Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Jae Wook Hyeon"'
Autor:
Jae Wook Hyeon, Su Yeon Kim, Sol Moe Lee, Jeongmin Lee, Seong Soo A An, Myung Koo Lee, Yeong Seon Lee
Publikováno v:
PLoS ONE, Vol 12, Iss 1, p e0170266 (2017)
Prion propagation is mediated by the structural alteration of normal prion protein (PrPC) to generate pathogenic prion protein (PrPSc). To date, compounds for the inhibition of prion propagation have mainly been screened using PrPSc-infected cells. R
Externí odkaz:
https://doaj.org/article/a58fb67f7c2a403090d96cf124a4d29f
Autor:
Sol Moe Lee, Myungguen Chung, Jae Wook Hyeon, Seok Won Jeong, Young Ran Ju, Heebal Kim, Jeongmin Lee, SangYun Kim, Seong Soo A An, Sung Beom Cho, Yeong Seon Lee, Su Yeon Kim
Publikováno v:
PLoS ONE, Vol 11, Iss 6, p e0157540 (2016)
Inherited prion diseases (IPDs), including genetic Creutzfeldt-Jakob disease (gCJD), account for 10-15% of cases of prion diseases and are associated with several pathogenic mutations, including P102L, V180I, and E200K, in the prion protein gene (PRN
Externí odkaz:
https://doaj.org/article/5ae6c7ca5e134d6d87ac54ad32a1f07a
Autor:
Jiwon Choi, Jeongmin Lee, Seong Soo A. An, Yeong Seon Lee, Jae Wook Hyeon, Sol Moe Lee, Ran Noh, Kyoung Tai No
Publikováno v:
Experimental Neurobiology
Prion diseases are a group of neurodegenerative and fatal central nervous system disorders. The pathogenic mechanism involves the conversion of cellular prion protein (PrPC) to an altered scrapie isoform (PrPSc), which accumulates in amyloid deposits
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ea5326a2909c48fa52f0b58af168c03
https://doi.org/10.5607/en.2020.29.1.93
https://doi.org/10.5607/en.2020.29.1.93
Autor:
Sol Moe Lee, Su Yeon Kim, Jae Wook Hyeon, Seong-Han Kim, Yeong Seon Lee, Heebal Kim, Soo Jin Kim, Ran Noh
Publikováno v:
Prion
The diagnosis of sporadic Creutzfeldt-Jakob disease (sCJD) can only be confirmed by abnormal protease-resistant prion protein accumulation in post-mortem brain tissue. The relationships between sCJD and cerebrospinal fluid (CSF) proteins such as 14
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07050c49c566c5ef82a6c54aef144aa1
https://doi.org/10.1080/19336896.2019.1639482
https://doi.org/10.1080/19336896.2019.1639482
Autor:
Su Yeon Kim, Jiwon Choi, Rajiv Gandhi Govindaraj, Jae Wook Hyeon, K. Lee, Song Ling Ma, Jeongmin Lee, Kyoung Tai No
Publikováno v:
Chemical Biology & Drug Design. 89:907-917
Transition of a physiological folded prion (PrPC ) into a pathogenic misfolded prion (PrPSc ) causes lethal neurodegenerative disorders and prion diseases. Antiprion compounds have been developed to prevent this conversion; however, their mechanism o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f88c00022052a175c46350c383f504bf
https://doi.org/10.1111/cbdd.12916
https://doi.org/10.1111/cbdd.12916
Autor:
Jae Wook Hyeon1, Jiwon Choi2, Su Yeon Kim1, Govindaraj, Rajiv Gandhi2, Kyu Jam Hwang1, Yeong Seon Lee1, Seong Soo A. An3, Myung Koo Lee4, Jong Young Joung5, Kyoung Tai No2,6 ktno@bmdrc.org, Jeongmin Lee1 jeongminlee@korea.kr
Publikováno v:
Scientific Reports. 10/9/2015, p1-11. 11p.
Publikováno v:
Journal of Medical Virology. 87:175-186
Creutzfeldt–Jakob disease (CJD) is a representative human transmissible spongiform encephalopathy associated with central nervous system degeneration. Prions, the causative agents of CJD, are composed of misfolded prion proteins and are able to sel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::82f23e6ba6ee323394794dd0a8578f92
https://doi.org/10.1002/jmv.24004
https://doi.org/10.1002/jmv.24004
Autor:
Jun Sun Park, Su Yeon Kim, Jae Wook Hyeon, Bo-Yeong Choi, Sol Moe Lee, Chi Kyeong Kim, Young Ran Ju
Publikováno v:
Prion. 6:375-382
Creutzfeldt-Jakob disease (CJD), included in the human transmissible spongiform encephalopathies (TSE), is widely known to be caused by an abnormal accumulation of misfolding prion protein in the brain. Human prion protein gene (PRNP) is mapped in ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9852b8ee78bc127a511ec4737116318
https://doi.org/10.4161/pri.20195
https://doi.org/10.4161/pri.20195
Autor:
Jae Wook Hyeon, Bo Yeong Choi, Seong Soo A. An, Chi-Kyeong Kim, Sol Moe Lee, Jun Sun Park, Su Yeon Kim, Young Ran Ju
Publikováno v:
Biochemical and Biophysical Research Communications. 424:214-220
Misfolding of prion protein (PrP to PrPSc) can cause neurodegenerative prion diseases. As a glycosylphosphatidylinositol (GPI)-anchored membrane protein, the normal form of PrP (PrPC) can function as a receptor for ligands in the extracellular space.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::72f5fcd08909f0be1223e8ede53d1afc
https://doi.org/10.1016/j.bbrc.2012.06.056
https://doi.org/10.1016/j.bbrc.2012.06.056
Autor:
Kyoung Tai No, Seong Soo A. An, Jeongmin Lee, Myung Koo Lee, Jong Young Joung, Yeong Seon Lee, Kyu Jam Hwang, Su Yeon Kim, Rajiv Gandhi Govindaraj, Ji-Won Choi, Jae Wook Hyeon
Publikováno v:
SCIENTIFIC REPORTS(5)
Scientific Reports
Scientific Reports
Prion diseases are associated with the conformational conversion of the physiological form of cellular prion protein (PrPC) to the pathogenic form, PrPSc. Compounds that inhibit this process by blocking conversion to the PrPSc could provide useful an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a12932b2a47d73b85aaa90dd1adbdce