Laboratory for Protein Functional and Structural Biology
- E-mail：mikako.shirouzu[at]riken.jpPlease replace [at] with @.
Establishment of a structural analysis technology platform that contributes to "life innovation" such as drug development and medical treatment.
The high-resolution structural information of proteins related to diseases shall increasingly become important for drug development leading to future individualized medicine. We plan to establish a structural analysis technology platform to contribute to "Life innovation" such as drug discovery as well as development of methods for the sample preparation of challenging proteins including membrane proteins/biomolecular complexes and for the structural analysis by cryo-electron microscopy (cryo-EM). The 3D-structural information will be used for in-silico screening/design of chemical compounds and for dynamic structural analysis toward simulation research of cell function.
cryo-EM (FEI Tecnai Arctica)
- Three-dimensional structure determination for drug development
- Development of methods for preparing difficult proteins including membrane proteins
- Structural analysis for huge complex of biomolecules by cryo-EM
Main Publications List
- Zyryanova AF, Kashiwagi K, Rato C, et al.
ISRIB blunts the integrated stress response by allosterically antagonising the inhibitory effect of phosphorylated eIF2 on eIF2B.
Molecular Cell (2020)doi: 10.1016/j.molcel.2020.10.031
- Needham D M, Yoshizawa S, Hosaka T, et al.
A distinct lineage of giant viruses brings a rhodopsin photosystem to unicellular marine predators.
Proceedings of the National Academy of Sciences of the United States of America 116(41), 20574-20583 (2019) doi: 10.1073/pnas.1907517116.
- Lee Y, Wiriyasermkul P, Jin C, et al.
Cryo-EM structure of the human L-type amino acid transporter 1 in complex with glycoprotein CD98hc.
Nature Structural & Molecular Biology 26(6), 510-517 (2019) doi: 10.1038/s41594-019-0237-7
- Yokoyama T, Machida K, Iwasaki W, et al.
HCV IRES Captures an Actively Translating 80S Ribosome.
Molecular Cell 74(6), 1205-1214 e1208 (2019) doi: 10.1016/j.molcel.2019.04.022.
- Kashiwagi K, Yokoyama T, Nishimoto M, et al.
Structural basis for eIF2B inhibition in integrated stress response.
Science 364(6439), 495-499 (2019) doi: 10.1126/science.aaw4104.
- Ehara H, Kujirai T, Fujino Y, et al.
Structural insight into nucleosome transcription by RNA polymerase II with elongation factors.
Science 363(6428), 744-747 (2019) doi: 10.1126/science.aav8912.
- Kujirai T, Ehara H, Fujino Y, et al.
Structural basis of the nucleosome transition during RNA polymerase II passage.
Science 362(6414). 595-598 (2018) doi: 10.1126/science.aau9904
- Shigematsu H, Imasaki T, Doki C, et al.
Structural insight into microtubule stabilization and kinesin inhibition by Tau-family MAPs.
The Journal of Cell Biology 217(12).4155-4163 (2018) doi: 10.1083/jcb.201711182
- Shima T, Morikawa M, Kaneshiro J, et al.
Kinesin-binding–triggered conformation switching of microtubules contributes to polarized transport.
The Journal of Cell Biology 217(12).4164-4183 (2018) doi: 10.1083/jcb.201711178
- Yamagata A, Miyazaki Y, Yokoi N, et al.
Structural basis of epilepsy-related ligand–receptor complex LGI1–ADAM22.
Nature communications 9(1). 1546 (2018) doi: 10.1038/s41467-018-03947-w
- Matsuda T, Ito T, Takemoto C, et al.
Cell-free synthesis of functional antibody fragments to provide a structural basis for antibody-antigen interaction.
PLoS One 13(2). e0193158(2018) doi: 10.1371/journal.pone.0193158