Relevant bibliographies by topics / HnRNPA1

Academic literature on the topic 'HnRNPA1'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "HnRNPA1"

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Pettit Kneller, Elizabeth L., John H. Connor, and Douglas S. Lyles. "hnRNPs Relocalize to the Cytoplasm following Infection with Vesicular Stomatitis Virus." Journal of Virology 83, no. 2 (November 12, 2008): 770–80. http://dx.doi.org/10.1128/jvi.01279-08.

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ABSTRACT Vesicular stomatitis virus (VSV) matrix protein inhibits nuclear-cytoplasmic mRNA transport. The goal of this work is to determine whether VSV inhibits the nuclear-cytoplasmic transport of heterogeneous ribonucleoproteins (hnRNPs), which are thought to serve as mRNA export factors. Confocal microscopy experiments showed that hnRNPA1, hnRNPK, and hnRNPC1/C2, but not hnRNPB1 or lamin A/C, are relocalized to the cytoplasm during VSV infection. We determined whether protein import is inhibited by VSV by transfecting cells with a plasmid encoding enhanced green fluorescent protein (EGFP) tagged with either the M9 nuclear localization sequence (NLS) or the classical NLS. These experiments revealed that both the M9 NLS and the classical NLS are functional during VSV infection. These data suggest that the inhibition of protein import is not responsible for hnRNP relocalization during VSV infection but that hnRNP export is enhanced. We found that hnRNPA1 relocalization was significantly reduced following the silencing of the mRNA export factor Rae1, indicating that Rae1 is necessary for hnRNP export. In order to determine the role of hnRNPA1 in VSV infection, we silenced hnRNPA1 in HeLa cells and assayed three aspects of the viral life cycle: host protein synthesis shutoff concurrent with the onset of viral protein synthesis, replication by plaque assay, and cell killing. We observed that host shutoff and replication are unaffected by the reduction in hnRNPA1 but that the rate of VSV-induced apoptosis is slower in cells that have reduced hnRNPA1. These data suggest that VSV promotes hnRNPA1 relocalization in a Rae1-dependent manner for apoptotic signaling.
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Komuro, Riho, Yuka Honda, Motoaki Yanaizu, Masami Nagahama, and Yoshihiro Kino. "Alzheimer’s Disease-Associated Alternative Splicing of CD33 Is Regulated by the HNRNPA Family Proteins." Cells 12, no. 4 (February 13, 2023): 602. http://dx.doi.org/10.3390/cells12040602.

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Genetic variations of CD33 have been implicated as a susceptibility factor of Alzheimer’s disease (AD). A polymorphism on exon 2 of CD33, rs12459419, affects the alternative splicing of this exon. The minor allele is associated with a reduced risk of AD and promotes the skipping of exon 2 to produce a shorter CD33 isoform lacking the extracellular ligand-binding domain, leading to decreased suppressive signaling on microglial activity. Therefore, factors that regulate the splicing of exon 2 may alter the disease-associated properties of CD33. Herein, we sought to identify the regulatory proteins of CD33 splicing. Using a panel of RNA-binding proteins and a human CD33 minigene, we found that exon 2 skipping of CD33 was promoted by HNRNPA1. Although the knockdown of HNRNPA1 alone did not reduce exon 2 skipping, simultaneous knockdown of HNRNPA1 together with that of HNRNPA2B1 and HNRNPA3 promoted exon 2 inclusion, suggesting functional redundancy among HNRNPA proteins. Similar redundant regulation by HNRNPA proteins was observed in endogenous CD33 of THP-1 and human microglia-like cells. Although mouse Cd33 showed a unique splicing pattern of exon 2, we confirmed that HNRNPA1 promoted the skipping of this exon. Collectively, our results revealed novel regulatory relationships between CD33 and HNRNPA proteins.
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Cloe, Adam, Li Chen, Yuan Li, Hongtao Liu, and Jason X. Cheng. "Identification of Specific Hnrnps As Novel Therapeutic Targets and Responsive Indicators of KPT330 (selinexor) in Leukemia." Blood 128, no. 22 (December 2, 2016): 1657. http://dx.doi.org/10.1182/blood.v128.22.1657.1657.

