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医学教育・国際化推進センター

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Erik Walinda

Erik Walinda

Message

Dear students and fellow scientists. How are you? I hope you are having a great day today. Thank you for checking out this page. I would like to keep it brief and share only one one sentence as a message. This might sound a little bit harsh to some ears, but I would like to share quote from one of my professors in Germany – what he told me before I left for Japan to do science. Here it goes:

“At the end of the day, if you don't write the paper, it is as if you never did the work.”

Feel free to also check out my Google Scholar page and my personal site.

Publications

原著論文

Transient Diffusive Interactions with a Protein Crowder Affect Aggregation Processes of Superoxide Dismutase 1 β-barrel

Naoto Iwakawa, Daichi Morimoto, Erik Walinda, Sarah Leeb, Masahiro Shirakawa, Jens Danielsson, and Kenji Sugase

J Phys Chem B 2021; in press DOI

Structural dynamics of double-stranded DNA with epigenome modification

Daichi Morimoto, Erik Walinda, Kyohei Arita, and Kenji Sugase

Biochemistry 60 (8):573-583, 2021

Structural dynamics of double-stranded DNA with epigenome modification

Ayako Furukawa, Erik Walinda, Kyohei Arita, and Kenji Sugase

Nucleic Acids Res 49 (2):1152-1162, 2021

Quantitative monitoring of ubiquitination/deubiquitination reaction cycles by 18O-incorporation

Yuka Tanaka, Daichi Morimoto, Erik Walinda, Kenji Sugase, and Masahiro Shirakawa

Biochem Biophys Res Com 529 (2):418-424, 2020

Tracking the 3D Rotational Dynamics in Nanoscopic Biological Systems

Ryuji Igarashi, Takuma Sugi, Shingo Sotoma, Takuya Genjo, Yuta Kumiya, Erik Walinda, Hiroshi Ueno, Kazuhiro Ikeda, Hitoshi Sumiya, Hidehito Tochio, Yohsuke Yoshinari, Yoshi Harada, and Masahiro Shirakawa

J Am Chem Soc 142(16):7542-7554, 2020

Pinpoint analysis of a protein in slow exchange using F1F2-selective ZZ-exchange spectroscopy: assignment and kinetic analysis

Mayu Nishizawa, Erik Walinda, Daichi Morimoto, and Kenji Sugase

J Biomol NMR 2020

Visualizing protein motion in Couette flow by all-atom molecular dynamics

Erik Walinda, Daichi Morimoto, Masahiro Shirakawa, Ulrich Scheler, and Kenji Sugase

Biochim Biophys Acta Gen Subj 1864(2):129383, 2019

NMR resonance assignments of the NZF domain of mouse HOIL-1L free and bound to linear di-ubiquitin

Naoki Ishii, Erik Walinda, Naoto Iwakawa, Daichi Morimoto, Kazuhiro Iwai, Kenji Sugase, and Masahiro Shirakawa

Biomol NMR Assign 13(1):149-153, 2018

Backbone and side-chain resonance assignments of the methyl-CpG-binding domain of MBD6 from Arabidopsis thaliana

Naoto Iwakawa, Yutaka Mahana, Arina Ono, Izuru Ohki, Erik Walinda, Daichi Morimoto, Kenji Sugase, and Masahiro Shirakawa

Biomol NMR Assign 13(1):59-62, 2018

Resolving biomolecular motion and interactions by R2 and R1ρ Relaxation Dispersion NMR

Erik Walinda, Daichi Morimoto, and Kenji Sugase

Methods 148:28-38, 2018

Cooperative domain formation by homologous motifs in HOIL-1L and SHARPIN plays crucial roles in LUBAC stabilization.

Fujita, H., Tokunaga, A., Shimizu, S., Whiting, A. L., Aguilar-Alonso, F., Takagi, K., Walinda, E., Sasaki, Y., Shimokawa, T., Mizushima, T., Ohki, I., Ariyoshi, M., Tochio, H., Bernal, F., Shirakawa, M., and Iwai, K.

