Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Wen-Sing Wen"'
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:
Wen-Sing Wen, Josephine W. Wu, Lilian Tsai-Wei Lin, Chen-Yuan Kao, Steven S.-S. Wang, Jinn-Tsyy Lai
Publikováno v:
Biochemical Engineering Journal. 78:189-197
Human γD-crystallin, a 173-residue protein, is a major protein component of the human eye lens and associated with the development of juvenile and mature-onset cataracts. The study reported here is aimed at examining the effects of resveratrol on hu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d537df1efd529cb2aca314a05491776b
https://doi.org/10.1016/j.bej.2013.03.014
https://doi.org/10.1016/j.bej.2013.03.014
Publikováno v:
Journal of the Taiwan Institute of Chemical Engineers. 42:547-555
Human γD-crystallin (HγDC), a 173 amino acid protein, is a primary protein component of the human eye lens. It is composed of two highly homologous β-sheet domains and is associated with the development of juvenile and adult-onset cataracts. In th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::01403edeedd8528fc99dd7c987075925
https://doi.org/10.1016/j.jtice.2010.10.002
https://doi.org/10.1016/j.jtice.2010.10.002
Publikováno v:
Food Biophysics. 6:138-151
The current research is aimed at exploring the inhibitory effect of glutathione on fibril formation of an important four disulfide bond-containing whey protein, α-lactalbumin. Through numerous spectroscopic techniques and transmission electron micro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::39251280ed86ee8cdea3ddcdb19216e9
https://doi.org/10.1007/s11483-010-9199-3
https://doi.org/10.1007/s11483-010-9199-3
Autor:
Chien-Ting Li, Mei-Er Chen, Chih-Kai Chang, Steven S.-S. Wang, Josephine W. Wu, Hwai-Shen Liu, Chun-Hsien Lo, Wen-Sing Wen, Wei-An Chen
Publikováno v:
PLoS ONE, Vol 9, Iss 11, p e112309 (2014)
PLoS ONE
PLoS ONE
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b76d1feec25b5a93dd80e868271936a4
http://europepmc.org/articles/PMC4229192?pdf=render
http://europepmc.org/articles/PMC4229192?pdf=render
Autor:
Yun Chiao Huang, Chia Min Lai, Wen Sing Wen, Steven S.-S. Wang, Yu-Jiun Lin, Jeng Shiung Jan, Jun-Kun Lai
Publikováno v:
Biopolymers. 97(2)
The fibrillation of hen egg-white lysozyme (HEWL) in the absence and presence of simple, unstructured D,L-lysine-co-glycine (D,L-Lys-co-gly) and D,L-lysine-co-L-phenylalanine (D,L-Lys-co-Phe) copolypeptides was studied by using a variety of analytica
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::523b8b36e78f7fcf5fa78fde0c2bd0bc
https://pubmed.ncbi.nlm.nih.gov/21858781
https://pubmed.ncbi.nlm.nih.gov/21858781
Publikováno v:
Biochimica et biophysica acta. 1811(5)
Amyloid fibrillogenesis is an important pathological feature of a group of degenerative human diseases. The 129-residue enzyme hen egg-white lysozyme has been shown to form fibrils in vitro at pH 2.0 and 55°C. In this research, using various spectro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc41968f1c3009bd072f3c30e4bb5a61
https://pubmed.ncbi.nlm.nih.gov/21320633
https://pubmed.ncbi.nlm.nih.gov/21320633
Publikováno v:
Journal of Bioscience and Bioengineering. 108:S73
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a99123876b6954ca0a3b75748875ecb9
https://doi.org/10.1016/j.jbiosc.2009.08.216
https://doi.org/10.1016/j.jbiosc.2009.08.216
Publikováno v:
Food Biophysics; Mar2011, Vol. 6 Issue 1, p138-151, 14p, 1 Black and White Photograph, 3 Charts, 4 Graphs