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pro vyhledávání: '"Keng-Chi Lin"'
Autor:
Keng-Chi Lin, 林耿琦
98
Previous studies have proved that the hydrophobic β-amyloid peptide (Aβ), the major proteinacious constituent of senile plaques, is the product of β-amyloid precursor protein cutting by two different enzymes. Due to the effects of various
Previous studies have proved that the hydrophobic β-amyloid peptide (Aβ), the major proteinacious constituent of senile plaques, is the product of β-amyloid precursor protein cutting by two different enzymes. Due to the effects of various
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/38335499710148535425
Autor:
Keng-Chi Lin, 林庚錡
98
The relaxation behaviors of poly(butylene adipate-co-terephthalate), PBAT, was studied using dielectric relaxation spectroscopy (DRS). PBAT was also mixed with dicumyl peroxide (DCP) to investigate the crosslinking effect on the relaxation be
The relaxation behaviors of poly(butylene adipate-co-terephthalate), PBAT, was studied using dielectric relaxation spectroscopy (DRS). PBAT was also mixed with dicumyl peroxide (DCP) to investigate the crosslinking effect on the relaxation be
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/87301615066785033127
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