Cell Reports 23(4):1192-1204, 2018. DOI

Overview of Relaxation Dispersion NMR Spectroscopy to Study Protein Dynamics and Protein-Ligand Interactions

Erik Walinda, Daichi Morimoto, and Kenji Sugase

Curr Protoc Protein Sci 92(1):e57, 2018 DOI

Hydrogen-Deuterium Exchange Profiles of Polyubiquitin Fibrils

Daichi Morimoto, Ryo Nishizawa, Erik Walinda, Shingo Takashima, Kenji Sugase, and Masahiro Shirakawa

Polymers 10(3):240, 2018

Isolation and characterization of a minimal building block of polyubiquitin fibrils

Daichi Morimoto, Erik Walinda, Mayo Shinke, Kenji Sugase, and Masahiro Shirakawa

Sci Rep 8:2711, 2018

Elucidating Functional Dynamics by R1ρ and R2 Relaxation Dispersion NMR Spectroscopy

Erik Walinda and Kenji Sugase

Experimental Approaches of NMR Spectroscopy pages 197-225. Springer, 2017

Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR

Naoto Iwakawa, Daichi Morimoto, Erik Walinda, Yasushi Kawata, Masahiro Shirakawa, and Kenji Sugase

Int J Mol Sci 18(11):2271, 2017

High-Sensitivity Rheo-NMR Spectroscopy for Protein Studies

Daichi Morimoto, Erik Walinda, Naoto Iwakawa, Mayu Nishizawa, Yasushi Kawata, Akihiko Yamamoto, Masahiro Shirakawa, Ulrich Scheler, and Kenji Sugase

Anal Chem 89(14):7286-7290, 2017

Biological and Physicochemical Functions of Ubiquitylation Revealed by Synthetic Chemistry Approaches

Daichi Morimoto, Erik Walinda, Masahiro Shirakawa, and Kenji Sugase

Int J Mol Sci 18(6):1145, 2017

F1F2-Selective NMR Spectroscopy

Erik Walinda, Daichi Morimoto, Masahiro Shirakawa, and Kenji Sugase

J Biomol NMR 68:41-52, 2017

Practical Considerations for Investigation of Protein Conformational Dynamics by 15N R1ρ Relaxation Dispersion

Erik Walinda, Daichi Morimoto, Masahiro Shirakawa, and Kenji Sugase

J Biomol NMR 67(3):201-209, 2017

Backbone Resonance Assignments of Monomeric SOD1 in Dilute and Crowded Environments

Naoto Iwakawa, Daichi Morimoto, Erik Walinda, Kenji Sugase, and Masahiro Shirakawa

Biomol NMR Assign 11(1):81-84, 2017

Efficient Identification and Analysis of Chemical Exchange in Biomolecules by R1ρ Relaxation Dispersion with Amaterasu

Erik Walinda, Daichi Morimoto, Mayu Nishizawa, Masahiro Shirakawa, and Kenji Sugase

Bioinformatics 32:2539-2541, 2016

Dual Function of Phosphoubiquitin in E3 Activation of Parkin

Erik Walinda, Daichi Morimoto, Kenji Sugase, and Masahiro Shirakawa

J Biol Chem 291(32):16879-16891, 2016

Ubiquitylation Directly Induces Folding Destabilization of Substrate Proteins

Daichi Morimoto, Erik Walinda, Kenji Sugase, and Masahiro Shirakawa

Sci Rep 6:39453, 2016

The unexpected role of polyubiquitin chains in the formation of fibrillar aggregates.

Morimoto, D., Walinda, E., Fukada, H., Sou, Y. S., Kageyama, S., Hoshino, M., Fujii, T., Tsuchiya, H., Saeki, Y., Arita, K., Ariyoshi, M., Tochio, H., Iwai, K., Namba, K., Komatsu, M., Tanaka, K., Shirakawa, M.

Nature Commun. 6:6116, 2015. DOI

Solution Structure of the Ubiquitin-associated (UBA) Domain of Human Autophagy Receptor NBR1 and Its Interaction with Ubiquitin and Polyubiquitin

Erik Walinda, Daichi Morimoto, Kenji Sugase, Tsuyoshi Konuma, Hidehito Tochio, and Masahiro Shirakawa

J Biol Chem 289(20):13890-13902, 2014