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International Journal of Molecular Sciences|April 3, 2021
NMR-Guided Repositioning of Non-Steroidal Anti-Inflammatory Drugs into Tight Junction ModulatorsTakeshi Tenno, Kohki Kataoka, Natsuko Goda, et al.
Food & Function|January 28, 2022
Direct inhibition of the first PDZ domain of ZO-1 by glycyrrhizin is a possible mechanism of tight junction opening of Caco-2 cellsEmi Hibino, Natsuko Goda, Misaki Hisada, et al.
Protein Science : a Publication of the Protein Society|February 24, 2004
The PRESAT-vector: asymmetric T-vector for high-throughput screening of soluble protein domains for structural proteomicsNatsuko Goda, Takeshi Tenno, Hirotoshi Takasu, et al.
International Journal of Molecular Sciences|February 2, 2018
Discovery of Cryoprotective Activity in Human Genome-Derived Intrinsically Disordered ProteinsNaoki Matsuo, Natsuko Goda, Kana Shimizu, et al.
Molecules (Basel, Switzerland)|August 23, 2013
Accidental interaction between PDZ domains and diclofenac revealed by NMR-assisted virtual screeningTakeshi Tenno, Natsuko Goda, Yoshitaka Umetsu, et al.
Experimental Cell Research|July 8, 2008
Intracellular protein delivery activity of peptides derived from insulin-like growth factor binding proteins 3 and 5Natsuko Goda, Takeshi Tenno, Kosuke Inomata, et al.
European Journal of Pharmacology|August 4, 2020
High dose of baicalin or baicalein can reduce tight junction integrity by partly targeting the first PDZ domain of zonula occludens-1 (ZO-1)Misaki Hisada, Minami Hiranuma, Mio Nakashima, et al.
Biomolecular NMR Assignments|June 7, 2011
¹H, ¹³C, and ¹⁵N resonance assignment of the SPFH domain of human stomatinTomoyuki Tsuruta, Natsuko Goda, Yoshitaka Umetsu, et al.
Biochimica Et Biophysica Acta|March 29, 2011
Structural difference of vasoactive intestinal peptide in two distinct membrane-mimicking environmentsYoshitaka Umetsu, Takeshi Tenno, Natsuko Goda, et al.
Current Research in Structural Biology|June 6, 2022
A cryptic phosphate-binding pocket on the SPFH domain of human stomatin that regulates a novel fibril-like self-assemblyKoki Kataoka, Shota Suzuki, Takeshi Tenno, et al.
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