anti-Heterogeneous Nuclear Ribonucleoprotein A1 (HNRNPA1) Antibodies

Human Heterogeneous Nuclear Ribonucleoprotein A1 (HNRNPA1) interaction partners

1. Loss of Hnrnpa1 expression leads to dysregulation of cardiac transcription networks and multiple signaling pathways, including BMP, FGF, and Notch in the second heart field. Finally, two rare heterozygous mutations of HNRNPA1 were detected in human congenital heart defects. These findings suggest a role of Hnrnpa1 in embryonic heart development in mice and humans.

2. A role is identified for hnRNP A1 in the pathogenesis of multiple sclerosis.

3. review attempts to delineate the interactions of VZV, gE of VZV, with M9 domain and PrLD of HNRNPA1 in a step-by-step process.

4. Data indicate that heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a negative regulator of IKK-complex-associated protein (IKBKAP) exon 20 splicing.

5. Report direct role for hnRNPA1 in MYLK alternative splicing in lung endothelial cells.

6. HNRNPA1 3'UTR was most pervasively mis-spliced in pediatric B-cell acute lymphoblastic leukemia, yielding the transcript subject to nonsense-mediated decay.

7. Study identified the reversible amyloid-forming cores of hnRNPA1 (named hnRACs). The atomic structures of hnRACs reveal a distinct feature of stacking Asp residues, which contributes to fibril reversibility and explains the irreversible pathological fibril formation caused by the Asp mutations identified in familial amyotrophic lateral sclerosis.

8. REVIEW: available structural biochemical developments of hnRNP A1-RNA recognition, as a framework to interpret its wide-range of RNA functions

9. Moreover, SRSF10, hnRNP A1/A2 and Sam68 collaborate to drive the DNA damage-induced splicing response of several transcripts that produce components implicated in apoptosis, cell-cycle control and DNA repair.

10. By using an integrative structural biology approach, we show that hnRNP A1 forms a 1:1 complex with pri-mir-18a where both RNA recognition motifs (RRMs) bind to cognate RNA sequence motifs in the terminal loop of pri-mir-18a.

11. Data suggest that one way heterogeneous nuclear ribonucleoprotein A1 (HNRNPA1) regulates exon definition is to modulate the interaction of U2 small nuclear RNA auxiliary factor 2 (U2AF2) with decoy or bona fide 3' splice site (3'ss).

12. Our results indicate that hnRNP A1 promotes cell survival and cell cycle progression following UVB radiation

13. These findings indicated that hnRNPA1 is highly expressed in gastric cancer (GC)and promoted invasion by inducing Epithelialtomesenchymal transition (EMT) in GC cells. Thus, hnRNPA1 may be a potential therapeutic target for GC.

14. A significant overlap between hnRNPA1 and DDX5 splicing targets and they share many closely linked binding sites.

15. Results suggest that telomeric repeat-containing RNA (TERRA) regulates binding of heterogeneous nuclear ribonucleoprotein A1 to the telomere in a region surrounding the telomere, leading to a deeper understanding of the mechanism of TERRA function.

16. mutation in HNRNPA1 located in the nuclear localization signal domain of hnRNPA1, enhances the recruitment of mutant hnRNPA1 into stress granules, indicating that an altered nuclear localization signal activity plays an essential role in amyotrophic lateral sclerosis pathogenesis.

17. Rules of RNA specificity of hnRNP A1 revealed by global and quantitative analysis of its affinity distribution have been described.

18. study showed that UVB induces alternative splicing of hdm2 by increasing the expression and the binding of hnRNP A1 to hdm2 full-length mRNA

19. The authors show by NMR spectroscopy that both RNA recognition motifs of hnRNP A1 can bind simultaneously to a single bipartite motif of the human intronic splicing silencer ISS-N1, which controls survival of motor neuron exon 7 splicing.

