Relevant bibliographies by topics / HnRNP E1

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  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'HnRNP E1'

Author: Grafiati
Published: 4 June 2021
Last updated: 12 February 2022

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Journal articles on the topic "HnRNP E1"

1

Choi, Mie-Young. "Cloning of hnRNP E1 cDNA via yeast two-hybrid system and a study on protein-protein interaction between hnRNP E1 and hnRNP K." Journal of the Korea Academia-Industrial cooperation Society 9, no. 6 (2008): 1795–99. http://dx.doi.org/10.5762/kais.2008.9.6.1795.

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Kosturko, Linda D., Michael J. Maggipinto, George Korza, Joo Won Lee, John H. Carson, and Elisa Barbarese. "Heterogeneous Nuclear Ribonucleoprotein (hnRNP) E1 Binds to hnRNP A2 and Inhibits Translation of A2 Response Element mRNAs." Molecular Biology of the Cell 17, no. 8 (2006): 3521–33. http://dx.doi.org/10.1091/mbc.e05-10-0946.

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Heterogeneous nuclear ribonucleoprotein (hnRNP) A2 is a trans-acting RNA-binding protein that mediates trafficking of RNAs containing the cis-acting A2 response element (A2RE). Previous work has shown that A2RE RNAs are transported to myelin in oligodendrocytes and to dendrites in neurons. hnRNP E1 is an RNA-binding protein that regulates translation of specific mRNAs. Here, we show by yeast two-hybrid analysis, in vivo and in vitro coimmunoprecipitation, in vitro cross-linking, and fluorescence correlation spectroscopy that hnRNP E1 binds to hnRNP A2 and is recruited to A2RE RNA in an hnRNP A
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3

Mohanty, Bidyut K., Joseph AQ Karam, Breege V. Howley, et al. "Heterogeneous nuclear ribonucleoprotein E1 binds polycytosine DNA and monitors genome integrity." Life Science Alliance 4, no. 9 (2021): e202000995. http://dx.doi.org/10.26508/lsa.202000995.

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Heterogeneous nuclear ribonucleoprotein E1 (hnRNP E1) is a tumor suppressor protein that binds site- and structure-specifically to RNA sequences to regulate mRNA stability, facilitate alternative splicing, and suppress protein translation on several metastasis-associated mRNAs. Here, we show that hnRNP E1 binds polycytosine-rich DNA tracts present throughout the genome, including those at promoters of several oncogenes and telomeres and monitors genome integrity. It binds DNA in a site- and structure-specific manner. hnRNP E1-knockdown cells displayed increased DNA damage signals including γ-H
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Ostareck-Lederer, Antje, Dirk H. Ostareck, Christophe Cans, et al. "c-Src-Mediated Phosphorylation of hnRNP K Drives Translational Activation of Specifically Silenced mRNAs." Molecular and Cellular Biology 22, no. 13 (2002): 4535–43. http://dx.doi.org/10.1128/mcb.22.13.4535-4543.2002.

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ABSTRACT hnRNPK and hnRNP E1/E2 mediate translational silencing of cellular and viral mRNAs in a differentiation-dependent way by binding to specific regulatory sequences. The translation of 15-lipoxygenase (LOX) mRNA in erythroid precursor cells and of the L2 mRNA of human papilloma virus type 16 (HPV-16) in squamous epithelial cells is silenced when either of these cells is immature and is activated in maturing cells by unknown mechanisms. Here we address the question of how the silenced mRNA can be translationally activated. We show that hnRNP K and the c-Src kinase specifically interact wi
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5

Han, Sun‐Young, and Mieyoung Choi. "Human ribosomal protein L18a interacts with hnRNP E1." Animal Cells and Systems 12, no. 3 (2008): 143–48. http://dx.doi.org/10.1080/19768354.2008.9647167.

