Author
T. Nishizawa
Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
Biology Disciplines
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2017-2023 · peak 2/yrCo-Author Collaboration Network
10 top collaborators · 27 mutual co-author links7 papers
Recent·Most cited
- BiochemistryNature CommunicationsPeer-reviewed
Structural basis of the regulation of normal and oncogenic methylation of nucleosomal histone H3 Lys36 by NSD2
K. Sato, A. Kumar, K. Hamada…·T. Sengoku
This study determines the cryo-EM structure of NSD2 bound to a nucleosome and identifies oncogenic mutations that increase its catalytic activity by altering the autoinhibitory loop conformation.
- Plant BiologybioRxiv
Tandem mass spectrum similarity-based network analysis using 13C-labeled and non-labeled metabolome data to identify the biosynthesis pathway of the blood pressure-lowering asparagus metabolite asparaptine A
R. Nakabayashi, Y. Yamada, T. Nishizawa…·K. Saito
The paper identifies the biosynthesis pathway of asparaptine A using metabolome network analysis and shows its blood pressure-lowering effects in mice.
DOI 10.1021/acs.jafc.1c01183 - BiochemistrybioRxiv
Cryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail
Y. Zhang, M. Inoue, A. Tsutsumi…·K. Inaba
Cryo-EM structures of SERCA2b reveal how the luminal extension tail regulates its activity by controlling conformational transitions between states.
- BiochemistrybioRxiv
Cryo-EM structures capturing the entire transport cycle of the P4-ATPase flippase
M. Hiraizumi, K. Yamashita, T. Nishizawa, O. Nureki
The paper reports cryo-EM structures of six intermediates in the ATP8A1-CDC50a flippase cycle, revealing the mechanism of phospholipid translocation.
- BiochemistrybioRxiv
Cryo-EM structure of the human L-type amino acid transporter 1 in complex with glycoprotein CD98hc
Y. Lee, P. Wiriyasermkul, C. Jin…·O. Nureki
This paper reports the cryo-EM structure of the human LAT1-CD98hc heterodimer, revealing its architecture and interactions, and maps disease mutations to explain congenital disorders.
- BiochemistrybioRxiv
Structure of the triose-phosphate/phosphate translocator reveals the basis of substrate specificity
Y. Lee, T. Nishizawa, M. Takemoto…·O. Nureki
This study determines the crystal structures of TPT bound to substrates, revealing the molecular basis of its strict 1:1 exchange mechanism.
DOI 10.1038/s41477-017-0022-8