20. current knowledge of the involvement of hnRNPA1 in cancer, including its roles in regulating cell proliferation, invasiveness, metabolism, adaptation to stress and immortalization.

Mouse (Murine) Heterogeneous Nuclear Ribonucleoprotein A1 (HNRNPA1) interaction partners

1. Loss of Hnrnpa1 expression leads to dysregulation of cardiac transcription networks and multiple signaling pathways, including BMP, FGF, and Notch in the second heart field. Finally, two rare heterozygous mutations of HNRNPA1 were detected in human congenital heart defects. These findings suggest a role of Hnrnpa1 in embryonic heart development in mice and humans.

2. Report direct role for hnRNPA1 in MYLK alternative splicing in lung endothelial cells.

3. Knockdown of hnRNP A1 led to a decrease in endogenous Nfil3 protein level, which could be due to a reduction in IRES-mediated translation.

4. Study demonstrated that hnRNPA1 plays a critical and irreplaceable role in embryonic muscle development by regulating the expression and alternative splicing of muscle-related genes.

5. hnRNPA1 is a critical regulator of vascular smooth muscle cell function and behavior in the context of neointima hyperplasia via miR-124/IQGAP1 regulatory axis.

6. PRMT5 regulates internal ribosome entry site-dependent translation via methylation of hnRNP A1.

7. Resveratrol causes a shift from the mesenchymal-specific forms of these factors to the respective epithelial forms and increases the expression of the RNA-binding proteins KHSRP and hnRNPA1.

8. this study identified hnRNPA1, an RNA-binding protein and auxiliary splicing factor, as a substrate of TRAF6; TRAF6 ubiquitination of hnRNPA1 regulated alternative splicing of Arhgap1, which resulted in activation of the GTP-binding Rho family protein Cdc42 and accounted for hematopoietic defects in TRAF6-expressing hematopoietic stem/ progenitor cells

9. A1 and A2/B1, which are required for transcript degradation

10. hnRNP A1 improves intestinal injury in anti-CD3 antibody-induced enteritis mice through the upregulation of TFF2, which regulates apoptosis and enhances epithelial restoration

11. Relevant to biological processes anticipated for hnRNP A1 and HuR.

12. This study provides evidence that PCBP2 and hnRNP A1 bind to the 5' and 3' ends of the murine norovirus 1 viral RNA and contribute to RNA circularization, playing a role in the virus life cycle.

13. Heteronuclear ribonucleoprotein A1 interacts with an element that overlaps the 5' splice site of Mag exon 12.

14. MMP-3-triggered Rac1 splicing regulation is modulated by hnRNP A1

15. the phosphorylation status of hnRNP A1 serine 199 regulates the AKT-dependent sensitivity of cells to rapamycin and functionally links IRES-transacting factor annealing activity to cellular responses to mTOR complex 1 inhibition.

16. eIF2alpha phosphorylation during hypertonic stress promotes apoptosis by sequestration of specific mRNAs in SGs in a process mediated by the cytoplasmic accumulation of hnRNP A1

17. splicing repressors hnRNP A1 and A2, as well as the polypyrimidine-tract-binding protein PTB, contribute to control of pyruvate kinase isoform M1 and M2 expression

18. data provide evidence that hnRNP A1 is directly or indirectly involved in mouse hepatitis virus RNA transcription and replication

19. study provides direct in vivo evidence demonstrating a functional role for hnRNP A1 in mouse hepatitis virus RNA synthesis

20. results are consistent with a model in which the binding of hnRNP A1 to the 71 nt putative hairpin-loop region in the CYP2A5 mRNA 3' UTR upregulates mRNA levels possibly by protecting the mRNA from degradation

Pig (Porcine) Heterogeneous Nuclear Ribonucleoprotein A1 (HNRNPA1) interaction partners

1. the swine HNRPA1 gene was moderately expressed in fat, spleen and kidney, weakly expressed in muscle and lung, and hardly expressed in small intestine, large intestine and liver.