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30 results on '"Yang, Shifan"'

16. Crystal structure of the Frizzled 4 receptor in a ligand-free state

Author

Yang, Shifan, Wu, Yiran, Xu, Ting-Hai, de Waal, Parker W., He, Yuanzheng, Pu, Mengchen, Chen, Yuxiang, DeBruine, Zachary J., Zhang, Bingjie, Zaidi, Saheem A., Popov, Petr, Guo, Yu, Han, Gye Won, Lu, Yang, Suino-Powell, Kelly, Dong, Shaowei, Harikumar, Kaleeckal G., Miller, Laurence J., Katritch, Vsevolod, Xu, H. Eric, Shui, Wenqing, Stevens, Raymond C., Melcher, Karsten, Zhao, Suwen, and Xu, Fei

Published
2018
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19. Substrate Binding and Inhibition of the Anion Exchanger 1 Transporter

Author

Capper, Michael J., primary, Yang, Shifan, additional, Stone, Alexander C., additional, Vatansever, Sezen, additional, Zilberg, Gregory, additional, Mathiharan, Yamuna Kalyani, additional, Habib, Raul, additional, Hutchinson, Keino, additional, Schlessinger, Avner, additional, Mezei, Mihaly, additional, Osman, Roman, additional, Zhang, Bin, additional, and Wacker, Daniel, additional

Published
2022
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20. Archaeal eukaryote-like serine/threonine protein kinase interacts with and phosphorylates a forkhead-associated-domain-containing protein

Author

Wang, Bin, Yang, Shifan, Zhang, Lei, and He, Zheng-Guo

Subjects
Protein kinases -- Properties, Bacterial proteins -- Properties, Phosphorylation -- Research, Archaeabacteria -- Physiological aspects, Biological sciences
Abstract

Protein phosphorylation plays an important role in cell signaling. However, in the Archaea, little is known about which proteins are phosphorylated and which kinases are involved. In this study, we identified, for the first time, a typical eukaryote-like Ser/Thr protein kinase and its protein partner, a forkhead-associated (FHA)-domain-containing protein, from the archaeon Sulfolobus tokodaii strain 7. This protein kinase, ST1565, physically interacted with the FHA-domain-containing protein, ST0829, both in vivo and in vitro. ST1565 preferred [Mn.sup.2+] as a cofactor for autophosphorylation and for substrate phosphorylation; the optimal temperature for this was 45[degrees]C, and the optimal pH was 5.5 to 7.5. The critical amino acid residues of the conserved FHA and kinase domain sites were identified by performing a series of mutation assays. Thr329 was part of a major activation site in the kinase, while Thr326 was a negative regulation site. Several mutants with amino acid substitutions in the conserved FHA domain sites of ST0829 did not physically interact with ST1565. A structural model for the FHA domain demonstrated that the mutation sites were located at the edge of the protein and thus were in the domain that potentially interacts with ST1565. This report describes pioneering work on the third domain of life, the Archaea, showing that a protein kinase interacts with and phosphorylates an FHA-domain-containing protein. Our data provide critical information on the structural or functional characteristics of archaeal proteins and could help increase our understanding of fundamental signaling mechanisms in all three domains of life. doi:10.1128/JB.01471-09

Published
2010

23. Association between social capital and mental health among older people living with HIV: The Sichuan Older HIV-Infected Cohort Study (SOHICS)

Author

Han, Jiayu, primary, Jia, Peng, additional, Huang, Yuling, additional, Gao, Bo, additional, Yu, Bin, additional, Yang, Shifan, additional, Yu, Jun, additional, Xiong, Jun, additional, Liu, Chang, additional, Xie, Tian, additional, Dong, Peijie, additional, Yang, Chao, additional, Wang, Zixin, additional, and Yang, Shujuan, additional

Published
2020
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30. Molecular Basis of Human Trace Amine-Associated Receptor 1 Activation.

Author

Zilberg G, Parpounas AK, Warren AL, Yang S, and Wacker D

Abstract

The human trace amine-associated receptor 1 (hTAAR1, hTA1) is a key regulator of monoaminergic neurotransmission and the actions of psychostimulants. Despite preclinical research demonstrating its tractability as a drug target, its molecular mechanisms of activation remain unclear. Moreover, poorly understood pharmacological differences between rodent and human TA1 complicate the translation of findings from preclinical disease models into novel pharmacotherapies. To elucidate hTA1's mechanisms on the molecular scale and investigate the underpinnings of its divergent pharmacology from rodent orthologs, we herein report the structure of the human TA1 receptor in complex with a Gαs heterotrimer. Our structure reveals shared structural elements with other TAARs, as well as with its closest monoaminergic ortholog, the serotonin receptor 5-HT4R. We further find that a single mutation dramatically shifts the selectivity of hTA1 towards that of its rodent orthologs, and report on the effects of substituting residues to those found in serotonin and dopamine receptors. Strikingly, we also discover that the atypical antipsychotic medication and pan-monoaminergic antagonist asenapine potently and efficaciously activates hTA1. Together our studies provide detailed insight into hTA1 structure and function, contrast its molecular pharmacology with that of related receptors, and uncover off-target activities of monoaminergic drugs at hTA1., Competing Interests: Competing Interests The authors declare no competing interests

Published
2023
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