Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Huailing Zhong"'
Publikováno v:
Journal of Hazardous Materials. 333:265-274
Natural products are becoming increasingly popular in multiple fields involving medicines, foods and beverages. However, due to the frequent occurrence of poisoning incidents, their toxicity and safety have caused a serious concern. Here we report a
Autor:
Lin An, Jun Chen, Jiancheng Wang, Hua Yang, Ping Li, Bixia Huang, Huailing Zhong, Weiwei Tang
Publikováno v:
RSC Advances. 7:43005-43013
Protease-activated receptor 1 (PAR-1) antagonists strongly inhibit thrombin-induced platelet aggregation and are proved to be effective as anti-thrombotic drugs. Traditional screening assays for PAR-1 antagonists require molecular labeling or cell en
Publikováno v:
Biochemical Pharmacology. 83:435-442
The serotonin transporter (SERT) functions to transport serotonin (5-HT) from the extracellular space into neurons to maintain homeostatic control of 5-HT. It is the molecular target for selective serotonin reuptake inhibitor (SSRI) antidepressants.
Autor:
Garrick Paul Smith, Huailing Zhong, Arne Mørk, Thomas Ruhland, Benny Bang-Andersen, Kristen Frederiksen, Klaus Gjervig Jensen, Sandra Hogg, Morten Jørgensen, Tine B. Stensbøl, Søren Møller Nielsen
Publikováno v:
Journal of Medicinal Chemistry. 54:3206-3221
The synthesis and structure-activity relationship of a novel series of compounds with combined effects on 5-HT(3A) and 5-HT(1A) receptors and on the serotonin (5-HT) transporter (SERT) are described. Compound 5m (Lu AA21004) was the lead compound, di
Autor:
Kiho Han, Xinyan Huang, Kasper B. Hansen, Noel J. Boyle, Jan Egebjerg, Connie Sanchez, Huailing Zhong, Galina Muske
Publikováno v:
Neuroscience Letters. 462:207-212
The human serotonin transporter (hSERT) has primary and allosteric binding sites for escitalopram and R-citalopram. Previous studies have established that the interaction of these two compounds at a low affinity allosteric binding site of hSERT can a
Autor:
Laxminarayan G. Hegde, Mary W. Walker, Vrej Jubian, Mariusz Papp, Mohammad R. Marzabadi, Douglas A. Craig, Christophe P. G. Gerald, David H. Overstreet, Silke Miller, Gamini Chandrasena, Huailing Zhong, Toni D. Wolinsky, Douglas A. Marsteller, Xinyan Huang
Publikováno v:
Journal of Pharmacology and Experimental Therapeutics. 328:900-911
Neuropeptide Y (NPY) regulates physiological processes via receptor subtypes (Y1, Y2, Y4, Y5, and y6). The Y5 receptor is well known for its role in appetite. Based on expression in the limbic system, we hypothesized that the Y5 receptor might also m
Publikováno v:
The Journal of Peptide Research. 63:141-146
Regulators of G-protein signaling (RGS) proteins form a multifunctional signaling family. A key role of RGS proteins is binding to the G-protein Galpha-subunit and acting as GTPase-activating proteins (GAPs), thereby rapidly terminating G protein-cou
Autor:
D. Dong, C. J. Swanson, Kristen C. Klemenhagen, Luca Santarelli, Huailing Zhong, Laxminarayan G. Hegde, Michael Saxe, Indira Mendez, Douglas A. Craig, Mohammad R. Marzabadi, Denis J. David, Christophe P. G. Gerald, René Hen, K. A. Holick, X. I. Ping
Publikováno v:
Journal of Pharmacology and Experimental Therapeutics. 321:237-248
Melanin-concentrating hormone (MCH) is a hypothalamic neuropeptide that plays a role in the modulation of food intake and mood. In rodents, the actions of MCH are mediated via the MCHR1 receptor. The goal of this study was to investigate the effects
Publikováno v:
Methods in Pharmacology and Toxicology ISBN: 9781493926169
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c006ba180f486951f956e63a07fba8b4
https://doi.org/10.1007/978-1-4939-2617-6_12
https://doi.org/10.1007/978-1-4939-2617-6_12
Autor:
Huailing Zhong, Ying Fu, Richard R. Neubig, Louis G. D'Alecy, Richard M. Mortensen, Xinyan Huang
Publikováno v:
Circulation Research. 98:659-666
Cardiac automaticity is controlled by G protein–coupled receptors, such as adrenergic, muscarinic, and adenosine receptors. The strength and duration of G protein signaling is attenuated by regulator of G protein signaling (RGS) proteins acting as