Relevant bibliographies by topics / RNA-Binding Protein FUS

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Academic literature on the topic 'RNA-Binding Protein FUS'

Author: Grafiati
Published: 4 June 2021
Last updated: 26 July 2025

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Journal articles on the topic "RNA-Binding Protein FUS"

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Yoneda, Ryoma, Naomi Ueda, and Riki Kurokawa. "m6A Modified Short RNA Fragments Inhibit Cytoplasmic TLS/FUS Aggregation Induced by Hyperosmotic Stress." International Journal of Molecular Sciences 22, no. 20 (2021): 11014. http://dx.doi.org/10.3390/ijms222011014.

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Translocated in LipoSarcoma/Fused in Sarcoma (TLS/FUS) is a nuclear RNA binding protein whose mutations cause amyotrophic lateral sclerosis. TLS/FUS undergoes LLPS and forms membraneless particles with other proteins and nucleic acids. Interaction with RNA alters conformation of TLS/FUS, which affects binding with proteins, but the effect of m6A RNA modification on the TLS/FUS–RNA interaction remains elusive. Here, we investigated the binding specificity of TLS/FUS to m6A RNA fragments by RNA pull down assay, and elucidated that both wild type and ALS-related TLS/FUS mutants strongly bound to
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Sévigny, Myriam, Isabelle Bourdeau Julien, Janani Priya Venkatasubramani, Jeremy B. Hui, Paul A. Dutchak, and Chantelle F. Sephton. "FUS contributes to mTOR-dependent inhibition of translation." Journal of Biological Chemistry 295, no. 52 (2020): 18459–73. http://dx.doi.org/10.1074/jbc.ra120.013801.

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The amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD)–linked RNA-binding protein called FUS (fused in sarcoma) has been implicated in several aspects of RNA regulation, including mRNA translation. The mechanism by which FUS affects the translation of polyribosomes has not been established. Here we show that FUS can associate with stalled polyribosomes and that this association is sensitive to mTOR (mammalian target of rapamycin) kinase activity. Specifically, we show that FUS association with polyribosomes is increased by Torin1 treatment or when cells are cultured in nutri
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Schwartz, Jacob C., Elaine R. Podell, Steve S. W. Han, James D. Berry, Kevin C. Eggan, and Thomas R. Cech. "FUS is sequestered in nuclear aggregates in ALS patient fibroblasts." Molecular Biology of the Cell 25, no. 17 (2014): 2571–78. http://dx.doi.org/10.1091/mbc.e14-05-1007.

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Mutations in the RNA-binding protein FUS have been shown to cause the neurodegenerative disease amyotrophic lateral sclerosis (ALS). We investigate whether mutant FUS protein in ALS patient–derived fibroblasts affects normal FUS functions in the nucleus. We investigated fibroblasts from two ALS patients possessing different FUS mutations and a normal control. Fibroblasts from these patients have their nuclear FUS protein trapped in SDS-resistant aggregates. Genome-wide analysis reveals an inappropriate accumulation of Ser-2 phosphorylation on RNA polymerase II (RNA Pol II) near the transcripti
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Tyzack, Giulia E., Raphaelle Luisier, Doaa M. Taha, et al. "Widespread FUS mislocalization is a molecular hallmark of amyotrophic lateral sclerosis." Brain 142, no. 9 (2019): 2572–80. http://dx.doi.org/10.1093/brain/awz217.

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Abstract Mutations causing amyotrophic lateral sclerosis (ALS) clearly implicate ubiquitously expressed and predominantly nuclear RNA binding proteins, which form pathological cytoplasmic inclusions in this context. However, the possibility that wild-type RNA binding proteins mislocalize without necessarily becoming constituents of cytoplasmic inclusions themselves remains relatively unexplored. We hypothesized that nuclear-to-cytoplasmic mislocalization of the RNA binding protein fused in sarcoma (FUS), in an unaggregated state, may occur more widely in ALS than previously recognized. To addr
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Li, Yun R., Oliver D. King, James Shorter, and Aaron D. Gitler. "Stress granules as crucibles of ALS pathogenesis." Journal of Cell Biology 201, no. 3 (2013): 361–72. http://dx.doi.org/10.1083/jcb.201302044.

