D. Kohda

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Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases

S. Matsumoto, A. Shimada, D. Kohda, 2013, BMC Structural Biology.

Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site.

D. Kohda, T. Katayama, T. Ueda, 2005, Biochemical and biophysical research communications.

Identification of the receptor-recognition surface of bombyxin-II, an insulin-like peptide of the silkmoth Bombyx mori: critical importance of the B-chain central part.

D. Kohda, K. Nagata, F. Inagaki, 1995, Journal of molecular biology.

Three-dimensional solution structure of bombyxin-II an insulin-like peptide of the silkmoth Bombyx mori: structural comparison with insulin and relaxin.

D. Kohda, K. Nagata, F. Inagaki, 1995, Journal of molecular biology.

Structure-activity relationships of mu-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations.

D. Kohda, F. Inagaki, H. Hatanaka, 1994, Biochemistry.

Homogeneous sugar modification improves crystallization of measles virus hemagglutinin.

D. Kohda, M. Takeda, Y. Yanagi, 2008, Journal of virological methods.

Ligand-binding enhances the affinity of dimerization of the extracellular domain of the epidermal growth factor receptor.

I. Lax, J. Schlessinger, D. Kohda, 1997, Journal of biochemistry.

Expression, crystallization and preliminary X-ray diffraction analysis of human paired Ig-like type 2 receptor α (PILRα)

D. Kohda, K. Maenaka, K. Kuroki, 2008 .

Biophysical Characterization of O-Glycosylated CD99 Recognition by Paired Ig-like Type 2 Receptors*

D. Kohda, K. Maenaka, K. Kuroki, 2008, Journal of Biological Chemistry.

Protein-ligand interactions studied by NMR

D. Kohda, H. Hiroaki, 2018 .

Structural basis for mutual relief of the Rac guanine nucleotide exchange factor DOCK2 and its partner ELMO1 from their autoinhibited forms

T. Kigawa, S. Yokoyama, T. Kinashi, 2012, Proceedings of the National Academy of Sciences.

Entropically driven MHC class I recognition by human inhibitory receptor leukocyte Ig-like receptor B1 (LILRB1/ILT2/CD85j).

Y. Shirakihara, K. Tsumoto, D. Kohda, 2006, Journal of molecular biology.

Crystal Structure of the Human Monocyte-activating Receptor, “Group 2” Leukocyte Ig-like Receptor A5 (LILRA5/LIR9/ILT11)*

D. Kohda, M. Shiroishi, K. Maenaka, 2006, Journal of Biological Chemistry.

Tertiary structure of mouse epidermal growth factor determined by two-dimensional 1H NMR.

N. Go, D. Kohda, F. Inagaki, 1988, Journal of biochemistry.

Methionyl-tRNA synthetase gene from an extreme thermophile, Thermus thermophilus HB8. Molecular cloning, primary-structure analysis, expression in Escherichia coli, and site-directed mutagenesis.

O. Nureki, K. Suzuki, S. Yokoyama, 1991, The Journal of biological chemistry.

Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 Å resolution.

S. Matsumoto, D. Kohda, F. Inagaki, 2012, Biochemistry.

Structural Basis for Marburg Virus Neutralization by a Cross-Reactive Human Antibody

James E. Crowe, Yusuke Yanagi, Marnie L. Fusco, 2015, Cell.

Relayed HOHAHA, a useful method for extracting subspectra of individual components of sugar chains

A. Bax, D. Kohda, I. Shimada, 1989 .

A Radioisotope-free Oligosaccharyltransferase Assay Method.

D. Kohda, T. Yamasaki, 2019, Bio-protocol.

N‐Glycosylation with Synthetic Undecaprenyl Pyrophosphate‐Linked Oligosaccharide to Oligopeptides by PglB Oligosaccharyltransferase from Campylobacter jejuni

Taisuke Watanabe, D. Kohda, Yukishige Ito, 2015, Chembiochem : a European journal of chemical biology.

Quantitative assessment of the preferences for the amino acid residues flanking archaeal N-linked glycosylation sites.

D. Kohda, Mayumi Igura, 2011, Glycobiology.

New oligosaccharyltransferase assay method.

D. Kohda, K. Maenaka, Jun Kamishikiryo, 2007, Glycobiology.

Dual role of the receptor Tom20 in specificity and efficiency of protein import into mitochondria

D. Kohda, R. Jensen, T. Endo, 2010, Proceedings of the National Academy of Sciences.

Crystallization and preliminary X-ray analysis of mitochondrial presequence receptor Tom20 in complexes with a presequence from aldehyde dehydrogenase.

