Zobrazeno 1 - 10
of 105
pro vyhledávání: '"Jia‐Cherng Horng"'
Autor:
Chin-Yu Chen, Tzu-Ping Ko, Kuan-Fu Lin, Bo-Lin Lin, Chun-Hsiang Huang, Cheng-Hung Chiang, Jia-Cherng Horng
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-12 (2018)
Abstract Ketol-acid reductoisomerase (KARI) is a bifunctional enzyme in the second step of branched-chain amino acids biosynthetic pathway. Most KARIs prefer NADPH as a cofactor. However, KARI with a preference for NADH is desirable in industrial app
Externí odkaz:
https://doaj.org/article/aa0ddd02b89541f7896091cc85e1327d
Publikováno v:
ACS Omega, Vol 2, Iss 9, Pp 5574-5581 (2017)
Externí odkaz:
https://doaj.org/article/88757276be384142a639d0ae33910ab4
Autor:
Cheng-Ying Hsieh, Pi-Wen Ko, Yu-Jui Chang, Mohit Kapoor, Yu-Chuan Liang, Hsueh-Liang Chu, Hui-Hsien Lin, Jia-Cherng Horng, Ming-Hua Hsu
Publikováno v:
Molecules, Vol 24, Iss 18, p 3259 (2019)
Numerous reports have shown that conjugated benzimidazole derivatives possess various kinds of biological activities, including anticancer properties. In this report, we designed and synthesized 24 new molecules comprising a benzimidazole ring, arene
Externí odkaz:
https://doaj.org/article/61e442e16fd14931b70d4765e9df6cc1
Autor:
Shwu-Chen Tsay, Shu-Yu Lin, Wen-Chieh Huang, Ming-Hua Hsu, Kuo Chu Hwang, Chun-Cheng Lin, Jia-Cherng Horng, I-Chia Chen, Jih Ru Hwu, Fa-Kuen Shieh, Pieter Leyssen, Johan Neyts
Publikováno v:
Molecules, Vol 21, Iss 2, p 228 (2016)
A series of new conjugated compounds with a –SCH2– linkage were synthesized by chemical methods from imidazole and coumarin derivatives. The experimental results indicate that of the twenty newly synthesized imidazole–coumarin conjugates, three
Externí odkaz:
https://doaj.org/article/faa4967ef6fd4219909f40d2c3f6cd9c
Publikováno v:
Process Biochemistry. 121:26-34
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::005de58efb4cc6f71866b78f1d83e981
https://doi.org/10.1016/j.procbio.2022.06.024
https://doi.org/10.1016/j.procbio.2022.06.024
Autor:
Tsai‐Ling Hsu, Jia‐Cherng Horng
Publikováno v:
Protein Science. 32
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8be4babe5e00e75f61bb28c5a55f69f5
https://doi.org/10.1002/pro.4650
https://doi.org/10.1002/pro.4650
Publikováno v:
Journal of Thermal Analysis and Calorimetry. 142:2003-2013
To elucidate the influence of commonly used biological buffers on the hemoglobin (Hb) structure, biomolecular interactions between Hb and the selected buffers, including tris (hydroxymethyl) aminomethane (TRIS), N-[tris (hydroxymethyl) methyl]-3-amin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f37dc74c584c665f4c83ee3a689b6519
https://doi.org/10.1007/s10973-020-09947-7
https://doi.org/10.1007/s10973-020-09947-7
Publikováno v:
Biomacromolecules. 21:1195-1201
A polyproline fragment containing a catalytic dyad of His-His or Ser-His was coupled with a self-assembling peptide MAX1 to design new hydrolases (H2H5 and H2S5) for catalyzing ester hydrolysis. Circular dichroism measurements indicated that the pept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d93accffc4b35dbac25a78565f1bf3c8
https://doi.org/10.1021/acs.biomac.9b01620
https://doi.org/10.1021/acs.biomac.9b01620
Autor:
Kuei-Yen Huang, I.-Chia Chen, Wei-Hao Chen, Michitoshi Hayashi, Jia-Cherng Horng, Mei-Chun Huang, Chen-Wei Huang
Publikováno v:
RSC Advances. 10:34493-34500
Using low-wavenumber Raman spectroscopy in combination with theoretical calculations via solid-state density functional theory (DFT)-D3, we studied the vibrational structures and interaction with solvent of poly-L-proline and the oligoproline P12 ser
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::848a70cfe7247e27fb27a6ca3ea51314
https://doi.org/10.1039/d0ra05746k
https://doi.org/10.1039/d0ra05746k
Autor:
He-Sheng Chiu, Jia-Cherng Horng
Publikováno v:
The journal of physical chemistry. B. 125(27)
Cationic or anionic residues are frequently located at the termini of proteins because their charged side chain can form electrostatic interactions with a terminal carboxylate or ammonium group to stabilize the structure under physiological condition
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d34a9b857a51591a6e22f03c59bb420
https://pubmed.ncbi.nlm.nih.gov/34213353
https://pubmed.ncbi.nlm.nih.gov/34213353