Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Yu-Yung Chang"'
Publikováno v:
Antioxidants, Vol 8, Iss 10, p 461 (2019)
Sulfur is an essential nutrient that can be converted into utilizable metabolic forms to produce sulfur-containing metabolites in plant. Adenosine 5′-phosphosulfate (APS) reductase (APR) plays a vital role in catalyzing the reduction of activated s
Externí odkaz:
https://doaj.org/article/5805edfb6f2941b99395f68fc78502d2
Publikováno v:
PLoS ONE, Vol 8, Iss 12, p e83091 (2013)
Malate dehydrogenase (MDH) catalyzes the conversion of oxaloacetate and malate by using the NAD/NADH coenzyme system. The system is used as a conjugate for enzyme immunoassays of a wide variety of compounds, such as illegal drugs, drugs used in thera
Externí odkaz:
https://doaj.org/article/ade3cf519d5247839d324b03168919e9
Publikováno v:
PLoS ONE, Vol 7, Iss 12, p e52292 (2012)
The novel tumor biomarker MIEN1, identified by representational difference analysis, is overexpressed in breast cancer and prostate cancer. MIEN1 is considered an oncogenic protein, because MIEN1 overexpression functionally enhances migration and inv
Externí odkaz:
https://doaj.org/article/c9a4506cfaf54ca38e285923f57bc89f
Autor:
Yu-Yung Chang, 張有庸
103
During the past 20 years, in the cooperation of the government and private sectors, the restoration of the traditional Indigo Dyeing is getting to know by general public. Highlight by ecological and environmental issues in recent years and t
During the past 20 years, in the cooperation of the government and private sectors, the restoration of the traditional Indigo Dyeing is getting to know by general public. Highlight by ecological and environmental issues in recent years and t
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/66649115197862049136
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 16; Pages: 9347
α-crystallin is a major structural protein in the eye lenses of vertebrates that is composed of two relative subunits, αA and αB crystallin, which function in maintaining lens transparency. As a member of the small heat-shock protein family (sHsp)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6afb8cea83de795b26885152183915f0
https://pubmed.ncbi.nlm.nih.gov/36012609
https://pubmed.ncbi.nlm.nih.gov/36012609
Publikováno v:
Journal of Agricultural and Food Chemistry. 68:6161-6169
α-Galactosidase catalyzes the hydrolysis of a terminal α-galactose residue in galacto-oligosaccharides and has potential in various industrial applications and food processing. We determined the crystal structures of α-galactosidase from the therm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::344e6d7cb074d78075577c750d78378b
https://doi.org/10.1021/acs.jafc.0c00871
https://doi.org/10.1021/acs.jafc.0c00871
Publikováno v:
Chemical communications (Cambridge, England). 56(72)
The common mechanism of N-acetyltransferases (NATs) is a water-mediated catalysis, which is not conducive to thermophilic acetyltransferases. The crystal structure of SsArd1 shows an ordered catalytic water molecule in a trap formed by the residues H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba3992d4f74068c9edf7a3c34b6351ab
https://pubmed.ncbi.nlm.nih.gov/32780067
https://pubmed.ncbi.nlm.nih.gov/32780067
Autor:
Sheng-Chia, Chen, Szu-Pei, Wu, Yu-Yung, Chang, Tzann-Shun, Hwang, Tzong-Huei, Lee, Chun-Hua, Hsu
Publikováno v:
Journal of agricultural and food chemistry. 68(30)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9e444c54b6495f103c715aeb753cdf79
https://pubmed.ncbi.nlm.nih.gov/32390413
https://pubmed.ncbi.nlm.nih.gov/32390413
Publikováno v:
Journal of structural biology. 212(1)
BCP1 is a protein enriched in the nucleus that is required for Mss4 nuclear export and identified as the chaperone of ribosomal protein Rpl23 in Saccharomyces cerevisiae. According to sequence homology, BCP1 is related to the mammalian BRCA2-interact
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::96c40a607d77562a075555c21e19ba65
https://pubmed.ncbi.nlm.nih.gov/32805410
https://pubmed.ncbi.nlm.nih.gov/32805410