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Heterogeneous nuclear ribonucleoprotein A0

hnRNP A0, hnRNA binding protein K, heterogeneous nuclear ribonucleoprotein A0
This gene belongs to the A/B 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 two repeats of quasi-RRM domains that bind RNAs, followed by a glycine-rich C-terminus. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MAPK, p38, V1a, SF-1, CAN
Papers on hnRNP A0
MK2 inhibitory peptide delivered in nanopolyplexes prevents vascular graft intimal hyperplasia.
Duvall et al., Nashville, United States. In Sci Transl Med, Jul 2015
In intact human saphenous vein, MK2i-NPs blocked inflammatory and migratory signaling, as confirmed by reduced phosphorylation of the posttranscriptional gene regulator heterogeneous nuclear ribonucleoprotein A0, the transcription factor cAMP (adenosine 3',5'-monophosphate) element-binding protein, and the chaperone heat shock protein 27.
Identifying rare variants for genetic risk through a combined pedigree and phenotype approach: application to suicide and asthma.
Coon et al., Salt Lake City, United States. In Transl Psychiatry, 2013
Our top associated genes included those related to neurodevelopment or neural signaling (brain-derived neurotrophic factor (BDNF), neutral sphingomyelinase 2 (SMPD2), homeobox b2 (HOXB2), neural cell adhesion molecule (NCAM2), heterogeneous nuclear ribonucleoprotein A0 (HNRNPA0)), inflammation (free fatty acid receptor 2 (FFAR2)) and inflammation with additional evidence of neuronal involvement (oxidized low density lipoprotein receptor 1 (OLR1), toll-like receptor 3 (TLR3)).
MAPKAP kinases MK2 and MK3 in inflammation: complex regulation of TNF biosynthesis via expression and phosphorylation of tristetraprolin.
Gaestel et al., Hannover, Germany. In Biochem Pharmacol, 2011
Among the substrates of MK2/3, there are mRNA-AU-rich-element (ARE)-binding proteins, such as tristetraprolin (TTP) and hnRNP A0, which regulate mRNA stability and translation in a phosphorylation-dependent manner.
Prefrontal cortex shotgun proteome analysis reveals altered calcium homeostasis and immune system imbalance in schizophrenia.
Turck et al., São Paulo, Brazil. In Eur Arch Psychiatry Clin Neurosci, 2009
Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
Nitric oxide-p38 MAPK signaling stabilizes mRNA through AU-rich element-dependent and -independent mechanisms.
Danner et al., Bethesda, United States. In J Leukoc Biol, 2008
Two proteins, HuR and heterogeneous nuclear ribonucleoprotein A0, were identified, which bound to the AURE-containing region of exogenous and endogenous IL-8 mRNA in a NO(*)-p38 MAPK-dependent manner.
Vertebrate 2xRBD hnRNP proteins: a comparative analysis of genome, mRNA and protein sequences.
Manzini et al., Trieste, Italy. In Comput Biol Chem, 2005
An exception is the gene of hnRNP A0, which is intronless consistently in all the four species.
Inhibition of SAPK2a/p38 prevents hnRNP A0 phosphorylation by MAPKAP-K2 and its interaction with cytokine mRNAs.
Cohen et al., Dundee, United Kingdom. In Embo J, 2003
Here, we identify 18 macrophage proteins that bind to AREs and show that hnRNP A0 is a major substrate for MAPKAP-K2 in this fraction.
Isolation and characterization of a novel, low abundance hnRNP protein: A0.
Steitz et al., New Haven, United States. In Rna, 1995
We report the cloning and characterization of a novel, low-abundance member of the A/B family named hnRNP A0.
Tissue specific expression and cDNA structure of a human transcript encoding a nucleic acid binding [oligo(dC)] protein related to the pre-mRNA binding protein K.
Smeland et al., Oslo, Norway. In Nucleic Acids Res, 1994
The predicted amino acid sequence shows homology to repeated domains in the human hnRNA binding protein K (hnRNP K), which are believed to be of functional importance.
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