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Amyotrophic lateral sclerosis (ALS) is a fatal human neurodegenerative disease affecting primarily motor neurons. Two RNA-binding proteins, TDP-43 and FUS, aggregate in the degenerating motor neurons of ALS patients, and mutations in the genes encoding these proteins cause some forms of ALS. TDP-43 and FUS and several related RNA-binding proteins harbor aggregation-promoting prion-like domains that allow them to rapidly self-associate. This property is critical for the formation and dynamics of cellular ribonucleoprotein granules, the crucibles of RNA metabolism and homeostasis. Recent work co
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Arenas, Alexandra, Jing Chen, Lisha Kuang, et al. "Lysine acetylation regulates the RNA binding, subcellular localization and inclusion formation of FUS." Human Molecular Genetics 29, no. 16 (2020): 2684–97. http://dx.doi.org/10.1093/hmg/ddaa159.

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Abstract Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease characterized by the preferential death of motor neurons. Approximately 10% of ALS cases are familial and 90% are sporadic. Fused in sarcoma (FUS) is a ubiquitously expressed RNA-binding protein implicated in familial ALS and frontotemporal dementia (FTD). The physiological function and pathological mechanism of FUS are not well understood, particularly whether post-translational modifications play a role in regulating FUS function. In this study, we discovered that FUS was acetylated at lysine-315/316 (K315/K316) and
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Yasuda, Kyota, Huaye Zhang, David Loiselle, Timothy Haystead, Ian G. Macara, and Stavroula Mili. "The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules." Journal of Cell Biology 203, no. 5 (2013): 737–46. http://dx.doi.org/10.1083/jcb.201306058.

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RNA localization pathways direct numerous mRNAs to distinct subcellular regions and affect many physiological processes. In one such pathway the tumor-suppressor protein adenomatous polyposis coli (APC) targets RNAs to cell protrusions, forming APC-containing ribonucleoprotein complexes (APC-RNPs). Here, we show that APC-RNPs associate with the RNA-binding protein Fus/TLS (fused in sarcoma/translocated in liposarcoma). Fus is not required for APC-RNP localization but is required for efficient translation of associated transcripts. Labeling of newly synthesized proteins revealed that Fus promot
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Korobeynikov, Vladislav A., Alexander K. Lyashchenko, Beatriz Blanco-Redondo, Paymaan Jafar-Nejad, and Neil A. Shneider. "Antisense oligonucleotide silencing of FUS expression as a therapeutic approach in amyotrophic lateral sclerosis." Nature Medicine 28, no. 1 (2022): 104–16. http://dx.doi.org/10.1038/s41591-021-01615-z.

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AbstractFused in sarcoma (FUS) is an RNA-binding protein that is genetically and pathologically associated with rare and aggressive forms of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). To explore the mechanisms by which mutant FUS causes neurodegeneration in ALS-FTD, we generated a series of FUS knock-in mouse lines that express the equivalent of ALS-associated mutant FUSP525L and FUSΔEX14 protein. In FUS mutant mice, we show progressive, age-dependent motor neuron loss as a consequence of a dose-dependent gain of toxic function, associated with the insolubility of F
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Sukhanova, Maria V., Anastasia S. Singatulina, David Pastré, and Olga I. Lavrik. "Fused in Sarcoma (FUS) in DNA Repair: Tango with Poly(ADP-ribose) Polymerase 1 and Compartmentalisation of Damaged DNA." International Journal of Molecular Sciences 21, no. 19 (2020): 7020. http://dx.doi.org/10.3390/ijms21197020.

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The fused in sarcoma (FUS) protein combines prion-like properties with a multifunctional DNA/RNA-binding domain and has functions spanning the regulation of RNA metabolism, including transcription, pre-mRNA splicing, mRNA transport and translation. In addition to its roles in RNA metabolism, FUS is implicated in the maintenance of DNA integrity. In this review, we examine the participation of FUS in major DNA repair pathways, focusing on DNA repair associated with poly(ADP-ribosyl)ation events and on how the interaction of FUS with poly(ADP-ribose) may orchestrate transient compartmentalisatio
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Humphrey, Jack, Nicol Birsa, Carmelo Milioto, et al. "FUS ALS-causative mutations impair FUS autoregulation and splicing factor networks through intron retention." Nucleic Acids Research 48, no. 12 (2020): 6889–905. http://dx.doi.org/10.1093/nar/gkaa410.