D. Kohda, T. Endo, K. Maenaka, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

Structure and activity of JAC1 J-domain implicate the involvement of the cochaperone activity with HSC70 in chloroplast photorelocation movement

D. Kohda, A. Takano, N. Suetsugu, 2010, Plant signaling & behavior.

Crystallographic and functional analyses of J-domain of JAC1 essential for chloroplast photorelocation movement in Arabidopsis thaliana.

D. Kohda, A. Takano, N. Suetsugu, 2010, Plant & cell physiology.

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation*

D. Kohda, Yuya Taguchi, D. Fujinami, 2016, The Journal of Biological Chemistry.

Crystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance.

S. Matsumoto, D. Kohda, F. Inagaki, 2013, Structure.

Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.

S. Yokoyama, D. Kohda, K. Saito, 2000, Journal of biochemistry.

Structural basis for the strict exclusion of proline from the N-glycosylation sequon

D. Kohda, K. Hirata, M. Mitani, 2021 .

Crystal contact-free conformation of an intrinsically flexible loop in protein crystal: Tim21 as the case study.

F. Tama, O. Miyashita, A. Shimada, 2020, Biochimica et biophysica acta. General subjects.

Molecular Basis of Presequence Recognition by the Mitochondrial Import Receptors.

D. Kohda, 2000 .

The BALB/c-specific polymorphic SIRPA enhances its affinity for human CD47, inhibiting phagocytosis against human cells to promote xenogeneic engraftment.

K. Akashi, H. Iwasaki, K. Takenaka, 2014, Experimental hematology.

Tertiary structure of erabutoxin b in aqueous solution as elucidated by two-dimensional nuclear magnetic resonance.

M. Oka, D. Kohda, F. Inagaki, 1994, Journal of molecular biology.

Active site of mu-conotoxin GIIIA, a peptide blocker of muscle sodium channels.

D. Kohda, Y. Ohizumi, Y. Ishida, 1991, The Journal of biological chemistry.

ジスルフィド結合型hla-g二量体を含む医薬組成物及びジスルフィド結合型hla-g二量体の製造方法

D. Kohda, M. Shiroishi, K. Maenaka, 2006 .

Composition pharmaceutique comprenant un dimere hla-g lie disulfide et procede de fabrication de ce dimere hla-g lie disulfide

D. Kohda, M. Shiroishi, K. Maenaka, 2006 .

Preparation and crystallization of the disulfide-linked HLA-G dimer.

D. Kohda, M. Shiroishi, K. Maenaka, 2006, Biochimica et biophysica acta.

Blockade of inflammatory responses by a small-molecule inhibitor of the Rac activator DOCK2.

S. Yokoyama, A. Suenaga, D. Kohda, 2012, Chemistry & biology.

Three-dimensional structure and receptor-recognition sites of bombyxin-II, an insulin-like brain-secretory peptide of the silkmoth

D. Kohda, K. Nagata, T. Kadowaki, 1999 .

Thermodynamic study of hybridization properties of heterochiral nucleic acids.

D. Kohda, H. Hiroaki, H. Urata, 2003, Biochemical and biophysical research communications.

NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.

T. Hosoya, D. Kohda, K. Morikawa, 2003, Protein engineering.

Purification, crystallization and preliminary X-ray diffraction studies of the soluble domain of the oligosaccharyltransferase STT3 subunit from the thermophilic archaeon Pyrococcus furiosus.

D. Kohda, K. Maenaka, T. Obita, 2007, Acta crystallographica. Section F, Structural biology and crystallization communications.

Structural Biology of Glycans

Katsunori Tanaka, M. Setou, D. Kohda, 2019, Glycoscience: Basic Science to Applications.

Ring A of nukacin ISK-1: a lipid II-binding motif for type-A(II) lantibiotic.

D. Kohda, H. Sahl, J. Nakayama, 2012, Journal of the American Chemical Society.

A 40-kDa epidermal growth factor/transforming growth factor alpha-binding domain produced by limited proteolysis of the extracellular domain of the epidermal growth factor receptor.

H. Kawasaki, K. Suzuki, A. Ullrich, 1993, The Journal of biological chemistry.

Uncoupling the hydrolysis of lipid-linked oligosaccharide from the oligosaccharyl transfer reaction by point mutations in yeast oligosaccharyltransferase

D. Kohda, T. Yamasaki, 2020, The Journal of Biological Chemistry.

Serotriflin, a CRISP family protein with binding affinity for small serum protein-2 in snake serum.