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Abstract Background: Activenuclear-cytoplasmic shuttling of proteins and RNAs, such as heterogeneous ribonucleoproteins (hnRNPs), is essential for the normal function and survival of eukaryotic cells and tumorigenesis (Dreyfuss et al. 1993 Annu Rev Biochem 62, 289; Gorlich and Mattaj 1996 Science 271, 1513). Up-regulation of exportin 1 (XPO1)/chromosomal maintenance 1 (CRM1), a member of the karyopherin-β family of nuclear export receptor proteins, has been implicated in solid and hematologic malignancies (Kau Kau et al. 2004).Selinexor (KPT-330) has been shown to be able block in vitro and in vivo XPO1/CRM1 functions and is currently in phase-II/IIb clinical trials for treatment of hematologic and solid tumors (Senapedis et al., 2014 Nat Rev Cancer 4, 106). However, the mechanisms underlying the selectivity and efficacy of selinexor are incompletely understood, and no biomarkers are currently available to predict clinical responses to selinexor in clinical settings. In this study, we focus on determining the effects of selinexor on the nuclear-cytoplasmic shuttling of hnRNPs, particularly hnRNPK and hnRNPA1, to elucidate the roles of the hnRNPs in the regulation of selectivity and efficacy of selinexor in myelodysplastic syndrome (MDS) and acute myeloid leukemia (AML). Method:We performed growth inhibition/killing assays, histopathologic evaluations, immunohistochemical studies, subcellular fraction western blotting, super-resolution stimulated emission depletion (STED) confocal microcopy and siRNA knockdown experiments. Results: Our in vitro experiments demonstrate a marked increase in XPO1/CRM1 protein and decrease in TP53 in our azacitidine-resistant MDS/AML cell lines compared to our azacitidine-sensitive MDS/AML cell lines. Selinexor treatment efficiently blocks export of hnRNP K from nuclei and increased nuclear accumulation of hnRNPK and inhibits MDS/AML cell growth, while the protein levels of XPO1/CRM1 and TP53 remain unchanged. Our experiments using clinical bone marrow specimens show no significant difference in the total protein level or nuclear accumulation of XPO1/CRM1 between the normal control and MDS or AML bone marrow specimens. In contrast, a strong positive correlation between MDS/AML disease progression and hnRNPK protein accumulation is observed in those clinical specimens. We have extended our experiments to clinical bone marrow specimens from a small cohort in a clinical trial for selinexor in AML at the University of Chicago (NCT02573363). In our small cohort, 5 patients responded to selinexor, 4 patients did not respond and 1 had a partial response. All 5 responders show a striking decrease in their bone marrow blast percentage from their pre-treatment marrows (average blast percentage 37.4%) to their post-treatment (average blast percentage 1.8%). Non-responders show no such difference in pre and post-treatment blast percentage (56.3 and 57.1%, respectively). Importantly, our experiments demonstrate a marked difference in the protein accumulation and subcellular localization of hnRNPK and hnRNPA1, another member of the hnRNP family, between selinexor-responder and selinexor-non-responder bone marrow specimens. Specifically, selinexor responders had much higher levels of hnRNPK and hnRNPA1 proteins in their pre-treatment bone marrows than non-responders, despite the fact that the latter had higher bone marrow blast percentages on average. There is markedly reduced accumulation of hnRNPK and hnRNPA1 in the post-selinexor treatment bone marrow specimens from the responders, but not the non-responders, suggesting these hnRNPs as key therapeutic targets for selinexor in MDS and AML. In contrast, no significant change in XPO1/CRM1 protein levels is observed in the selinexor-responder vs. selinexor-non-responder bone marrow specimens. Conclusion:Our data have revealed a novel drug-action mechanism by which selinexor impairs the nuclear-cytoplasmic shuttling of hnRNPK and hnRNPA1 in MDS and AML cells. Differential expression and localization of these hnRNPs in normal vs. MDS vs. AML cells may provide the rationale for the preferential killing of leukemia cells by selinexor. Our data also suggest the possibility to develop novel hnRNP-based biomarkers to predict the response to selinexor in clinical settings. Disclosures Liu: Karyopharm: Research Funding; BMS: Research Funding.
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Rothzerg, Emel, Wenyu Feng, Dezhi Song, Hengyuan Li, Qingjun Wei, Archa Fox, David Wood, Jiake Xu, and Yun Liu. "Single-Cell Transcriptome Analysis Reveals Paraspeckles Expression in Osteosarcoma Tissues." Cancer Informatics 21 (January 2022): 117693512211401. http://dx.doi.org/10.1177/11769351221140101.

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Nuclear paraspeckles are subnuclear bodies contracted by nuclear-enriched abundant transcript 1 (NEAT1) long non-coding RNA, localised in the interchromatin space of mammalian cell nuclei. Paraspeckles have been critically involved in tumour progression, metastasis and chemoresistance. To this date, there are limited findings to suggest that paraspeckles, NEAT1 and heterogeneous nuclear ribonucleoproteins (hnRNPs) directly or indirectly play roles in osteosarcoma progression. Herein, we analysed NEAT1, paraspeckle proteins (SFPQ, PSPC1 and NONO) and hnRNP members (HNRNPK, HNRNPM, HNRNPR and HNRNPD) gene expression in 6 osteosarcoma tumour tissues using the single-cell RNA-sequencing method. The normalised data highlighted that the paraspeckles transcripts were highly abundant in osteoblastic OS cells, except NEAT1, which was highly expressed in myeloid cell 1 and 2 subpopulations.
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White, Theresa L., Matthew Gable, Ye Jin, and Penelope Morel. "Understanding how AKT phosphorylation of hnRNPA1 modulates T cell fate and function." Journal of Immunology 202, no. 1_Supplement (May 1, 2019): 115.21. http://dx.doi.org/10.4049/jimmunol.202.supp.115.21.

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Abstract T regulatory cells (Treg) play a significant role in maintaining self-tolerance and preventing autoimmune diseases. We and others have shown that low dose favors Treg and T helper (Th) 2 cell differentiation, while high Ag dose stimulation activates the PI3K/Akt/mTOR pathway, favoring inflammatory Th1 and Th17 cell differentiation (Tconv). Differences in PI3K/Akt/mTOR signaling not only affects T cell fate but our research shows that Akt phosphorylation of the RNA-binding protein, (RBP) heterogeneous nuclear ribonucleoprotein (hnRNP) A1, is dependent on TCR signal strength. RBPs such as hnRNPA1 are emerging as regulators of RNA processing and stability in immune cells, and the effect of RBP on T cell differentiation is a growing subject of interest. We have shown hnRNPA1 is required for optimal Treg differentiation by performing knockdown experiments, and our present research is focused on identifying a role for Akt phosphorylation in hnRNPA1 function. HnRNPA1 is known to have a single Akt phosphorylation site at S199 and our lab has generated a new mutant mouse model, hnRNPA1-S199A (mA1). This mutation affects the ability of Akt to phosphorylate hnRNPA1 in all immune cells. Using Cytek’s Aurora flow cytometer we characterized the immune cell populations of mA1 at steady state. Preliminary data do not indicate any major changes in innate immune and B cells populations at steady state. We observed modest changes in CD4 T cell population frequencies at steady state. Current work using In vitro skewing suggests that Akt phosphorylation of hnRNPA1 influences Treg fate. This project suggests a novel mechanism by which Akt modulates T cell fate.
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White, Tristan L., Matthew Gable, Ye Jin, and Penelope A. Morel. "The Role of HnRNPA1 in T Cell-Mediated Gut Tolerance." Journal of Immunology 208, no. 1_Supplement (May 1, 2022): 56.12. http://dx.doi.org/10.4049/jimmunol.208.supp.56.12.