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Chaudhury, A., P. Chander, and P. H. Howe. "Heterogeneous nuclear ribonucleoproteins (hnRNPs) in cellular processes: Focus on hnRNP E1's multifunctional regulatory roles." RNA 16, no. 8 (2010): 1449–62. http://dx.doi.org/10.1261/rna.2254110.

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7

Brown, Andrew S., Bidyut K. Mohanty, and Philip H. Howe. "Identification and characterization of an hnRNP E1 translational silencing motif." Nucleic Acids Research 44, no. 12 (2016): 5892–907. http://dx.doi.org/10.1093/nar/gkw241.

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8

Tang, Ying-Sheng, Rehana A. Khan, Yonghua Zhang, et al. "Incrimination of Heterogeneous Nuclear Ribonucleoprotein E1 (hnRNP-E1) as a Candidate Sensor of Physiological Folate Deficiency." Journal of Biological Chemistry 286, no. 45 (2011): 39100–39115. http://dx.doi.org/10.1074/jbc.m111.230938.

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9

Ajiro, Masahiko, Shuang Tang, John Doorbar, and Zhi-Ming Zheng. "Serine/Arginine-Rich Splicing Factor 3 and Heterogeneous Nuclear Ribonucleoprotein A1 Regulate Alternative RNA Splicing and Gene Expression of Human Papillomavirus 18 through Two Functionally DistinguishablecisElements." Journal of Virology 90, no. 20 (2016): 9138–52. http://dx.doi.org/10.1128/jvi.00965-16.

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ABSTRACTHuman papillomavirus 18 (HPV18) is the second most common oncogenic HPV type associated with cervical, anogenital, and oropharyngeal cancers. Like other oncogenic HPVs, HPV18 encodes two major (one early and one late) polycistronic pre-mRNAs that are regulated by alternative RNA splicing to produce a repertoire of viral transcripts for the expression of individual viral genes. However, RNAcis-regulatory elements andtrans-acting factors contributing to HPV18 alternative RNA splicing remain unknown. In this study, an exonic splicing enhancer (ESE) in the nucleotide (nt) 3520 to 3550 regi
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10

Link, Laura A., Breege V. Howley, George S. Hussey, and Philip H. Howe. "PCBP1/HNRNP E1 Protects Chromosomal Integrity by Translational Regulation of CDC27." Molecular Cancer Research 14, no. 7 (2016): 634–46. http://dx.doi.org/10.1158/1541-7786.mcr-16-0018.

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Dissertations / Theses on the topic "HnRNP E1"

1

Schwartz, Laura Link. "HnRNP E1 Protects Chromosomal Stability Through Post-Transcriptional Regulation of Cdc27 Expression." Kent State University / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=kent1445519325.

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Brown, Andrew S. "Identification of a phospho-hnRNP E1 Nucleic Acid Consensus Sequence Mediating Epithelial to Mesenchymal Transition." Kent State University / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=kent1437943957.

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Chaudhury, Arindam. "Transforming Growth Factor-Beta (TGFΒ)-Mediated Post-Transcriptional Regulation of Epithelial-Mesenchymal Transdifferentiation (EMT)". Cleveland State University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=csu1268963035.

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Thornbury, Mackenzie. "The role of poly(C)-binding protein 1 in HSV-1 Infection." Thesis, 2020. http://hdl.handle.net/1866/25195.

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Lors de l'infection par le virus herpès simplex de type 1 (VHS-1), quatre types de capsides nucléaires sont créés : les procapsides et les capsides A, B, et C. Sur les quatre capsides, seules les capsides C contiennent de l'ADN viral et deviendront des particules infectieuses. Un niveau de régulation se produit lors de la sortie du noyau qui favorise la sortie d’es capsides C du noyau. Le mécanisme qui sous-tend ce phénomène est actuellement inconnu. Les recherches actuelles suggèrent que l'interaction entre la protéine virale pUL25 modifie la conformation de la couche hexamérique plane du com
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Journal articles
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