Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Kuan Nan Liu"'
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:
European Biophysics Journal. Jul2010, Vol. 39 Issue 8, p1229-1242. 14p. 1 Black and White Photograph, 3 Charts, 7 Graphs.
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
Publikováno v:
Amino Acids. 39:821-829
This work examines the effects of L-arginine (L-Arg) on the aggregation and amyloid fibrillation of bovine serum albumin (BSA). We demonstrate that L-Arg dose-dependently reduces thioflavin T (ThT) fluorescence of BSA within the L-Arg concentration r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bebbc699d5238ffc86526d5208b5bae4
https://doi.org/10.1007/s00726-010-0536-0
https://doi.org/10.1007/s00726-010-0536-0
Publikováno v:
European Biophysics Journal. 39:1229-1242
At least 25 human proteins can fold abnormally to form pathological deposits that are associated with several degenerative diseases. Despite extensive investigation on amyloid fibrillation, the detailed molecular mechanisms remain rather elusive and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f487e6177144f8197d5274b58045440f
https://doi.org/10.1007/s00249-010-0576-0
https://doi.org/10.1007/s00249-010-0576-0
Publikováno v:
International Journal of Biological Macromolecules. 45:321-329
This study examined the effects of glutathione on the fibrillation of hen egg-white lysozyme. We found that the fibrillation of lysozyme was considerably reduced by GSH while no anti-aggregating activity was detected with only GSSG. SDS-PAGE results
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb167f6ccac39dc3972c7f4e633ea621
https://doi.org/10.1016/j.ijbiomac.2009.08.003
https://doi.org/10.1016/j.ijbiomac.2009.08.003
Publikováno v:
Biophysical Chemistry. 144:78-87
At least twenty human proteins can fold abnormally to form pathological deposits that are associated with several degenerative diseases. Despite extensive investigation on amyloid fibrillogenesis, its detailed molecular mechanisms remain unknown. Thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7968a4b3a36d1acdee656f5bedd00af0
https://doi.org/10.1016/j.bpc.2009.06.010
https://doi.org/10.1016/j.bpc.2009.06.010
Autor:
Kuan-Nan Liu, Steven S.-S. Wang
Publikováno v:
Journal of the Chinese Institute of Chemical Engineers. 39:321-328
At least 20 different human proteins can fold abnormally resulting in the formation of pathological aggregates and several deadly degenerative diseases. Evidence also suggests that non-disease-associated proteins, under appropriate conditions, can ag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8306bc305fbe68adfc4b7ea140bcaf6b
https://doi.org/10.1016/j.jcice.2008.03.001
https://doi.org/10.1016/j.jcice.2008.03.001
Publikováno v:
Biochemical Engineering Journal. 29:129-138
β-Amyloid peptide (Aβ) is the major proteinacious constituent of senile plaques in Alzheimer's disease and is believed to be responsible for the neurodegeneration associated with the disease. This work is aimed at determining the effect of solvent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9c62d81ac12b8a4fad3aa5fc1fbd5573
https://doi.org/10.1016/j.bej.2005.02.037
https://doi.org/10.1016/j.bej.2005.02.037
Autor:
Kuan Nan Liu, Jeng Shiung Jan, Sung Ning Wang, Chia Min Lai, Hwai-Shen Liu, Yi Ting Lee, Rita P.-Y. Chen, Steven S.-S. Wang
Publikováno v:
Biochimica et biophysica acta. 1820(11)
Background More than twenty-seven human proteins can fold abnormally to form amyloid deposits associated with a number of degenerative diseases. The research reported here is aimed at exploring the connection between curcumin's thermostability and it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1863b6591703016958cf2ad02f1439c7
https://pubmed.ncbi.nlm.nih.gov/22884915
https://pubmed.ncbi.nlm.nih.gov/22884915