Impact
Burge et al., Cambridge, United States. In Science, 2013
Thousands of previously unknown, lineage-specific, and conserved alternative exons were identified; widely conserved alternative exons had signatures of binding by MBNL, PTB, RBFOX, STAR, and TIA family splicing factors, implicating them as ancestral mammalian splicing regulators.
The uterine myocyte as a target for prevention of preterm birth.
Review
Slater et al., Edmonton, Canada. In Facts Views Vis Obgyn, 2012
Preterm birth (PTB) remains the most common cause of neonatal morbidity and mortality as well as long-term disability.
ERK1/2-dependent phosphorylation and nuclear translocation of PKM2 promotes the Warburg effect.
Impact
Lu et al., Houston, United States. In Nat Cell Biol, 2012
Nuclear PKM2 acts as a coactivator of β-catenin to induce c-Myc expression, resulting in the upregulation of GLUT1, LDHA and, in a positive feedback loop, PTB-dependent PKM2 expression.
Stem cell factor receptor/c-Kit: from basic science to clinical implications.
Review
Impact
Rönnstrand et al., Uppsala, Sweden. In Physiol Rev, 2012
Signaling proteins are recruited to activated c-Kit by certain interaction domains (e.g., SH2 and PTB) that specifically bind to phosphorylated tyrosine residues in the intracellular region of c-Kit.
The defective splicing caused by the ISCU intron mutation in patients with myopathy with lactic acidosis is repressed by PTBP1 but can be derepressed by IGF2BP1.
GeneRIF
Holmberg et al., Umeå, Sweden. In Hum Mutat, 2012
The defective splicing caused by the ISCU intron mutation in patients with myopathy with lactic acidosis is repressed by PTBP1 but can be derepressed by IGF2BP1.
PSD-95 is post-transcriptionally repressed during early neural development by PTBP1 and PTBP2.
GeneRIF
Black et al., Los Angeles, United States. In Nat Neurosci, 2012
The polypyrimidine tract binding proteins PTBP1 and PTBP2 repressed Psd-95 (also known as Dlg4) exon 18 splicing, leading to premature translation termination and nonsense-mediated mRNA decay.
Polypyrimidine tract binding protein (hnRNP I) is possibly a conserved modulator of miRNA-mediated gene regulation.
GeneRIF
Hutvagner et al., Dundee, United Kingdom. In Plos One, 2011
Polypyrimidine tract binding protein (hnRNP I) is possibly a conserved modulator of miRNA-mediated gene regulation.
Polypyrimidine tract-binding protein regulates the cell cycle through IRES-dependent translation of CDK11(p58) in mouse embryonic stem cells.
GeneRIF
Yoshida et al., Tokyo, Japan. In Cell Cycle, 2011
PTB regulates the precise expression of CDK11(p58) through direct interaction with CDK11(p58) IRES and promotes M phase progression in ES cells.
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