@article{oai:repo.qst.go.jp:00086471,
 author = {Qingzhen, Yu, and Katsushi, Kumata and Jian, Rong, and Zhen, Chen, and Tomoteru, Yamasaki and Jiahui, Chen, and Zhiwei, Xiao, and Hideki, Ishii and Atsuto, Hiraishi and Tuo, Shao, and Zhang, Yiding and Kuan, Hu and Lin, Xie and Masayuki, Fujinaga and Chunyu, Zhao, and Wakana, Mori and Thomas, Collier, and Ahmed, Haider, and Susumu, Tomita, and Zhang, Ming-Rong and Steven, Liang, and Katsushi, Kumata and Tomoteru, Yamasaki and Hideki, Ishii and Atsuto, Hiraishi and Zhang, Yiding and Kuan, Hu and Lin, Xie and Masayuki, Fujinaga and Wakana, Mori and Zhang, Ming-Rong},
 issue = {13},
 journal = {Journal of Medicinal Chemistry},
 month = {Jun},
 note = {ABSTRACT: The transmembrane α-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid (AMPA) receptor regulatory protein γ-8 (TARP γ-8)
constitutes an auxiliary subunit of AMPA receptors, which mediates various
brain functions including learning and memory. TARP γ-8 has emerged as a
promising therapeutic target for central nervous system disorders. Despite
considerable efforts, previously reported TARP γ-8 PET radioligands, such as
[
11C]TARP-1903 and [11C]TARP-1811 series, were plagued by limited brain
uptake and/or high nonspecific binding in vivo. Herein, we developed two
novel 11C-labeled probes, [11C]8 and [11C]15 (also named as [11C]TARP2105), of which the latter exhibited a reasonable brain uptake as well as
specific binding toward TARP γ-8 both in vitro and in vivo, as confirmed by
blocking experiments with the commercially available TARP γ-8 inhibitor,
JNJ-55511118 in the TARP γ-8-rich hippocampus. Overall, [11C]15 exhibited
promising tracer characteristics and proved to be a lead positron-emission tomography ligand for the non-invasive quantification of
TARP γ-8 in the mammalian brain.},
 pages = {9144--9158},
 title = {Imaging of transmembrane AMPA receptor regulatory  protein by positron emission tomography},
 volume = {65},
 year = {2022}
}