Joo Y Hong
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Explore the profile of Joo Y Hong including associated specialties, affiliations and a list of published articles.
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8
Citations
341
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Recent Articles
1.
Park S, Hong J, Arslan F, Kanneganti V, Patel B, Tietsort A, et al.
PLoS Genet
. 2017 May;
13(5):e1006805.
PMID: 28531192
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...
2.
Arslan F, Hong J, Kanneganti V, Park S, Liebman S
PLoS Genet
. 2015 Jan;
11(1):e1004814.
PMID: 25568955
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+],...
3.
Yang Z, Hong J, Derkatch I, Liebman S
PLoS Genet
. 2013 Jan;
9(1):e1003236.
PMID: 23358669
Prions are self-propagating conformations of proteins that can cause heritable phenotypic traits. Most yeast prions contain glutamine (Q)/asparagine (N)-rich domains that facilitate the accumulation of the protein into amyloid-like aggregates....
4.
Huh S, Chung Y, Piao Y, Jin M, Son H, Yoon N, et al.
J Immunol
. 2011 Jun;
187(2):960-9.
PMID: 21685323
This study examined whether ethyl pyruvate (EP) promotes the survival of nigrostriatal dopaminergic (DA) neurons in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease. MPTP induced degeneration of nigrostriatal DA...
5.
Manogaran A, Hong J, Hufana J, Tyedmers J, Lindquist S, Liebman S
PLoS Genet
. 2011 Jun;
7(5):e1001386.
PMID: 21625618
Prions are self-perpetuating aggregated proteins that are not limited to mammalian systems but also exist in lower eukaryotes including yeast. While much work has focused around chaperones involved in prion...
6.
Hong J, Mathur V, Liebman S
Yeast
. 2011 May;
28(7):555-60.
PMID: 21590810
Most scoring assays for yeast prions are dependent on specific genetic markers and constructs that differ for each prion. Here we describe a simple colour assay for the [URE3] prion...
7.
Mathur V, Hong J, Liebman S
J Mol Biol
. 2009 May;
390(2):155-67.
PMID: 19422835
Several cellular chaperones have been shown to affect the propagation of the yeast prions [PSI(+)], [PIN(+)] and [URE3]. Ssa1 and Ssa2 are Hsp70 family chaperones that generally cause pro-[PSI(+)] effects,...
8.
Bradley M, Edskes H, Hong J, Wickner R, Liebman S
Proc Natl Acad Sci U S A
. 2002 Aug;
99 Suppl 4:16392-9.
PMID: 12149514
Prions are "infectious" proteins. When Sup35, a yeast translation termination factor, is aggregated in its [PSI(+)] prion form its function is compromised. When Rnq1 is aggregated in its [PIN(+)] prion...