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Dissertations / Theses on the topic 'RNA-Binding Protein FUS'

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Published: 4 June 2021
Last updated: 26 July 2025

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Singatulina, Anastasiya. "The link between PARP1-mediated signaling and RNA-binding protein FUS in response to DNA damage PARP-1 Activation Directs FUS to DNA Damage Sites to Form PARG-Reversible Compartments Enriched in Damaged DNA." Thesis, Université Paris-Saclay (ComUE), 2019. http://www.theses.fr/2019SACLE042.

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La stabilité du génome est contrôlée par une machinerie complexe qui répare les dommages causés à l'ADN, le principal responsable du cancer et des maladies associées au vieillissement. En effet, Les cellules humaines sont exposées à différentes sources de stress oxydatif qui entraînent des dommages de l'ADN, notamment les cassures simple brin et les cassures double brin. Les sources de cassures de l’ADN peuvent être exogènes (lumière ultraviolette, pollution, rayonnements ionisants) ou endogènes (métabolisme cellulaire et inflammation). Après un stress génotoxique, les cellules de mammifères d
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12

Kaushansky, Laura J. "Investigating the Effects of Mutant FUS on Stress Response in Amyotrophic Lateral Sclerosis: A Thesis." eScholarship@UMMS, 2015. https://escholarship.umassmed.edu/gsbs_diss/792.

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During stress, eukaryotes regulate protein synthesis in part through formation of cytoplasmic, non-membrane-bound complexes called stress granules (SGs). SGs transiently store signaling proteins and stalled translational complexes in response to stress stimuli (e.g. oxidative insult, DNA damage, temperature shifts and ER dysfunction). The functional outcome of SGs is proper translational regulation and signaling, allowing cells to overcome stress. The fatal motor neuron disease Amyotrophic Lateral Sclerosis (ALS) develops in an age-related manner and is marked by progressive neuronal death, wi
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13

Kaushansky, Laura J. "Investigating the Effects of Mutant FUS on Stress Response in Amyotrophic Lateral Sclerosis: A Thesis." eScholarship@UMMS, 2008. http://escholarship.umassmed.edu/gsbs_diss/792.

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During stress, eukaryotes regulate protein synthesis in part through formation of cytoplasmic, non-membrane-bound complexes called stress granules (SGs). SGs transiently store signaling proteins and stalled translational complexes in response to stress stimuli (e.g. oxidative insult, DNA damage, temperature shifts and ER dysfunction). The functional outcome of SGs is proper translational regulation and signaling, allowing cells to overcome stress. The fatal motor neuron disease Amyotrophic Lateral Sclerosis (ALS) develops in an age-related manner and is marked by progressive neuronal death, wi
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14

Taha, Mohammed. "L'utilisation de cellules natural killer (NK) comme outil thérapeutique : étude clinique de phase 1 de perfusion de cellules NK du donneur après HSCT : Annexe : Pumilio 2, une protéine de liaison à l'ARN surexprimée dans les cellules NK de patients atteints de LAM, réprime les fonctions des cellules NK." Thesis, Aix-Marseille, 2018. http://www.theses.fr/2018AIXM0233.

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Les cellules Natural Killer (NK) sont jouent un rôle essentiel dans la surveillance des hémopathies malignes. Cependant, les cellules tumorales développent des mécanismes immunosuppresseurs pour échapper à l'immunité cellulaire NK. Ainsi, le maintien ou l'amélioration des performances des cellules NK sont considérés comme des défis majeurs. Les objectifs de cette partie étaient d'évaluer l'impact de la perfusion de cellules NK activées sur la récupération et la biologie des cellules NK circulantes après l'allo-SCT. Des doses croissantes de cellules NK activées par IL-2 ex-vivo ont été perfusée
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15

Baethge, Kerstin. "Functional characterization of the FET family of RNA-binding proteins." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2014. http://dx.doi.org/10.18452/16996.

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RNA-bindende Proteine spielen eine zentrale Rolle in der posttranskriptionellen Kontrolle von mRNAs, die zwischen Transkription und Abbau von mRNAs stattfindet. RNA-bindende Proteine beeinflussen Spleißen, Export, Stabilität, Lokalisierung und Translation von mRNAs. FUS, EWSR1 und TAF15 gehören zu der Familie der FET Proteine. Diese wirken an verschiedenen zellulären Prozessen wie Transkription, Spleißen und der Prozessierung von miRNAs mit. Translokationen und Mutationen der FET Proteine führen zu verschiedenen Krankheiten. FUS spielt eine Rolle bei den neurodegenerativen Krankheiten frontote
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16

Alibhai, Imran Nizamudin. "Regulation of FOSB MRNA isoforms by drugs of abuse." Access to abstract only; dissertation is embargoed until after 5/15/2007, 2005. http://www4.utsouthwestern.edu/library/ETD/etdDetails.cfm?etdID=144.

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17

Tejedor, Vaquero Juan Ramón 1984. "Systematic functional analyses of spliceosomal components reveal novel mechanisme of alternative splicing regulation." Doctoral thesis, Universitat Pompeu Fabra, 2014. http://hdl.handle.net/10803/385718.

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Alternative splicing is an essential regulatory layer of gene expression that expands the coding potential of the genome in multicellular organisms. The spliceosome -the sophisticated machinery involved in intron removal- allows versatile regulation of gene expression programs. The splicing process relies on the dynamic interplay between hundreds of components of the spliceosome, and the steps at which the complex process of the splicing reaction can be regulated remain largely unknown. The main objective of this thesis has been to develop high- throughput approaches to systematically identif
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18

Tsai, Yueh-Lin. "Function and Regulation of ALS/FTD-associated RNA Binding Protein FUS." Thesis, 2021. https://doi.org/10.7916/d8-j4g9-m045.

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Fused in Sarcoma (FUS) is a nuclear RNA binding protein functioning in a number of essential cellular processes such as RNA processing and DNA damage response. Mutations in FUS gene contribute to 5% of familial Amyotrophic Lateral Sclerosis (ALS) characterized by FUS protein cytoplasmic aggregation. Despite efforts have been made in the past decade, mechanisms of FUS aggregates to induce cytotoxicity are not fully understood. In addition, wild-type FUS protein has been found mis-localized to cytoplasm in sporadic ALS and Frontotemporal Dementia (FTD) patients with unclear mechanisms. Here, we
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19

Fernandes, Ana Miguel Guterres Coelho 1988. "MicroRNA regulation by the DNA and RNA binding proteins EWS and FUS." Master's thesis, 2012. http://hdl.handle.net/10451/8017.

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Tese de mestrado. Biologia (Biologia Molecular e Genética). Universidade de Lisboa, Faculdade de Ciências, 2012<br>As proteínas EWS (Ewing sarcoma breakpoint region 1), FUS [Fused in sarcoma ou TLS (Translocated in liposarcoma)] e TAF15 (TATA box binding protein-associated factor) fazem parte da família de proteínas denominada FET (FUS, EWS e TAF15). A região amino-terminal destas proteínas é composta por um domínio de activação transcricional enquanto a região C-terminal é constituída pelo domínio de ligação ao RNA, onde existem locais de interacção com os ácidos nucleicos. Desta forma, as pr
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