Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Xingliang Lu"'
Publikováno v:
Land, Vol 13, Iss 9, p 1441 (2024)
Optimizing resource efficiency and mitigating climate change have become consensuses of human society. However, there is still a gap in assessing the carbon emission efficiency (CEE) and identifying the influence of various factors, especially in rap
Externí odkaz:
https://doaj.org/article/8aa6545027d744f1967026c6cdead812
Publikováno v:
Natural Product Research; Aug2019, Vol. 33 Issue 15, p2145-2150, 6p
Autor:
Richard B. Silverman, Dejan Nikolic, Xingliang Lu, Richard B. van Breemen, Deanna J. Mitchell, Russ Hille, John A. Mersfelder
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 13:4129-4132
Experiments are described to determine the origin of the 6-hydroxyl group of 6-hydroxyFMN produced by the substrate-induced transformation of FMN in the C30A mutant of trimethylamine dehydrogenase. The conversion of FMN to 6-hydroxyFMN is carried out
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2af20f44fa97c0d97d71df8e21bcea64
https://doi.org/10.1016/j.bmcl.2003.07.032
https://doi.org/10.1016/j.bmcl.2003.07.032
Publikováno v:
Bioorganic & Medicinal Chemistry. 11:4423-4430
Mitochondrial monoamine oxidase was inactivated by o-mercaptobenzylamine (1) and o- (2) and p-methylthiobenzylamine (5). Experiments were carried out to provide evidence for possible mechanisms of inactivation. The corresponding o- (3) and p-hydroxyb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22d37e75f90864bfe877cdb804e709e4
https://doi.org/10.1016/s0968-0896(03)00486-3
https://doi.org/10.1016/s0968-0896(03)00486-3
Autor:
Jean Quancard, Yumee Kim Koo, Dhirendra L. Nandi, Eric S. Lightcap, Richard B. Silverman, Xingliang Lu
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 35:1085-1097
3-Hydroxyanthranilic acid 3,4-dioxygenase (EC 1.13.11.6; HADO) was purified to homogeneity from beef liver with the use of two dye columns (Cibacron Blue and Reactive Green 19) and hydroxyapatite. Two active peaks of enzyme were isolated from the hyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7305ad31003ffbba98eae253d998c64c
https://doi.org/10.1016/s1357-2725(02)00347-3
https://doi.org/10.1016/s1357-2725(02)00347-3
Autor:
Richard B. Silverman, Younghee Lee, Lawrence M. Sayre, Ke Qing Ling, Xingliang Lu, Eric M. Shepard, David M. Dooley
Publikováno v:
Journal of the American Chemical Society. 124:12135-12143
We previously reported that 3-pyrroline and 3-phenyl-3-pyrroline effect a time-dependent inactivation of the copper-containing quinone-dependent amine oxidase from bovine plasma (BPAO) (Lee et al. J. Am. Chem. Soc. 1996, 118, 7241-7242). Quinone cofa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfab46c0790962ca78599acb7b524278
https://doi.org/10.1021/ja0205434
https://doi.org/10.1021/ja0205434
Autor:
Richard B. Silverman, Xingliang Lu
Publikováno v:
Journal of the American Chemical Society. 120:10583-10587
Monoamine oxidase B (MAO B) was previously shown to catalyze the decarboxylation of cis- (1) and trans-5-(aminomethyl)-3-(4-methoxyphenyl)dihydrofuran-2(3H)-one hydrochloride (2) (Silverman, R. B.;...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c9a9bfd07867141ea098568995c95774
https://doi.org/10.1021/ja9811041
https://doi.org/10.1021/ja9811041
Publikováno v:
Bioorganic & Medicinal Chemistry. 5:297-304
Monoamine oxidase (MAO) is a flavoenzyme that catalyzes the oxidation of various biogenic and xenobiotic amines. Benzyl 1-(aminomethyl)cyclopropane-1-carboxylate (1) was designed as a diactivated cyclopropane mechanism-based inactivator of MAO (Silve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8712f5f1d3fa9c87e81099dc1f74883
https://doi.org/10.1016/s0968-0896(96)00235-0
https://doi.org/10.1016/s0968-0896(96)00235-0
Publikováno v:
Journal of the American Chemical Society. 115:4949-4954
The anticonvulsant agent milacemide (2-(n-pentylamino)acetamide) is known to inactivate monoamine oxidase-B (MAO-B). Various isotopically labeled analogues of milacemide are used to elucidate the mechanism of inactivation of MAO-B by this compound. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::760437f19b742d13dba0a86c1af4730e
https://doi.org/10.1021/ja00065a001
https://doi.org/10.1021/ja00065a001
Publikováno v:
Journal of the American Chemical Society. 115:4955-4961
The inactivation of monoamine oxidase (MAO) by 1-phenylcyclopropylamine (1-PCPA, 1) has been proposed (Silverman, R. B.; Zieske, P. A. Biochemistry 1985, 74, 2128-2138) to proceed via a radical mechanism involving ring opening of an unstable cyclopro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a6ac6da0f06218d5914650ab343c9741
https://doi.org/10.1021/ja00065a002
https://doi.org/10.1021/ja00065a002