Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Josephine W Wu"'
Autor:
Josephine W Wu, Mei-Er Chen, Wen-Sing Wen, Wei-An Chen, Chien-Ting Li, Chih-Kai Chang, Chun-Hsien Lo, Hwai-Shen Liu, Steven S-S Wang
Publikováno v:
PLoS ONE, Vol 9, Iss 11, p e112309 (2014)
Cataract, a major cause of visual impairment worldwide, is the opacification of the eye's crystalline lens due to aggregation of the crystallin proteins. The research reported here is aimed at investigating the aggregating behavior of γ-crystallin p
Externí odkaz:
https://doaj.org/article/6e4795810efc4048a6dc76b700e651e4
Autor:
Josephine W Wu, Kuan-Nan Liu, Su-Chun How, Wei-An Chen, Chia-Min Lai, Hwai-Shen Liu, Chaur-Jong Hu, Steven S-S Wang
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e81982 (2013)
Carnosine, a common dipeptide in mammals, has previously been shown to dissemble alpha-crystallin amyloid fibrils. To date, the dipeptide's anti-fibrillogensis effect has not been thoroughly characterized in other proteins. For a more complete unders
Externí odkaz:
https://doaj.org/article/5dc412791cf14c928aa2800efb5298aa
Publikováno v:
Journal of the Taiwan Institute of Chemical Engineers. 118:187-195
Amyloid fibrils’ stable structure and nice biocompatibility make them good candidates as the templates used in engineering and biomedicine. While palladium nanoparticles have been widely used as catalysts, their high surface energy results in aggre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f029b4b3a5b648056a5664ec9a3591f9
https://doi.org/10.1016/j.jtice.2020.12.030
https://doi.org/10.1016/j.jtice.2020.12.030
Autor:
Erna Demjen, Zuzana Gazova, Maria-Magdalena Mocanu, Silvio Dutz, Zuzana Bednarikova, Josephine W. Wu, Steven S.-S. Wang, Jozef Marek
Publikováno v:
Journal of Magnetism and Magnetic Materials. 473:1-6
More than 50 diseases are associated with a conversion of proteins or peptides from their soluble functional states to highly organized fibrillar aggregates called amyloid fibrils. Due to the specific physico-chemical properties, specifically designe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b2e4bf55da816ddb74057b47e2681bc
https://doi.org/10.1016/j.jmmm.2018.10.018
https://doi.org/10.1016/j.jmmm.2018.10.018
Autor:
Andrea Antosova, Zuzana Bednarikova, Iryna Antal, Josephine W. Wu, Martina Koneracka, Zuzana Gazova, Martina Kubovcikova, Vlasta Zavisova, Steven S.-S. Wang
Publikováno v:
Journal of Magnetism and Magnetic Materials. 471:169-176
A great variety of human protein deposition and protein aggregation diseases (Alzheimer’s disease, diabetes mellitus, cataract, systemic amyloidosis and other) have been associated with the accumulation of amyloid fibrils in different tissues. Ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::04afcfc35efafc704d2a8b698b55d805
https://doi.org/10.1016/j.jmmm.2018.09.096
https://doi.org/10.1016/j.jmmm.2018.09.096
Autor:
Ning-Hui Lu, Diana Fedunova, Shen-Long Tsai, Zuzana Bednarikova, Josephine W. Wu, Zuzana Gazova, Steven S.-S. Wang, Su-Chun How, Chien-Yu Lin
Publikováno v:
Colloids and Surfaces B: Biointerfaces. 172:674-683
More than thirty human proteins and/or peptides can aggregate to form amyloid deposits that are linked to several amyloid diseases including clinical syndrome injection-localized amyloidosis, which is correlated with the aggregation of the 51-residue
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4092ac2b726ae253651b9120f1d337c
https://doi.org/10.1016/j.colsurfb.2018.09.029
https://doi.org/10.1016/j.colsurfb.2018.09.029
Autor:
Josephine W. Wu, Su Chun How, Zuzana Bednarikova, Steven S.-S. Wang, Andrea Antosova, Ta Hsien Lin, Jinn Tsyy Lai, Zuzana Gazova, Yu-Hong Cheng, Chun Hsien Lo
Publikováno v:
International Journal of Biological Macromolecules. 119:1059-1067
The 129-residue lysozyme has been shown to form amyloid fibrils in vitro. While methylene blue (MB), a compound in the phenothiazinium family, has been shown to dissemble tau fibril formation, its anti-fibrillogenic effect has not been thoroughly cha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4897531bab931df1caa81a465362328c
https://doi.org/10.1016/j.ijbiomac.2018.08.038
https://doi.org/10.1016/j.ijbiomac.2018.08.038
Autor:
Chun-Hsien Lo, Steven S.-S. Wang, Chih-Kai Chang, Su-Chun How, Chien-Ting Li, Mei-Er Chen, Wei-An Chen, Josephine W. Wu, Min-Chih Chun
Publikováno v:
International Journal of Biological Macromolecules. 118:442-451
Human γ d -crystallin (Hγ d -crystallin), a major protein component of the human eye lens, is associated with the development of juvenile- and mature-onset cataracts. Evidence suggests that nonenzymatic protein glycation plays an important role in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::144d60575ba65dbdbf5ea81d27c49bf4
https://doi.org/10.1016/j.ijbiomac.2018.06.108
https://doi.org/10.1016/j.ijbiomac.2018.06.108
Publikováno v:
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 261:120023
Cataract is known as one of the leading causes of vision impairment worldwide. While the detailed mechanism of cataratogenesis remains unclear, cataract is believed to be correlated with the aggregation and/or misfolding of human ocular lens proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9a90d129d053f646adf4b8d09aae7429
https://doi.org/10.1016/j.saa.2021.120023
https://doi.org/10.1016/j.saa.2021.120023
Autor:
Yu-Hong Cheng, Ta Hsien Lin, Yi Lin Chen, Steven S.-S. Wang, Chun Tien Kuo, Shu Shun Hsueh, Su Chun How, Wei-Tse Hsu, Josephine W. Wu, Hwai-Shen Liu
Publikováno v:
International Journal of Biological Macromolecules. 98:159-168
Formation of amyloid fibrils has been associated with at least 30 different protein aggregation diseases. The 129-residue polypeptide hen lysozyme, which is structurally homologous to human lysozyme, has been demonstrated to exhibit amyloid fibril-fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc8e695c770cfa0e414ab66d9e58b2f2
https://doi.org/10.1016/j.ijbiomac.2017.01.110
https://doi.org/10.1016/j.ijbiomac.2017.01.110