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Abstract Our previous research showed that Akt phosphorylation of the RNA-binding protein, (RBP) heterogeneous nuclear ribonucleoprotein (hnRNP) A1, is dependent on TCR signal strength, and occurs under conditions of induced T regulatory (Treg) cell differentiation. We have shown hnRNPA1 is required for optimal Treg differentiation by performing knockdown experiments, and our present research is focused on identifying a role for Akt phosphorylation in hnRNPA1 function. HnRNPA1 is phosphorylated by Akt at S199 and our lab has generated a new mutant mouse model, hnRNPA1-S199A (mA1), in which hnRNPA1 will no longer be Akt-phosphhorylated. Our initial characterization of mA1 mouse model failed to reveal major abnormalities in immune cells populations at steady state except for changes in the Treg proportion in the mesenteric lymph nodes. To investigate the effect of the mA1 on the development of oral tolerance we used an adoptive transfer model in which OT-II mA1 or OT-II WT naïve T cells were transferred into congenic strains and then the mice were given OVA food. Results indicate that mA1 OT-II T cells have a proliferation defect in vivo and we also observed a significant reduction in the induction of OVA-specific Treg in the mA1 T cells. Similar results were obtained when adoptively transferred OT-II mA1 T cells were challenged with limiting doses of specific peptide, given iv. RNASeq analysis of the transferred mA1 and WT T cells is being performed. These results suggest that Akt phosphorylation of hnRNPA1 is necessary for T cell response to low dose antigen and Treg induction in vivo. Our studies identify a new mechanism by which RBP influence T cell proliferation and Treg differentiation which has implications for tolerance to food antigens in the gut. Supported by NIH (F31-AI152320-02) NIH (R01-AI125513-03)
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Zhang, Li, Qishan Chen, Weiwei An, Feng Yang, Eithne Margaret Maguire, Dan Chen, Cheng Zhang, et al. "Novel Pathological Role of hnRNPA1 (Heterogeneous Nuclear Ribonucleoprotein A1) in Vascular Smooth Muscle Cell Function and Neointima Hyperplasia." Arteriosclerosis, Thrombosis, and Vascular Biology 37, no. 11 (November 2017): 2182–94. http://dx.doi.org/10.1161/atvbaha.117.310020.

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Objective— hnRNPA1 (heterogeneous nuclear ribonucleoprotein A1) plays a variety of roles in gene expression. However, little is known about the functional involvement of hnRNPA1 in vascular smooth muscle cell (VSMC) function and neointima hyperplasia. In this study, we have attempted to investigate the functional roles of hnRNPA1 in the contexts of VSMC function, injury-induced vessel remodeling, and human atherosclerotic lesions, as well as discern the molecular mechanisms involved. Approach and Results— hnRNPA1 expression levels were consistently modulated during VSMC phenotype switching and neointimal lesion formation induced by wire injury. Functional studies showed that VSMC-specific gene expression, proliferation, and migration were regulated by hnRNPA1. Our data show that hnRNPA1 exerts its effects on VSMC functions through modulation of IQGAP1 (IQ motif containing GTPase activating protein 1). Mechanistically, hnRNPA1 regulates IQGAP1 mRNA degradation through 2 mechanisms: upregulating microRNA-124 (miR-124) and binding to AU-rich element of IQGAP1 gene. Further evidence suggests that hnRNPA1 upregulates miR-124 by modulating miR-124 biogenesis and that IQGAP1 is the authentic target gene of miR-124. Importantly, ectopic overexpression of hnRNPA1 greatly reduced VSMC proliferation and inhibited neointima formation in wire-injured carotid arteries. Finally, lower expression levels of hnRNPA1 and miR-124, while higher expression levels of IQGAP1, were observed in human atherosclerotic lesions. Conclusions— Our data show that hnRNPA1 is a critical regulator of VSMC function and behavior in the context of neointima hyperplasia, and the hnRNPA1/miR-124/IQGAP1 regulatory axis represents a novel therapeutic target for the prevention of cardiovascular diseases.
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Toosaranont, Jarichad, Sukanya Ruschadaariyachat, Warasinee Mujchariyakul, Jantarika Kumar Arora, Varodom Charoensawan, Bhoom Suktitipat, Thomas N. Palmer, Sue Fletcher, Steve D. Wilton, and Chalermchai Mitrpant. "Antisense Oligonucleotide Induction of the hnRNPA1b Isoform Affects Pre-mRNA Splicing of SMN2 in SMA Type I Fibroblasts." International Journal of Molecular Sciences 23, no. 7 (April 1, 2022): 3937. http://dx.doi.org/10.3390/ijms23073937.

