Tsung-Han Chou - Publications

Affiliations: 
Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 

7 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2022 Chou TH, Kang H, Simorowski N, Traynelis SF, Furukawa H. Structural insights into assembly and function of GluN1-2C, GluN1-2A-2C, and GluN1-2D NMDARs. Molecular Cell. PMID 36309015 DOI: 10.1016/j.molcel.2022.10.008  0.741
2022 Yovanno RA, Chou TH, Brantley SJ, Furukawa H, Lau AY. Excitatory and inhibitory D-serine binding to the NMDA receptor. Elife. 11. PMID 36301074 DOI: 10.7554/eLife.77645  0.71
2022 Steigerwald R, Chou TH, Furukawa H, Wünsch B. GluN2A-selective NMDA receptor antagonists: Mimicking the U-shaped bioactive conformation of TCN-201 by a [2.2]paracyclophane system. Chemmedchem. PMID 36169098 DOI: 10.1002/cmdc.202200484  0.699
2022 Chou TH, Epstein M, Michalski K, Fine E, Biggin PC, Furukawa H. Structural insights into binding of therapeutic channel blockers in NMDA receptors. Nature Structural & Molecular Biology. 29: 507-518. PMID 35637422 DOI: 10.1038/s41594-022-00772-0  0.769
2020 Chou TH, Tajima N, Romero-Hernandez A, Furukawa H. Structural Basis of Functional Transitions in Mammalian NMDA Receptors. Cell. PMID 32610085 DOI: 10.1016/J.Cell.2020.05.052  0.585
2020 Syrjanen JL, Michalski K, Chou TH, Grant T, Rao S, Simorowski N, Tucker SJ, Grigorieff N, Furukawa H. Publisher Correction: Structure and assembly of calcium homeostasis modulator proteins. Nature Structural & Molecular Biology. PMID 32066965 DOI: 10.1038/S41594-020-0396-6  0.624
2020 Syrjanen JL, Michalski K, Chou TH, Grant T, Rao S, Simorowski N, Tucker SJ, Grigorieff N, Furukawa H. Structure and assembly of calcium homeostasis modulator proteins. Nature Structural & Molecular Biology. PMID 31988524 DOI: 10.1038/s41594-019-0369-9  0.664
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