Výsledky vyhledávání - "Sei-Kyoung Park"

Akademický článek

TDP-43 Toxicity in Yeast Is Associated with a Reduction in Autophagy, and Deletions of TIP41 and PBP1 Counteract These Effects

Autor: Sei-Kyoung Park, Sangeun Park, Susan W. Liebman

Publikováno v: Viruses, Vol 14, Iss 10, p 2264 (2022)

When human TDP-43 is overexpressed in yeast it is toxic and forms cytoplasmic aggregates. The mechanism of this toxicity is unknown. Genetic screens for TDP-43 toxicity modifiers in the yeast system previously identified proteins, including PBP1, tha

Externí odkaz: https://doaj.org/article/b4f5aaf9f2c346339a0a61e6782e73b7

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Akademický článek

Tumor suppressor protein p53 expressed in yeast can remain diffuse, form a prion, or form unstable liquid-like droplets

Autor: Sei-Kyoung Park, Sangeun Park, Christine Pentek, Susan W. Liebman

Publikováno v: iScience, Vol 24, Iss 1, Pp 102000- (2021)

Summary: Mutations in the p53 tumor suppressor are frequent causes of cancer. Because p53 aggregates appear in some tumor cells, it has been suggested that p53 could also cause cancer by forming self-replicating protein aggregates (prions). Here, usi

Externí odkaz: https://doaj.org/article/7579be3ba4da42a9b33b57f0031cb3bc

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Akademický článek

Calcium-responsive transactivator (CREST) toxicity is rescued by loss of PBP1/ATXN2 function in a novel yeast proteinopathy model and in transgenic flies.

Autor: Sangeun Park, Sei-Kyoung Park, Naruaki Watanabe, Tadafumi Hashimoto, Takeshi Iwatsubo, Tatyana A Shelkovnikova, Susan W Liebman

Publikováno v: PLoS Genetics, Vol 15, Iss 8, p e1008308 (2019)

Proteins associated with familial neurodegenerative disease often aggregate in patients' neurons. Several such proteins, e.g. TDP-43, aggregate and are toxic when expressed in yeast. Deletion of the ATXN2 ortholog, PBP1, reduces yeast TDP-43 toxicity

Externí odkaz: https://doaj.org/article/715c39ae19a3469ab13eac20d342bec5

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Akademický článek

Inhibition of Aβ42 oligomerization in yeast by a PICALM ortholog and certain FDA approved drugs

Autor: Sei-Kyoung Park, Kiira Ratia, Mariam Ba, Maria Valencik, Susan W. Liebman

Publikováno v: Microbial Cell, Vol 3, Iss 2, Pp 53-64 (2016)

The formation of small Aβ42 oligomers has been implicated as a toxic species in Alzheimer disease (AD). In strong support of this hypothesis we found that overexpression of Yap1802, the yeast ortholog of the human AD risk factor, phosphatidylinosito

Externí odkaz: https://doaj.org/article/e75f1d33dc05436a90b47e0a32b0f50f

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Akademický článek

Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.

Autor: Sei-Kyoung Park, Joo Y Hong, Fatih Arslan, Vydehi Kanneganti, Basant Patel, Alex Tietsort, Elizabeth M H Tank, Xingli Li, Sami J Barmada, Susan W Liebman

Publikováno v: PLoS Genetics, Vol 13, Iss 5, p e1006805 (2017)

Amyotrophic lateral sclerosis (ALS) is a devastating neurodegenerative disease characterized by selective loss of motor neurons with inclusions frequently containing the RNA/DNA binding protein TDP-43. Using a yeast model of ALS exhibiting TDP-43 dep

Externí odkaz: https://doaj.org/article/c28ff73ebc9b458c8c669f2f26ffcbc2

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Akademický článek

Development and validation of a yeast high-throughput screen for inhibitors of Aβ42 oligomerization

Autor: Sei-Kyoung Park, Scott D. Pegan, Andrew D. Mesecar, Lisa M. Jungbauer, Mary Jo LaDu, Susan W. Liebman

Publikováno v: Disease Models & Mechanisms, Vol 4, Iss 6, Pp 822-831 (2011)

SUMMARY Recent reports point to small soluble oligomers, rather than insoluble fibrils, of amyloid β (Aβ), as the primary toxic species in Alzheimer’s disease. Previously, we developed a low-throughput assay in yeast that is capable of detecting

Externí odkaz: https://doaj.org/article/8ed34ee4bb1b403ba8a75a49986c745a

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Akademický článek

Heterologous aggregates promote de novo prion appearance via more than one mechanism.

Autor: Fatih Arslan, Joo Y Hong, Vydehi Kanneganti, Sei-Kyoung Park, Susan W Liebman

Publikováno v: PLoS Genetics, Vol 11, Iss 1, p e1004814 (2015)

Prions are self-perpetuating conformational variants of particular proteins. In yeast, prions cause heritable phenotypic traits. Most known yeast prions contain a glutamine (Q)/asparagine (N)-rich region in their prion domains. [PSI+], the prion form

Externí odkaz: https://doaj.org/article/41c6f2b39d1c428abc33c97f078051ff

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