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Spinal muscular atrophy (SMA) is a severe, debilitating neuromuscular condition characterised by loss of motor neurons and progressive muscle wasting. SMA is caused by a loss of expression of SMN1 that encodes the survival motor neuron (SMN) protein necessary for the survival of motor neurons. Restoration of SMN expression through increased inclusion of SMN2 exon 7 is known to ameliorate symptoms in SMA patients. As a consequence, regulation of pre-mRNA splicing of SMN2 could provide a potential molecular therapy for SMA. In this study, we explored if splice switching antisense oligonucleotides could redirect the splicing repressor hnRNPA1 to the hnRNPA1b isoform and restore SMN expression in fibroblasts from a type I SMA patient. Antisense oligonucleotides (AOs) were designed to promote exon 7b retention in the mature mRNA and induce the hnRNPA1b isoform. RT-PCR and western blot analysis were used to assess and monitor the efficiency of different AO combinations. A combination of AOs targeting multiple silencing motifs in hnRNPA1 pre-mRNA led to robust hnRNPA1b induction, which, in turn, significantly increased expression of full-length SMN (FL-SMN) protein. A combination of PMOs targeting the same motifs also strongly induced hnRNPA1b isoform, but surprisingly SMN2 exon 5 skipping was detected, and the PMO cocktail did not lead to a significant increase in expression of FL-SMN protein. We further performed RNA sequencing to assess the genome-wide effects of hnRNPA1b induction. Some 3244 genes were differentially expressed between the hnRNPA1b-induced and untreated SMA fibroblasts, which are functionally enriched in cell cycle and chromosome segregation processes. RT-PCR analysis demonstrated that expression of the master regulator of these enrichment pathways, MYBL2 and FOXM1B, were reduced in response to PMO treatment. These findings suggested that induction of hnRNPA1b can promote SMN protein expression, but not at sufficient levels to be clinically relevant.
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Fifita, Jennifer A., Katharine Y. Zhang, Jasmin Galper, Kelly L. Williams, Emily P. McCann, Alison L. Hogan, Neil Saunders, et al. "Genetic and Pathological Assessment of hnRNPA1, hnRNPA2/B1, and hnRNPA3 in Familial and Sporadic Amyotrophic Lateral Sclerosis." Neurodegenerative Diseases 17, no. 6 (2017): 304–12. http://dx.doi.org/10.1159/000481258.

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Möller, Katharina, Anna Lena Wecker, Doris Höflmayer, Christoph Fraune, Georgia Makrypidi-Fraune, Claudia Hube-Magg, Martina Kluth, et al. "Upregulation of the heterogeneous nuclear ribonucleoprotein hnRNPA1 is an independent predictor of early biochemical recurrence in TMPRSS2:ERG fusion-negative prostate cancers." Virchows Archiv 477, no. 5 (May 16, 2020): 625–36. http://dx.doi.org/10.1007/s00428-020-02834-4.

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Abstract Heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1) is a ubiquitous RNA splicing factor that is overexpressed and prognostically relevant in various human cancer types. To study the impact of hnRNPA1 expression in prostate cancer, we analyzed a tissue microarray containing 17,747 clinical prostate cancer specimens by immunohistochemistry. hnRNPA1 was expressed in normal prostate glandular cells but often overexpressed in cancer cells. hnRNPA1 immunostaining was interpretable in 14,258 cancers and considered strong in 33.4%, moderate in 45.9%, weak in 15.3%, and negative in 5.4%. Moderate to strong hnRNPA1 immunostaining was strongly linked to adverse tumor features including high classical and quantitative Gleason score, lymph node metastasis, advanced tumor stage, positive surgical margin, and early biochemical recurrence (p < 0.0001 each). The prognostic impact of hnRNPA1 immunostaining was independent of established preoperatively or postoperatively available prognostic parameters (p < 0.0001). Subset analyses revealed that all these associations were strongly driven by the fraction of cancers lacking the TMPRSS2:ERG gene fusion. Comparison with other key molecular data that were earlier obtained on the same TMA showed that hnRNPA1 overexpression was linked to high levels of androgen receptor (AR) expression (p < 0.0001) as well as presence of 9 of 11 chromosomal deletions (p < 0.05 each). A strong association between hnRNPA1 upregulation and tumor cell proliferation that was independent from the Gleason score supports a role for tumor cell aggressiveness. In conclusion, hnRNPA1 overexpression is an independent predictor of poor prognosis in ERG-negative prostate cancer. hnRNPA1 measurement, either alone or in combination, might provide prognostic information in ERG-negative prostate cancer.
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Dissertations / Theses on the topic "HnRNPA1"

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Najim, Mustafa. "Hepatitis C virus induced changes in cellular trafficking and lipid metabolism - identifying novel host factors required for HCV replication." Thesis, The University of Sydney, 2018. http://hdl.handle.net/2123/20895.

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Hepatitis C virus (HCV) infection is endemic in numerous countries and is a global health issue, placing a huge burden on health care systems and society. The high prevalence of people who are chronically infected with HCV, the disease burden and the absence of an effective vaccine reinforce the importance of HCV treatment in controlling this disease. Direct acting antivirals (DAAs), have revolutionised HCV treatment over the last few years. However, people failing DAAs typically develop antiviral resistance, so new treatments may still be needed in future. To identify novel host factors involved in HCV infection, a mass spectrometry based Stable Isotope Labelling of Amino acids in Cell culture (SILAC) screen was performed, to identify proteins that are enriched in the Endoplasmic Reticulum (ER) of HCV infected hepatocytes. This showed significant upregulation of Coatomer Protein Complex-I (COPI). Next, we examined the effect of Phosphatidylinositol 4-phosphate (PI4P) depletion on tafficking of COPI to the ER and on HCV replication, by over-expressing the PI4P phosphatase Sac1. However, due to the limitations of the model, we could neither prove or disprove this hypothesis, as we could not achieve sustained overexpression of Sac1. Next, we evaluated the consequence of silencing heterogeneous nuclear ribonucleoproteins C1/C2 (hnRNPC1/C2) and transmembrane 6 superfamily member 2 (TM6SF2) on HCV replication. We found that hnRNPC1/C2 inhibition has no effect on HCV replication, while TM6SF2 is required for HCV replication. In summary, these findings identify a range of essential host proteins that could be targeted by novel host-targeting antiviral drugs. Finally, our findings provide potential insights into the life cycle of other related viruses, which have far fewer treatments available.
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Labrecque, Benoît. "Identification des résidus contribuant à l'interaction hnRNP A1- hnRNP A1." Mémoire, Université de Sherbrooke, 2003. http://savoirs.usherbrooke.ca/handle/11143/3336.