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Abstract Mutations in the RNA-binding protein FUS cause amyotrophic lateral sclerosis (ALS), a devastating neurodegenerative disease. FUS plays a role in numerous aspects of RNA metabolism, including mRNA splicing. However, the impact of ALS-causative mutations on splicing has not been fully characterized, as most disease models have been based on overexpressing mutant FUS, which will alter RNA processing due to FUS autoregulation. We and others have recently created knockin models that overcome the overexpression problem, and have generated high depth RNA-sequencing on FUS mutants in parallel
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Dissertations / Theses on the topic "RNA-Binding Protein FUS"

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Bourdeau-Julien, Isabelle. "ALS-associated RNA-binding protein FUS and mRNA translation regulation." Master's thesis, Université Laval, 2020. http://hdl.handle.net/20.500.11794/68742.

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Des mutations dans plusieurs gènes ont été liés à la sclérose latérale amyotrophique (SLA),en particulier dans celui codant pour la protéine Fused in Sarcoma (FUS). Les mutations sont retrouvées dans la partie codant pour le signal de localisation nucléaire, rendant la protéine anormalement abondante dans le cytoplasme. Combiné à d’autres observations, ça suggère qu’un gain de fonction toxique de FUS dans le cytoplasme serait à l’origine de la neurodégénérescence. La SLA est une maladie neurodégénérative qui affecte les neurones moteurs et cause une paralysie progressive. Les mécanismes molécu
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Culley, Rachel Louise. "The role of the RNA binding protein FUS in androgen signalling." Thesis, Imperial College London, 2012. http://hdl.handle.net/10044/1/14613.

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The multi-functional RNA binding protein FUS was identified as an androgen down-regulated target in a 2D proteomic screen in the LNCaP cell line. This screen was designed to identify novel markers and therapeutic targets for prostate cancer. Cell cycle analysis and growth assays revealed that increased FUS levels in LNCaP cells resulted in inhibition of the androgen-dependent G1-S cell cycle transition and induced apoptosis. This is brought about, in part, via the FUS-dependent modulation of the expression of G1- S check-point regulatory proteins, including decreased expression of Cyclin D1. T
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Kamelgarn, Marisa Elizabeth. "MUTATIONS OF FUS CAUSE AGGREGATION OF RNA BINDING PROTEINS, DISRUPTIONS IN PROTEIN SYNTHESIS, AND DYSREGULATION OF NONSENSE MEDIATED DECAY." UKnowledge, 2019. https://uknowledge.uky.edu/toxicology_etds/27.

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Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by motor neuron death and subsequent muscle atrophy. Approximately 15% of ALS cases are inheritable, and mutations in the Fused in Sarcoma (FUS) gene contribute to approximately 5% of these cases, as well as about 2% of sporadic cases. FUS performs a diverse set of cellular functions, including being a major regulator of RNA metabolism. FUS undergoes liquid- liquid phase transition in vitro, allowing for its participation in stress granules and RNA transport granules. Phase transition also contributes to the
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Sama, Reddy Ranjith Kumar. "FUS/TLS in Stress Response - Implications for Amyotrophic Lateral Sclerosis: A Dissertation." eScholarship@UMMS, 2014. http://escholarship.umassmed.edu/gsbs_diss/704.

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Amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig’s disease is a fatal neurodegenerative disease. ALS is typically adult onset and is characterized by rapidly progressive loss of both upper and lower motor neurons that leads to death usually within 3-5 years. About 90% of all the cases are sporadic with no family history while the remaining 10% are familial cases with mutations in several genes including SOD1, FUS/TLS, TDP43 and C9ORF72. FUS/TLS (Fused in Sarcoma/Translocated in Liposarcoma or FUS) is an RNA/DNA binding protein that is involved in multiple cellular functions includ
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Lin, Yen-Chen. "Lost in Nucleocytoplasmic Transportation: New Insights Into FUS-Mediated Neurodegeneration." eScholarship@UMMS, 2020. https://escholarship.umassmed.edu/gsbs_diss/1107.

