Relevant bibliographies by topics / Translocated in Liposarcoma

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  1. Journal articles
  2. Dissertations / Theses

Academic literature on the topic 'Translocated in Liposarcoma'

Author: Grafiati
Published: 4 June 2021
Last updated: 18 February 2022

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Journal articles on the topic "Translocated in Liposarcoma"

1

Yang, Shu, Sadaf T. Warraich, Garth A. Nicholson, and Ian P. Blair. "Fused in sarcoma/translocated in liposarcoma: A multifunctional DNA/RNA binding protein." International Journal of Biochemistry & Cell Biology 42, no. 9 (September 2010): 1408–11. http://dx.doi.org/10.1016/j.biocel.2010.06.003.

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2

Staege, Martin S., and Daniela Max. "Genetics and Epigenetics of the TET-ETS Translocation Network." Genetics & Epigenetics 2 (January 2009): GEG.S2815. http://dx.doi.org/10.4137/geg.s2815.

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In the present paper we review the translocation network involving TET and ETS family members with special focus on the Ewing family of tumors. FUS (fusion, involved in t(12;16) in malignant liposarcoma = TLS, Translocated in liposarcoma), EWSR1 (Ewing sarcoma breakpoint region 1) and TAF15 (TATA box-binding protein-associated factor, 68-KD) are the three human members of the TET family of RNA binding proteins. In addition, two EWSR1 pseudogenes are present in the human genome. TET family members are involved in several oncogenic gene fusions. Five of the 18 known fusion partners belong to the E26 (E twenty-six, ETS) family of transcription factors. Gene fusions between TET or ETS family members and other fusion partners link these gene fusions to a large network of oncogenic gene rearrangements.
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3

Sánchez-Ramos, Cristina, Alberto Tierrez, Oscar Fabregat-Andrés, Brigitte Wild, Fatima Sánchez-Cabo, Alessandro Arduini, Ana Dopazo, and María Monsalve. "PGC-1α Regulates Translocated in Liposarcoma Activity: Role in Oxidative Stress Gene Expression." Antioxidants & Redox Signaling 15, no. 2 (July 15, 2011): 325–37. http://dx.doi.org/10.1089/ars.2010.3643.

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4

Klint, Peter, Ulf Hellman, Christer Wernstedt, Pierre Åman, David Ron, and Lena Claesson-Welsh. "Translocated in liposarcoma (TLS) is a substrate for fibroblast growth factor receptor-1." Cellular Signalling 16, no. 4 (April 2004): 515–20. http://dx.doi.org/10.1016/j.cellsig.2003.09.007.

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5

Aoki, Masashi. "Amyotrophic lateral sclerosis (ALS) with the mutations in the fused in sarcoma/translocated in liposarcoma gene." Rinsho Shinkeigaku 53, no. 11 (2013): 1080–83. http://dx.doi.org/10.5692/clinicalneurol.53.1080.

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6

Powers, C. Andrew, Mukul Mathur, Bruce M. Raaka, David Ron, and Herbert H. Samuels. "TLS (Translocated-in-Liposarcoma) Is a High-Affinity Interactor for Steroid, Thyroid Hormone, and Retinoid Receptors." Molecular Endocrinology 12, no. 1 (January 1, 1998): 4–18. http://dx.doi.org/10.1210/mend.12.1.0043.

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7

Sugiura, Tomohito, Shuji Matsuda, Satoshi Kurosaka, Nobuhiro Nakai, Keita Fukumoto, Tetsuya Takahashi, Hirofumi Maruyama, Kazunori Imaizumi, Masayasu Matsumoto, and Toru Takumi. "Translocated in liposarcoma regulates the distribution and function of mammalian enabled, a modulator of actin dynamics." FEBS Journal 283, no. 8 (March 2, 2016): 1475–87. http://dx.doi.org/10.1111/febs.13685.

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8

Powers, C. A. "TLS (Translocated-in-Liposarcoma) Is a High-Affinity Interactor for Steroid, Thyroid Hormone, and Retinoid Receptors." Molecular Endocrinology 12, no. 1 (January 1, 1997): 4–18. http://dx.doi.org/10.1210/me.12.1.4.

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9

Tan, A. Y., T. R. Riley, T. Coady, H. J. Bussemaker, and J. L. Manley. "TLS/FUS (translocated in liposarcoma/fused in sarcoma) regulates target gene transcription via single-stranded DNA response elements." Proceedings of the National Academy of Sciences 109, no. 16 (March 29, 2012): 6030–35. http://dx.doi.org/10.1073/pnas.1203028109.

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10

Uranishi, Hiroaki, Toshifumi Tetsuka, Mayumi Yamashita, Kaori Asamitsu, Manabu Shimizu, Makoto Itoh, and Takashi Okamoto. "Involvement of the Pro-oncoprotein TLS (Translocated in Liposarcoma) in Nuclear Factor-κB p65-mediated Transcription as a Coactivator." Journal of Biological Chemistry 276, no. 16 (January 24, 2001): 13395–401. http://dx.doi.org/10.1074/jbc.m011176200.

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Dissertations / Theses on the topic "Translocated in Liposarcoma"

1

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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Abstract:
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, with cytoplasmic protein aggregation, excitotoxicity and increased oxidative stress as major hallmarks. Fused in Sarcoma/Translocated in Liposarcoma (FUS) is an RNA-binding protein mutated in ALS with roles in RNA and DNA processing. Most ALS-associated FUS mutations cause FUS to aberrantly localize in the cytoplasm due to a disruption in the nuclear localization sequence. Intriguingly, pathological inclusions in human FUSALS cases contain aggregated FUS as well as several SG-associated proteins. Further, cytoplasmic mutant FUS incorporates into SGs, which increases SG volume and number, delays SG assembly, accelerates SG disassembly, and alters SG dynamics. I posit that mutant FUS association with stress granules is a toxic gain-of-function in ALS that alters the function of SGs by interaction with SG components. Here, I show that mutant FUS incorporates in to SGs via its Cterminal RGG motifs, the methylation of which is not required for this localization. Further, I identify protein interactions specific to full-length mutant FUS under stress conditions that are potentially capable of interacting with FUS in SGs. Finally, I demonstrate a potential change in the protein composition of SGs upon incorporation of mutant FUS. These findings advance the field of ALS and SG biology, thereby providing groundwork for future investigation.
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2

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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Abstract:
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, with cytoplasmic protein aggregation, excitotoxicity and increased oxidative stress as major hallmarks. Fused in Sarcoma/Translocated in Liposarcoma (FUS) is an RNA-binding protein mutated in ALS with roles in RNA and DNA processing. Most ALS-associated FUS mutations cause FUS to aberrantly localize in the cytoplasm due to a disruption in the nuclear localization sequence. Intriguingly, pathological inclusions in human FUSALS cases contain aggregated FUS as well as several SG-associated proteins. Further, cytoplasmic mutant FUS incorporates into SGs, which increases SG volume and number, delays SG assembly, accelerates SG disassembly, and alters SG dynamics. I posit that mutant FUS association with stress granules is a toxic gain-of-function in ALS that alters the function of SGs by interaction with SG components. Here, I show that mutant FUS incorporates in to SGs via its Cterminal RGG motifs, the methylation of which is not required for this localization. Further, I identify protein interactions specific to full-length mutant FUS under stress conditions that are potentially capable of interacting with FUS in SGs. Finally, I demonstrate a potential change in the protein composition of SGs upon incorporation of mutant FUS. These findings advance the field of ALS and SG biology, thereby providing groundwork for future investigation.
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