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HnRNP A1 est une protéine impliquée dans la sélection des sites 5 ' d'épissage in vitro et in vivo . Il est connu que son domaine riche en glycines est important pour médier son activité dans l'épissage alternatif. Le modèle"looping-out" a été proposé comme mécanisme d'action de A1; lorsque A1 lie des sites de haute affinité localisés dans la région intronique de part et d'autre d'un exon alternatif, l'exclusion de celui-ci est favorisé par une interaction A1-A1 impliquant le domaine riche en glycines. Les régions et les acides aminés impliqués dans l'interaction A1-A1 restent méconnus. Une mutagénèse aléatoire de l'ADNc de A1, suivie d'une approche génétique chez la bactérie basée sur la répression traductionnelle, nous a permis d'aborder l'importance du domaine riche en glycines et du domaine RRM2 dans la liaison coopérative de la protéine hnRNP A1 à PARN. La majorité des mutants identifiés montrent un défaut au niveau de l'interaction A1-A1 lorsque quantifiés dans un essai double-hybride chez la levure."--Résumé abrégé par UMI.
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Fisette, Jean-François. "Le contrôle de l'épissage alternatif par les protéines hnRNP H et hnRNP A1." Thèse, Université de Sherbrooke, 2009. http://savoirs.usherbrooke.ca/handle/11143/4275.

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Les protéines hnRNP A1 sont impliquées dans l'épissage alternatif. Un mode d'action proposé implique la formation d'homodimères entre molécules hnRNP A1 causant un réarrangement dans la structure de l'ARN pré-messager. Cette modulation de l'ARN permettrait le rapprochement de sites d'épissage 5' et 3' d'exons situés de par et d'autres d'un exon alternatif. Le domaine riche en résidus glycines est responsable, en grande partie, de l'interaction entre les deux protéines hnRNP A1. Comme la protéine hnRNP H contient aussi un domaine riche en résidus glycines, nous avons postulé que cette dernière pouvait moduler l'épissage alternatif de la même manière que hnRNP A1. Afin de vérifier cette hypothèse, nous avons utilisé un ARN pré-messager constitué de deux sites d'épissage 5' (distal et proximal) en compétition pour un seul site d'épissage 3'. En présence de sites de liaison pour hnRNP H, nous observons que le choix du site d'épissage 5' est déplacé vers le site distal. Nous avons confirmé le rôle des protéines hnRNP H dans la sélection des sites d'épissage 5' in vitro et avons déterminé que le domaine riche en résidus glycines (GRD) est important pour l'activité d'épissage de ce régulateur. Nous avons ensuite exploré la possibilité que des combinaisons de sites de liaison pour hnRNP H et hnRNP A1 puissent activer l'utilisation du site d'épissage 5' distal. Nous avons observé que des combinaisons hétérotypiques peuvent reproduire cette activité d'épissage. Finalement, nous avons utilisé la technologie BRET ("bioluminescence resonance energy transfer") pour démontrer que des interactions homotypiques entre protéines hnRNP H et hétérotypiques entre molécules hnRNP A1 et hnRNP H peuvent se former dans les cellules vivantes. Notre étude suggère que les protéines hnRNP H et hnRNP A1 peuvent changer la conformation de l'ARN pré-messager et affecter le choix du site d'épissage.
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Moran-Jones, Kim. "hnRNPs A2 and A3 : nucleic acid interactions /." St. Lucia, Qld, 2004. http://www.library.uq.edu.au/pdfserve.php?image=thesisabs/absthe17983.pdf.

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Jansen, Lara [Verfasser], and Christian [Akademischer Betreuer] Haass. "Generation and functional analysis of the ALS associated HNRNPA zebrafish mutants / Lara Jansen ; Betreuer: Christian Haass." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2019. http://d-nb.info/122243654X/34.

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Barral, Paola. "Characterization of a novel hnRNP : E1B-AP5." Thesis, University of Birmingham, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.403905.

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Le, Bras Morgane. "Rôle des protéines de liaison à l'ARN hnRNP H et hnRNP F dans les régulations traductionnelles dans les glioblastomes." Thesis, Toulouse 3, 2018. http://www.theses.fr/2018TOU30277.