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Nucleocytoplasmic transport (NCT) declines during aging and in the context of age-dependent neurodegenerative diseases. However, the mechanisms underlying NCT decline in the disease are poorly understood. FUS is an RNA binding protein that shuttles between the nucleus and cytoplasm and is actively involved in NCT. Mutations in FUS cause amyotrophic lateral sclerosis (ALS), a fatal and incurable motor neuron disorder. We sought to understand the disease mechanism underlying FUS-induced NCT decline in ALS. Here, I uncovered NCT-related defects in motor neurons derived from human induced pluripot
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Schön, Michael [Verfasser]. "Analysis of the synaptic localization of the FUS RNA-binding protein with high- and super-resolution microscopy / Michael Schön." Ulm : Universität Ulm, 2018. http://d-nb.info/1162953934/34.

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Ko, Hae Kyung. "Exploring the Role of FUS Mutants from Stress Granule Incorporation to Nucleopathy in Amyotrophic Lateral Sclerosis: A Dissertation." eScholarship@UMMS, 2015. https://escholarship.umassmed.edu/gsbs_diss/799.

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Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease characterized by preferential motor neuron death in the brain and spinal cord. The rapid disease progression results in death due to respiratory failure, typically within 3-5 years after disease onset. While ~90% of cases occur sporadically, remaining 10% of ALS cases show familial inheritance, and the number of genes linked to ALS has increased dramatically over the past decade. FUS/TLS (Fused in Sarcoma/ Translocated to liposarcoma) is a nucleic acid binding protein that may regulate several cellular functions, in
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Ward, Catherine L. "The Cellular Consequences of FUS/TLS Depletion: A Loss of Function Model for Amyotrophic Lateral Sclerosis: A Dissertation." eScholarship@UMMS, 2014. https://escholarship.umassmed.edu/gsbs_diss/738.

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Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the death of motor neurons, generally leading to paralysis and death within 3-5 years of onset. Over 50 different mutations in the gene encoding FUS/TLS (or FUS) will result in ALS, accounting for ~4% of all inherited cases. FUS is a multifunctional protein with important functions in DNA/RNA processing and stress response. How these mutations affect the structure or function of FUS protein and ultimately cause ALS is not known. The fact that mutations cause the protein to mislocalize from the nucleus to
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Ward, Catherine L. "The Cellular Consequences of FUS/TLS Depletion: A Loss of Function Model for Amyotrophic Lateral Sclerosis: A Dissertation." eScholarship@UMMS, 2007. http://escholarship.umassmed.edu/gsbs_diss/738.

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Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease characterized by the death of motor neurons, generally leading to paralysis and death within 3-5 years of onset. Over 50 different mutations in the gene encoding FUS/TLS (or FUS) will result in ALS, accounting for ~4% of all inherited cases. FUS is a multifunctional protein with important functions in DNA/RNA processing and stress response. How these mutations affect the structure or function of FUS protein and ultimately cause ALS is not known. The fact that mutations cause the protein to mislocalize from the nucleus to
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Ko, Hae Kyung. "Exploring the Role of FUS Mutants from Stress Granule Incorporation to Nucleopathy in Amyotrophic Lateral Sclerosis: A Dissertation." eScholarship@UMMS, 2009. http://escholarship.umassmed.edu/gsbs_diss/799.

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Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease characterized by preferential motor neuron death in the brain and spinal cord. The rapid disease progression results in death due to respiratory failure, typically within 3-5 years after disease onset. While ~90% of cases occur sporadically, remaining 10% of ALS cases show familial inheritance, and the number of genes linked to ALS has increased dramatically over the past decade. FUS/TLS (Fused in Sarcoma/ Translocated to liposarcoma) is a nucleic acid binding protein that may regulate several cellular functions, in
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Books on the topic "RNA-Binding Protein FUS"

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Tsai, Yueh-Lin. Function and Regulation of ALS/FTD-associated RNA Binding Protein FUS. [publisher not identified], 2021.

