Hiro Furukawa

Hiro Furukawa


Ph.D., The University of Tokyo, 2001

furukawa@cshl.edu | 516-367-8872

Furukawa Lab Website   Faculty Profile

The nervous system transmits information by passing chemical signals from one nerve cell to the others. This signal transmission relies on a variety of proteins to receive and transmit the chemical signals. My group studies the structure and function of neurotransmitter receptors and ion channels that regulate fundamental neuronal activities.

Hiro Furukawa’s lab studies receptor molecules involved in neurotransmission. Its members mainly focus on the structure and function of NMDA (N-methyl-d-aspartate) receptors — ion channels that mediate excitatory transmission. Dysfunctional NMDA receptors cause neurological disorders and diseases including Alzheimer’s disease, Parkinson’s disease, schizophrenia, depression, and stroke-related ischemic injuries. The Furukawa lab is working to solve the threedimensional structure of the very large NMDA receptor by dividing it into several domains. They seek to understand the pharmacological specificity of neurotransmitter ligands and allosteric modulators in different subtypes of NMDA receptors at the molecular level. Toward this end, they use cutting-edge techniques in X-ray crystallography to obtain crystal structures of the NMDA receptor domains and validate structure-based functional hypotheses by a combination of biophysical techniques including electrophysiology, fluorescence analysis, isothermal titration calorimetry, and analytical centrifugation. Crystal structures of NMDA receptors serve as a blueprint for creating and improving the design of therapeutic compounds with minimal side effects for treating neurological disorders and diseases. During the last several years, the team discovered and mapped several regulatory sites in specific classes of NMDA receptors, progress that now opens the way to the development of a new potential class of drugs to modulate the receptor activity.

See all Furukawa news

Selected Publications

On the molecular nature of large-pore channels.

15 Apr 2021 | Journal of Molecular Biology | :166994
Syrjanen, Johanna, Michalski, Kevin, Kawate, Toshimitsu, Furukawa, Hiro

Hodgkin-Huxley-Katz Prize Lecture: Genetic and pharmacological control of glutamate receptor channel through a highly conserved gating motif

Aug 2020 | The Journal of Physiology | 598(15):3071-3083
Perszyk, R, Myers, S, Yuan, H, Gibb, A, Furukawa, H, Sobolevsky, A, Traynelis, S

Publisher Correction: Structure and assembly of calcium homeostasis modulator proteins.

Mar 2020 | Nature Structural and Molecular Biology | 27(3):305
Syrjanen, Johanna, Michalski, Kevin, Chou, Tsung-Han, Grant, Timothy, Rao, Shanlin, Simorowski, Noriko, Tucker, Stephen, Grigorieff, Nikolaus, Furukawa, Hiro

The cryo-EM structure of a pannexin 1 reveals unique motifs for ion selection and inhibition

12 Feb 2020 | eLife | 9
Michalski, K, Syrjanen, J, Henze, E, Kumpf, J, Furukawa, H, Kawate, T

All Publications

Dendritic, delayed, and stochastic CaMKII activation underlies behavioral time scale plasticity in CA1 synapses

01 Aug 2023 | bioRxiv
Jain, Anant, Nakahata, Yoshihisa, Watabe, Tetsuya, Rusina, Polina, South, Kelly, Adachi, Kengo, Yan, Long, Simorowski, Noriko, Furukawa, Hiro, Yasuda, Ryohei

Structure of human CALHM1 reveals key locations for channel regulation and blockade by ruthenium red.

28 Jun 2023 | Nature Communications | 14(1):3821
Syrjänen, Johanna, Epstein, Max, Gómez, Ricardo, Furukawa, Hiro

Novel GluN2B-Selective NMDA Receptor Negative Allosteric Modulator Possesses Intrinsic Analgesic Properties and Enhances Analgesia of Morphine in a Rodent Tail Flick Pain Model

13 Feb 2023 | ACS Chemical Neuroscience
Harris, Lynnea, Regan, Michael, Myers, Scott, Nocilla, Kelsey, Akins, Nicholas, Tahirovic, Yesim, Wilson, Lawrence, Dingledine, Ray, Furukawa, Hiro, Traynelis, Stephen, Liotta, Dennis

Excitatory and inhibitory D-serine binding to the NMDA receptor

27 Oct 2022 | eLife | 11:e77645
Yovanno, Remy, Chou, Tsung, Brantley, Sarah, Furukawa, Hiro, Lau, Albert

Structural insights into assembly and function of GluN1-2C, GluN1-2A-2C, and GluN1-2D NMDARs

20 Oct 2022 | Molecular Cell | :S1097-2765(22)00965
Chou, Tsung-Han, Kang, Hyunook, Simorowski, Noriko, Traynelis, Stephen, Furukawa, Hiro

GluN2A-selective NMDA receptor antagonists: Mimicking the U-shaped bioactive conformation of TCN-201 by a [2.2]paracyclophane system

28 Sep 2022 | ChemMedChem: chemistry enabling drug discovery
Steigerwald, Ruben, Chou, Tsung-Han, Furukawa, Hiro, Wünsch, Bernhard

See more publications