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Le glioblastome multiforme (GBM) est une tumeur cérébrale extrêmement agressive associée à un mauvais pronostic. C'est pourquoi, il apparaît nécessaire d'identifier les mécanismes moléculaires participant au développement des GBM ainsi qu'à leurs résistances aux traitements afin de développer de nouvelles approches thérapeutiques. Récemment, il a été montré que les régulations traductionnelles jouent un rôle fondamental dans les propriétés agressives du GBM. Les protéines de liaison à l'ARN (RBP) sont des acteurs majeurs de ces régulations dont l'expression/activité est altérée dans les GBM. Les RBP hnRNP HF (HF) font partie des RBP les plus surexprimées dans les GBM et leur contribution dans la régulation traductionnelle des GBM n'a encore jamais été investiguée. Nous avons émis l'hypothèse que hnRNP H et hnRNP F soient au centre d'un réseau de régulations post-transcriptionnelles impactant la machinerie traductionnelle qui contrôle le développement tumoral et la résistance aux traitements des GBM. Nos résultats montrent qu'HF régulent la prolifération et la réponse aux traitements car leur perte d'expression (i) diminue la prolifération des GBM (modèle cellulaire, sphéroïde et xénogreffes in vivo), (ii) active les voies de réponse aux dommages à l'ADN et (iii) sensibilise les cellules de GBM aux irradiations. De plus, nous avons identifié un nouveau rôle pour HF en tant que régulateurs de la traduction. En effet, nos données montrent que les hnRNP HF contrôlent la traduction d'un ensemble d'ARNm en régulant l'expression et l'activité de facteurs d'initiation ainsi qu'en collaborant avec des ARN hélicases partenaires en ciblant des ARNm impliqués dans des processus reliés au développement tumoral et la résistance aux traitements possédant des structures secondaires G-quadruplexe dans leurs 5'UTR. Les données que nous avons générées suggèrent que hnRNP H et hnRNP F sont des régulateurs traductionnels essentiels au développement tumoral et à la résistance aux traitements des GBM
Glioblastoma multiforme (GBM) is one of the most aggressive brain tumors with poor prognosis. Understanding the molecular mechanisms involved in the development and resistance to treatments of gliomas could improve treatment efficiency. Recently, it has been demonstrated that translational regulations play a key role in the GBM aggressivity. RNA binding proteins (RBP) are major regulators of these processes and have altered expression / activity in GBM. The RBP hnRNP H and hnRNP F (HF) are among the most overexpressed RBP in GBM and their role in GBM translational regulation has never been investigated yet. We hypothesize that HF are at the core of a post-transcriptional regulation network which impacts the translational machinery that controls GBM tumor development and resistance to treatment. We have demonstrated that hnRNP H and hnRNP F regulate proliferation and response to treatment because their depletion (i) decreases the GBM proliferation (cell line model, spheroid and in vivo xenografts), (ii) activates the DNA damage response pathways and (iii) sensitizes the GBM cells to irradiation. We have identified HF as new regulators of GBM translation. Indeed, our data show that hnRNP H and hnRNP F control mRNA translation by regulating expression/activity of initiation factors and in collaboration with RNA helicases by targeting mRNA involved in oncogenic processes and containing secondary structures called G-quadruplex in their 5'UTR. The data that we have generated suggest that HF are essential translational regulators involved in tumor development and resistance to treatment in GBM
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Santerre, Maryline. "Étude de l'action sur l'épissage de protéines nucléaires se liant à la région de l'ARN du virus VIH-1 contenant le site d'épissage A7 et role de ces protéines sur d'autres sites accepteurs d'épissage de VIH-1." Thesis, Nancy 1, 2010. http://www.theses.fr/2010NAN10115/document.

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L'épissage est une étape clef de la multiplication du VIH-1. Par utilisation de 4 sites donneurs et 8 sites accepteurs d'épissage, plus de 40 ARNm différents sont produits. Une approche protéomique nous a permis d'identifier de nouvelles protéines interagissant avec la région de l'ARN viral contenant le site A7. Nous avons démontré l'interaction directe avec l'ARN viral de 5 des protéines identifiées (nucléoline, hnRNP A1/B, hnRNP H et hnRNP K). Nous avons montré que hnRNP K a plusieurs sites de fixation dans la région du site A7 et que hnRNP A1et hnRNP K se lient de façon coopérative. Nous avons montré un effet inhibiteur de hnRNP K sur l'épissage au site A7. Comme la protéine hnRNP A1 est un régulateur négatif de plusieurs sites accepteurs d'épissage (A1, A2, A3, A7), nous avons testé si la protéine hnRNP K pouvait renforcer l'inhibition à ces sites. En fait, hnRNP K active l'épissage in vitro des introns entre le site donneur D1 et les sites accepteurs A1, A2 et A3. Nous avons montré que la protéine hnRNP K renforce fortement l'activité de ASF/SF2 au site A2, ce qui indique que selon le contexte, la protéine hnRNP K peut être activatrice ou inhibitrice de l'épissage du VIH-1. J'ai observé de plus que la surexpression de la protéine hnRNP K dans des cellules HeLa, transfectées avec le plasmide p PSP contenant le virus VIH-1 dépourvu de ses capacités d'encapsidation, produit un changement très marqué de l'épissage alternatif de l'ARN PSP, ce qui confirme la forte influence de hnRNP K sur l'épissage alternatif du VIH-1. L'augmentation de la concentration cellulaire de hnRNP K dans les cellules HeLa conduit aussi à une diminution de la protéine virale Nef. La protéine hnRNP K intervient donc non seulement dans la régulation du site A7, mais aussi dans celle de la majorité des sites d'épissage régulés de l'ARN du VIH. L'action de cette protéine sur plusieurs des sites d'épissage montre que la protéine hnRNP K est probablement un régulateur général de l'épissage de VIH-1
HIV-1 pre-mRNA splicing depends upon 4 donor and 8 acceptor sites, which are used in combination to produce more than 40 different mRNAs. To further characterize nuclear factors involved in these processes, we purified RNP complexes formed by incubation of SLS2-A7 transcripts in HeLa cell nuclear extracts by affinity chromatography to identify new associated proteins. We showed that, in addition to the well known hnRNP A1 inhibitor of site A7, nucleolin, hnRNP H and hnRNP K interact directly with SLS2-A7 RNA. We demonstrated that hnRNP K has multiple binding sites in the vicinity of site A7 and that binds cooperatively to hnRNP A1 to the A7 RNA region and limits the A7 utilization in vitro. As hnRNP A1 is a negative regulator of several HIV-1 splicing sites (A1, A2, A3), we tested whether hnRNP K may also reinforce hnRNP A1 inhibition at these sites. Surprisingly, hnRNP K activated in vitro splicing of the D1-A1, D1-A2 and D1-A3 introns. Interestingly, hnRNP K was found to reinforce strongly the ASF/SF2 activity at site A2, which indicates that depending on the splicing site hnRNP K can be a splicing activator or inhibitor. To test how hnRNP K influences the relative utilization of HIV-1 splicing sites in cellulo, we used plasmid p PSP containing all the HIV-1 splicing sites and tested the effect of over-expression in HeLa cells on alternative splicing of the PSP RNA. Doubling the amount of hnRNP K in HeLa cells led to a drastic change of the PSP RNA alternative splicing, which confirms the strong influence of hnRNP K on alternative splicing. Moreover, increase of cellular concentration of hnRNP K strongly decrease the viral Nef protein production. hnRNP K protein affects A7 splicing regulation but also regulates the majority of regulated splicing sites of HIV. By extension of the study of hnRNP K effect to other HIV-1 splicing sites, we discovered that hnRNP K is a general regulator of HIV-1 splicing
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Paradis, Caroline. "Rôles de SRp30c et hnRNP I/PTB dans le contrôle de l'épissage alternatif du pré-ARN messager de hnRNP A1." Mémoire, Université de Sherbrooke, 2007. http://savoirs.usherbrooke.ca/handle/11143/3857.