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Bagni, Claudia, and Eric Klann. Molecular Functions of the Mammalian Fragile X Mental Retardation Protein: Insights Into Mental Retardation and Synaptic Plasticity. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199744312.003.0008.

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Chapter 8 discusses how Fragile X syndrome (FXS) is caused by the absence of the RNA-binding protein fragile X mental retardation protein (FMRP). FMRP is highly expressed in the brain and gonads, the two organs mainly affected in patients with the syndrome. Functionally, FMRP belongs to the family of RNA-binding proteins, shuttling from the nucleus to the cytoplasm, and, as shown for other RNA-binding proteins, forms large messenger ribonucleoparticles.
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Book chapters on the topic "RNA-Binding Protein FUS"

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Muthuramalingam, Akila, Ashok Kumar Pandurangan, and Subhamoy Banerjee. "Role of Cannabinoids in the Regulation of Amyotrophic Lateral Sclerosis (ALS)." In Medical Cannabis and the Effects of Cannabinoids on Fighting Cancer, Multiple Sclerosis, Epilepsy, Parkinson's, and Other Neurodegenerative Diseases. IGI Global, 2022. http://dx.doi.org/10.4018/978-1-6684-5652-1.ch007.

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Amyotrophic lateral sclerosis (ALS) is a degenerative disease that manifests in older adults as a result of death of motor neurons. Incidence is 60-80% sporadic and 10-20% familial. The most common mutations are SOD-1, TARDBP, and FUS. Abnormal protein aggregation, inflammation, and dysfunction of RNA are seen. Tremors, dyslexia, and inability to walk progress to death. No cure is available to date. Medical cannabis may delay ALS progression by its neuroprotective, antioxidant, and anti-inflammatory properties. This chapter examines the effects of cannabinoids in ALS and discusses their mechan
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"The Functions of Glycine-Rich Regions in TDP-43, FUS and Related RNA-Binding Proteins." In RNA Binding Proteins. CRC Press, 2012. http://dx.doi.org/10.1201/9781498713368-9.

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Hamamura, Mitsuko, Gareth Leng, Piers C. Emson, and Hiroshi Kiyama. "c-fos mRNA in oxytocin neurons: selective induction by CCK." In Multiple Cholecystokinin Receptors in the CNS. Oxford University PressOxford, 1992. http://dx.doi.org/10.1093/oso/9780198577560.003.0030.

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Abstract The magnocellular neurosecretory system of the rat hypothalamus has long been considered to be an excellent model for the study of mammalian peptidergic neurons. The magnocellular neurons are confined to relatively homogenous nuclei within the hypothalamus- the supra-optic nucleus (SON) and the paraventricular nucleus (PVN)- and the neuronal cell bodies are separated anatomically from the nerve terminals that are present at the site of neurosecretion in the neural lobe of the pituitary (Sofroniew 1983). The outputs of these neurons are the hormones oxytocin and vasopressin, the concen
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Conference papers on the topic "RNA-Binding Protein FUS"

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Brooke, GN, CL Bevan, B. Rudraraju, and C. Palmieri. "P5-06-06: The RNA Binding Protein FUS Is a Potential Marker for Breast Cancer Progression and Therapy Response." In Abstracts: Thirty-Fourth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 6‐10, 2011; San Antonio, TX. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/0008-5472.sabcs11-p5-06-06.

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Singatulina, A. S., M. V. Sukhanova, and O. I. Lavrik. "FACTOR HPF1 REGULATES THE ACTIVITY OF POLY(ADP-RIBOSE)POLYMERASES 1 AND 2 AND THE FORMATION OF POLY(ADP-RIBOSE)-CONTAINING COMPARTMENTS WITH THE PARTICIPATION OF THE RNA-BINDING PROTEIN FUS." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-281.

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Poly(ADP-ribose) polymerases 1 and 2 (PARP1/2) synthesize poly(ADP-ribose) (PAR) by covalently modifying a number of proteins involved in DNA/RNA metabolism, including themselves. PARP1/2 are key regulators of DNA repair via autopoly(ADP-ribosyl)ation at the site of DNA damage. The study of factors that modulate PARP1/2 activity in response to genotoxic stress is an important task in modern biology.
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