1. Solution Structure of the SH3 Domain of Phospholipase Cγ
D. Kohda, H. Hatanaka, M. Odaka, V. Mandiyan, A. Ullrich, J. Schlessinger, and F. Inagaki
Cell 72, 953-960 (1993).
PubMed: 0007681365

2. Solution Structure of the Link Module: A Hyaluronan-Binding Domain Involved in Extracellular Matrix Stability and Cell Migration
D. Kohda. C. J. Morton, A. A. Parkar, H. Hatanaka, F. M. Inagaki, I. D. Campbell, and A. J. Day
Cell, 86, 767-775 (1996).
PubMed: 0008797823

3. Structural Basis of Presequence Recognition by the Mitochondrial Protein Import Receptor Tom20
Y. Abe, Toshihiro S., T. Muto, K. Mihara, H. Torii, S. Nishikawa, T. Endo, and D. Kohda
Cell 100, 551-560 (2000).
PubMed: 0010721992

4. Solution Structure of the PX domain, a Target of the SH3 domain
H. Hiroaki, T. Ago, T. Ito, H. Sumimoto, and D. Kohda
Nature Struct. Biol. 8, 526-530 (2001).
PubMed: 0011373621

5. Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states.
Saitoh T, Igura M, Obita T, Ose T, Kojima R, Maenaka K, Endo T, Kohda D
Embo J 26, 4777-4787 (2007).
PubMed: 0017948058
This paper was selected as "Must Read " by Faculty of 1000 Biology (http://www.f1000biology.com/)

6. Rational design of crystal contact-free space in protein crystals for analyzing spatial distribution of motions within protein molecules
Matsuoka R, Shimada A, Komuro Y, Sugita Y, Kohda D
Protein Sci 25, 754–768 (2016).
PubMed: 26694222

7. Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation
Taguchi Y, Fujinami D, Kohda D
J Biol Chem 291, 11042–11054 (2016).
PubMed: 27997792

8. The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon.
Taguchi Y, Yamasaki T, Ishikawa M, Kawasaki Y, Yukimura R, Mitani M, Hirata K, Kohda D.
Commun Biol 4, 941 (2021).
PubMed: 34354228

9. The time-zero HSQC method improves the linear free energy relationship of a polypeptide chain through the accurate measurement of residue-specific equilibrium constants.
Hayashi S, Kohda D.
J Biomol NMR 76, 87-94 (2022).
PubMed: 35699866

10. Retrospective study for the universal applicability of the residue-based linear free energy relationship in the two-state exchange of protein molecules.
Fujinami D, Hayashi S, Kohda D.
Sci Rep. 12, 16843 (2022).
PubMed: 36207470

11. Residue-based correlation between equilibrium and rate constants is an experimental formulation of the consistency principle for smooth structural changes of proteins.
Kohda D, Hayashi S, Fujinami D.
Biophysics and Physicobiology 20, e200046 (2023).
PubMed: 38344030

Reviews

1. Functions of outer membrane receptors in mitochondrial protein import
Endo T, Kohda D
Biochim Biophys Acta 1592, 3-14 (2002).
PubMed: 12191763

2. Structural Biology of Oligosaccharyltransferases
Matsumoto S, Nyirenda J, Kohda D
in Glycoscience: Biology and Medicine, Pages 437-445
Publisher: Springer Japan
Editors: Taniguchi, N., Endo, T., Hart, G.W., Seeberger, P.H., Wong, C.-H.
Year of publication: 2014
print ISBN: 978-4-431-54840-9, e-book ISBN: 978-4-431-54841-6

3. Chapter 21: Protein ligand interactions studied by NMR
Hiroaki H, Kohda D
in Experimental approaches of NMR spectroscopy -Methodology and application to life science and materials science-
Publisher: Springer Singapore
Editor: The Nuclear Magnetic Resonance Society of Japan
Year of publication: 2017
print ISBN: 978-981-10-5965-0, e-book ISBN: 978-981-10-5966-7

4. “Multiple partial recognitions in dynamic equilibrium" in the binding sites of proteins form the molecular basis of promiscuous recognition of structurally diverse ligands
Kohda D
Biophys Rev 10, 421-433 (2018)
doi: 10.1007/s12551-017-0365-4
PubMed: 29243092

5. Structural Basis of Protein Asn-Glycosylation by Oligosaccharyltransferases
Kohda D
Glycobiophysics, Chapter 9 (Eds: Yoshiki Yamaguchi, Koichi Kato), Adv Exp Med Biol, Volume 1104
Chapter DOI 10.1007/978-981-13-2158-0_9
PubMed: 30484249