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L'épissage alternatif des pré-ARN messagers est un mécanisme qui permet de générer une très grande diversité protéique chez les eucaryotes supérieurs. La sélection des sites d'épissage permet ainsi de produire certains isoformes protéiques plutôt que d'autres dans des conditions précises. Cette modulation implique généralement la participation d'une multitude de facteurs aux propriétés parfois synergiques et/ou antagonistes. Dans le cas du pré-ARN messager hnRNP A1, au moins trois éléments distincts renforcent l'exclusion de l'exon 7B. Par contre, l'élément intronique conservé de 38 nt (CE9) situé en aval de l'exon 7B permet la répression du site d'épissage 3', ce qui entraînerait l'inclusion de l'exon 7B. La portion 5' de l'élément CE9 est liée par la protéine SRp30c et cette interaction est importante pour permettre l'activité de CE9 in vitro. Afin de déterminer les composantes essentielles à l'activité de répression de SRp30c, des sites de liaison de haute affinité pour cette protéine ont été identifiés à l'aide de la procédure"SELEX". Les résultats obtenus indiquent que plusieurs sites de haute affinité reproduisent l'activité de l'élément CE9 complet dans un essai d'épissage où deux sites d'épissage 3' sont en compétition pour un seul site d'épissage 5'. De plus, les résultats suggèrent une contribution de la portion 3' de CE9, en plus de la partie 5', pour la liaison de la protéine SRp30c. En utilisant la séquence complète de CE9 pour effectuer une chromatographie d'affinité, la protéine hnRNP UPTB a été isolée et identifiée par spectrométrie de masse. Cependant, nous avons été surpris de constater que la protéine recombinante PTB agit comme activateur du site d'épissage 3' en diminuant l'activité de répression de CE9. Ces résultats suggèrent donc un nouveau rôle pour la protéine PTB, c'est-à-dire comme anti-répresseure de l'activité d'inhibition de SRp30c. PTB pourrait donc être un nouveau facteur capable de contrôler l'épissage alternatif du pré-ARN messager de hnfP A1.
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Söderberg, Malin. "Post-Transcriptional Regulation of the Murine Inducible Nitric Oxide Synthase Gene." Doctoral thesis, Uppsala University, Department of Pharmaceutical Biosciences, 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-6137.

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Large amounts of nitric oxide (NO) are produced by the inducible nitric oxide synthase (iNOS) upon inflammatory stimuli. NO is a multifaceted molecule, which may have beneficial effects as an antimicrobial agent in the immune defense, or cytotoxic effects in chronic inflammations, manifested as e.g. arthritis and asthma. Understanding the mode of regulation of the iNOS gene is a prerequisite for developing intervention strategies in various pathological conditions where detrimental effects of NO need to be prevented.

Transcriptional processes of the iNOS gene regulation are well described, while post-transcriptional events have not been studied in detail. The aim of the present thesis was to investigate post-transcriptional regulatory mechanisms involving the 3’untranslated region (UTR) of the murine iNOS mRNA.

Inflammation-dependent RNA-protein interactions with the iNOS mRNA 3’UTR were characterized by RNA gel shift analysis and UV cross-linking. Trans-acting factors interacting with the 3’UTR were detected in mouse liver and macrophages and identified as heterogeneous nuclear ribonucleoproteins (hnRNP) I and L. Western blot revealed that reduced hnRNPI levels are responsible for the decreased interaction of hnRNPI with iNOS 3’UTR upon induction in inflammatory conditions. This decrease was reversed by the glucocorticoid dexamethasone, concomitant with decreased iNOS mRNA levels and stability. Introduction of the iNOS 3’UTR into a luciferase reporter gene reduced its expression in macrophages. Upon deletions of the binding sites for hnRNPI and hnRNPL, the luciferase expression was recovered. In addition, inflammatory stimuli increased the luciferase activity of the construct with the full-length 3’UTR, while only weak effects of the stimuli were seen on the deletion constructs.

In conclusion, the results suggest that binding of hnRNPI and hnRNPL to the iNOS mRNA 3’UTR promotes degradation of the transcript. Induction of iNOS by inflammatory stimuli dissociates the RNA-protein complex, yielding a more stable mRNA. In addition, post-transcriptional down-regulation of the iNOS gene by the anti-inflammatory glucocorticoid dexamethasone, seems to involve hnRNPI.

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Books on the topic "HnRNPA1"

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Dugger, Sarah Anne. Evaluation of a precision medicine approach for hnRNP U-related developmental epileptic encephalopathy using a mouse model of disease. [New York, N.Y.?]: [publisher not identified], 2020.

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Jensen, Danielle Kristen. Degradation of multiple hnRNPs during apoptosis. 2010.

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Leser, George P. The immunological analysis of the major proteins associated with hnRNP. 1985.

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Book chapters on the topic "HnRNPA1"

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Berson, Amit, and Hermona Soreq. "HNRNPA1." In Encyclopedia of Signaling Molecules, 2407–15. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_101642.

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Berson, Amit, and Hermona Soreq. "HNRNPA1." In Encyclopedia of Signaling Molecules, 1–9. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_101642-1.

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Iwamoto, Ryo, Eisuke Mekada, Thomas G. Hofmann, Eva Krieghoff-Henning, Masaaki Kobayashi, Ken Takamatsu, Jennifer Defren, et al. "hnRNP D." In Encyclopedia of Signaling Molecules, 871. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_100621.

