Relevant bibliographies by topics / TCF11/Nrf1

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  1. Journal articles
  2. Dissertations / Theses
  3. Conference papers

Academic literature on the topic 'TCF11/Nrf1'

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

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Journal articles on the topic "TCF11/Nrf1"

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Fassmannová, Dominika, František Sedlák, Jindřich Sedláček, Ivan Špička, and Klára Grantz Šašková. "Nelfinavir Inhibits the TCF11/Nrf1-Mediated Proteasome Recovery Pathway in Multiple Myeloma." Cancers 12, no. 5 (2020): 1065. http://dx.doi.org/10.3390/cancers12051065.

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Proteasome inhibitors are the backbone of multiple myeloma therapy. However, disease progression or early relapse occur due to development of resistance to the therapy. One important cause of resistance to proteasome inhibition is the so-called bounce-back response, a recovery pathway driven by the TCF11/Nrf1 transcription factor, which activates proteasome gene re-synthesis upon impairment of the proteasome function. Thus, inhibiting this recovery pathway potentiates the cytotoxic effect of proteasome inhibitors and could benefit treatment outcomes. DDI2 protease, the 3D structure of which re
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Sotzny, Franziska, Eileen Schormann, Ina Kühlewindt, et al. "TCF11/Nrf1-Mediated Induction of Proteasome Expression Prevents Cytotoxicity by Rotenone." Antioxidants & Redox Signaling 25, no. 16 (2016): 870–85. http://dx.doi.org/10.1089/ars.2015.6539.

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Johnsen, O. "Small Maf proteins interact with the human transcription factor TCF11/Nrf1/LCR-F1." Nucleic Acids Research 24, no. 21 (1996): 4289–97. http://dx.doi.org/10.1093/nar/24.21.4289.

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Myhrstad, Mari C. W., Cathrine Husberg, Paula Murphy та ін. "TCF11/Nrf1 overexpression increases the intracellular glutathione level and can transactivate the γ-glutamylcysteine synthetase (GCS) heavy subunit promoter". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression 1517, № 2 (2001): 212–19. http://dx.doi.org/10.1016/s0167-4781(00)00276-1.

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Johnsen, O., P. Murphy, H. Prydz, and A. B. Kolsto. "Interaction of the CNC-bZIP factor TCF11/LCR-F1/Nrf1 with MafG: Binding-site selection and regulation of transcription." Nucleic Acids Research 26, no. 2 (1998): 512–20. http://dx.doi.org/10.1093/nar/26.2.512.

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Nowak, Karolin, Ramona M. Taubert, Stefanie Haberecht, Simone Venz, and Elke Krüger. "Inhibition of calpain-1 stabilizes TCF11/Nrf1 but does not affect its activation in response to proteasome inhibition." Bioscience Reports 38, no. 5 (2018). http://dx.doi.org/10.1042/bsr20180393.

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Protein degradation is essential to compensate for the damaging effects of proteotoxic stress. To ensure protein and redox homeostasis in response to proteasome inhibition, the cleavage and nuclear translocation of the endoplasmic reticulum (ER)-bound transcription factor TCF11/Nrf1 (NFE2L1) is crucial for the activation of rescue factors including the synthesis of new proteasomal subunits. Even though TCF11/Nrf1 is an essential transcription factor, the exact mechanisms by which it is activated and stabilized are not fully understood. It was previously shown that the calcium-dependent proteas
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Wang, Meng, Yonggang Ren, Shaofan Hu, Keli Liu, Lu Qiu та Yiguo Zhang. "TCF11 Has a Potent Tumor-Repressing Effect Than Its Prototypic Nrf1α by Definition of Both Similar Yet Different Regulatory Profiles, With a Striking Disparity From Nrf2". Frontiers in Oncology 11 (29 червня 2021). http://dx.doi.org/10.3389/fonc.2021.707032.

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Nrf1 and Nrf2, as two principal CNC-bZIP transcription factors, regulate similar but different targets involved in a variety of biological functions for maintaining cell homeostasis and organ integrity. Of note, the unique topobiological behavior of Nrf1 makes its functions more complicated than Nrf2, because it is allowed for alternatively transcribing and selectively splicing to yield multiple isoforms (e.g., TCF11, Nrf1α). In order to gain a better understanding of their similarities and differences in distinct regulatory profiles, all four distinct cell models for stably expressing TCF11,
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Dissertations / Theses on the topic "TCF11/Nrf1"

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Sotzny, Franziska. "Regulation des Ubiquitin-Proteasom-Systems unter proteotoxischem Stress." Doctoral thesis, Humboldt-Universität zu Berlin, Lebenswissenschaftliche Fakultät, 2016. http://dx.doi.org/10.18452/17599.

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Das Ubiquitin-Proteasom-System (UPS) stellt eines der wichtigsten zellulären Abbausysteme dar. Es vermittelt die Degradation fehlgefalteter, beschädigter sowie regulatorischer Proteine. Folglich ist es essentiell für die Proteinqualitätskontrolle und für eine Vielzahl zellulärer Prozesse. Eine Störung des UPS steht im engen Zusammenhang mit neurodegenerativen Erkrankungen und malignen Tumoren. Adaptive Mechanismen ermöglichen es der Zelle das UPS an den stetig schwankenden Bedarf proteolytischer Aktivität anzupassen. So wirkt eine erhöhte Expression proteasomaler Gene einem Abfall der proteaso
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Conference papers on the topic "TCF11/Nrf1"

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Cuevas Mora, K., D. Sales, W. Roque, and F. Romero. "TCF11/Nrf1-Mediated Activation of Proteasome Expression Is Compromised in Chronically Injured Alveolar Epithelial Cells and Aged-Related Lung Fibrosis." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a4393.

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