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Defren, Jennifer, and Gary Brewer. "hnRNP D (AUF1)." In Encyclopedia of Signaling Molecules, 2403–7. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_150.

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Iwamoto, Ryo, Eisuke Mekada, Thomas G. Hofmann, Eva Krieghoff-Henning, Masaaki Kobayashi, Ken Takamatsu, Jennifer Defren, et al. "hnRNP D (AUF1)." In Encyclopedia of Signaling Molecules, 872–76. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_150.

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Martinez-Contreras, Rebeca, Philippe Cloutier, Lulzim Shkreta, Jean-François Fisette, Timothée Revil, and Benoit Chabot. "hnRNP Proteins and Splicing Control." In Advances in Experimental Medicine and Biology, 123–47. New York, NY: Springer New York, 2007. http://dx.doi.org/10.1007/978-0-387-77374-2_8.

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Jung, Frank, Constantin E. Sekeris, and Johannes Schenkel. "Isolation and Immunochemical Characterization of hnRNP Particles." In RNP Particles, Splicing and Autoimmune Diseases, 1–28. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-80356-7_1.

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Zhang, Xuming, Christopher Lyle, Yicheng Wang, and Lin Zeng. "Role of hnRNP Al in Coronavirus RNA Synthesis." In Advances in Experimental Medicine and Biology, 437–46. Boston, MA: Springer US, 2001. http://dx.doi.org/10.1007/978-1-4615-1325-4_64.

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Michlewski, Gracjan, Sonia Guil, and Javier F. Cáceres. "Stimulation of pri-miR-18a Processing by hnRNP A1." In Advances in Experimental Medicine and Biology, 28–35. New York, NY: Springer US, 2010. http://dx.doi.org/10.1007/978-1-4419-7823-3_3.

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da Silva, Vinicius Barreto, Flavia Amoroso Matos e Silva, Cristiana Bernadelli Garcia, Andreia Machado Leopoldino, Carlos Henrique Tomich de Paula da Silva, and Carlton Anthony Taft. "Anticancer Lead Compounds that Prevent DNA Binding to hnRNP K." In Functional Properties of Advanced Engineering Materials and Biomolecules, 677–94. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-62226-8_23.

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Conference papers on the topic "HnRNPA1"

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Lampe, Sebastian, Thilo Brauß, Michael Kunze, Anica Scholz, Sofia Winslow, Bernhard Brüne, and Tobias Schmid. "Abstract B09: hnRNPA1 is a regulator of UNR IRES activity." In Abstracts: AACR Special Conference on Translational Control of Cancer: A New Frontier in Cancer Biology and Therapy; October 27-30, 2016; San Francisco, CA. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.transcontrol16-b09.

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Pham, Thao, Sophie Stempel, Mario Shields, Christina Spaulding, Krishan Kumar, David Bentrem, and Hidayatullah Munshi. "Abstract 2086: Targeting the MNK effector hnRNPA1 enhances the efficacy of BET inhibitors in cancer cells." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-2086.

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Pham, Thao, Sophie Stempel, Mario Shields, Christina Spaulding, Krishan Kumar, David Bentrem, and Hidayatullah Munshi. "Abstract 2086: Targeting the MNK effector hnRNPA1 enhances the efficacy of BET inhibitors in cancer cells." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-2086.

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Zhang, Hui, PamelaSara E. Head, Duc M. Duong, Nicholas T. Seyfried, and David S. Yu. "Abstract 3452: hnRNPUL1 regulation by ATR in DNA damage response." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-3452.

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Zhang, Hui, PamelaSara E. Head, Duc M. Duong, Nicholas T. Seyfried, and David S. Yu. "Abstract 3452: hnRNPUL1 regulation by ATR in DNA damage response." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-3452.

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Coyle, Krysta M., Quratulain Qureshi, Prasath Pararajalingam, Nicole Thomas, Timothy E. Audas, and Ryan D. Morin. "Abstract PO-04: Noncoding mutations in mantle cell lymphoma disrupt regulation of HNRNPH1 by alternative splicing." In Abstracts: AACR Virtual Meeting: Advances in Malignant Lymphoma; August 17-19, 2020. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/2643-3249.lymphoma20-po-04.

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Neckles, Carla, Robert Boer, Nicholas Aboreden, Robert L. Walker, Bong-Hyun Kim, Suntae Kim, John S. Schneekloth, and Natasha J. Caplen. "Abstract 4494: HNRNPH1-dependent splicing of a fusion oncogene reveals a targetable RNA G-quadruplex interaction." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4494.

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Neckles, Carla, Robert Boer, Nicholas Aboreden, Robert L. Walker, Bong-Hyun Kim, Suntae Kim, John S. Schneekloth, and Natasha J. Caplen. "Abstract 4494: HNRNPH1-dependent splicing of a fusion oncogene reveals a targetable RNA G-quadruplex interaction." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4494.

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Neckles, Carla, Robert E. Boer, Nicholas Aboreden, Allison M. Cross, Robert L. Walker, Bong-Hyun Kim, Suntae Kim, John S. Schneekloth, and Natasha J. Caplen. "Abstract B25: HNRNPH1-dependent splicing of the fusion oncogene EWS-FLI1 reveals a targetable RNA G-quadruplex interaction." In Abstracts: AACR Special Conference on the Advances in Pediatric Cancer Research; September 17-20, 2019; Montreal, QC, Canada. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.pedca19-b25.

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Chen, Tsung-Ming, Ming-Chih Lai, Yi-Han Li, Shaw-Jenq Tsai, and H. Sunny Sun. "Abstract LB-205: hnRNPM-IRES-mediated translation promotes colon cancer tumorigenesis." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-lb-205.

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