D. Kohda, K. Maenaka, K. Kuroki, 2008, Biochimica et biophysica acta.

Effects of targeting signal mutations in a mitochondrial presequence on the spatial distribution of the conformational ensemble in the binding site of Tom20

A. Shimada, D. Kohda, N. Maita, 2022, Protein science : a publication of the Protein Society.

Structural Basis of the Asparagine Side Chain Activation in N-Linked Protein Glycosylation

S. Matsumoto, D. Kohda, 2014 .

The benzylisoquinoline alkaloids, berberine and coptisine, act against camptothecin-resistant topoisomerase I mutants

D. Kohda, T. Ishizaki, K. Hanada, 2021, Scientific Reports.

The PX domain as a novel phosphoinositide- binding module.

T. Ito, D. Kohda, H. Sumimoto, 2001, Biochemical and biophysical research communications.

Trypanosoma brucei 14-3-3I and II proteins predominantly form a heterodimer structure that acts as a potent cell cycle regulator in vivo.

A. Schnaufer, H. Doi, D. Kohda, 2013, Journal of biochemistry.

Residue-based quadratic free energy relationship is a mathematical formulation of the consistency principle of protein folding

D. Kohda, D. Fujinami, Seiichiro Hayashi, 2022, bioRxiv.

Polypeptide chain fold of human transforming growth factor alpha analogous to those of mouse and human epidermal growth factors as studied by two-dimensional 1H NMR.

D. Kohda, I. Shimada, F. Inagaki, 1989, Biochemistry.

Metal Ion Induced Self-Assembly of a Designed Peptide into a Triple-Stranded α-Helical Bundle: A Novel Metal Binding Site in the Hydrophobic Core

Haruki Nakamura, Hidekazu Hiroaki, Daisuke Kohda, 1998 .

Structural Basis of Protein Asn-Glycosylation by Oligosaccharyltransferases.

D. Kohda, 2018, Advances in experimental medicine and biology.

Efficient Leukocyte Ig-like Receptor Signaling and Crystal Structure of Disulfide-linked HLA-G Dimer*

Kouhei Tsumoto, Daisuke Kohda, K. Tsumoto, 2006, Journal of Biological Chemistry.

NMR analyses of the conformations of L-isoleucine and L-valine bound to Escherichia coli isoleucyl-tRNA synthetase.

S. Yokoyama, D. Kohda, G. Kawai, 1987, Biochemistry.

Soft metal ions, Cd(II) and Hg (II), induce triple‐stranded α‐helical assembly and folding of a de novo designed peptide in their trigonal geometries

D. Kohda, H. Hiroaki, Toshiki Tanaka, 2000, Protein science : a publication of the Protein Society.

1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin

D. Kohda, I. Shimada, F. Inagaki, 1990, FEBS letters.

Structural basis for recognition of the nonclassical MHC molecule HLA-G by the leukocyte Ig-like receptor B2 (LILRB2/LIR2/ILT4/CD85d)

Kouhei Tsumoto, Eiji Kurimoto, Daisuke Kohda, 2006, Proceedings of the National Academy of Sciences.

Asn-linked oligosaccharide chain of a crenarchaeon, Pyrobaculum calidifontis, is reminiscent of the eukaryotic high-mannose-type glycan

D. Kohda, Yuya Taguchi, D. Fujinami, 2017, Glycobiology.

A simplified recipe for assigning amide NMR signals using combinatorial 14N amino acid inverse-labeling

Y. Nabeshima, D. Kohda, H. Hiroaki, 2011, Journal of Structural and Functional Genomics.

Activation of the superoxide-producing phagocyte NADPH oxidase requires co-operation between the tandem SH3 domains of p47phox in recognition of a polyproline type II helix and an adjacent alpha-helix of p22phox.

D. Kohda, K. Ogura, F. Inagaki, 2006, The Biochemical journal.

Solution structure of the PX domain, a target of the SH3 domain

Hidekazu Hiroaki, Tetsuro Ago, Daisuke Kohda, 2001, Nature Structural Biology.

Phosphorylation of p47phox directs phox homology domain from SH3 domain toward phosphoinositides, leading to phagocyte NADPH oxidase activation

Hidekazu Hiroaki, Tetsuro Ago, Daisuke Kohda, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Stalled replication forks: Making ends meet for recognition and stabilization

D. Kohda, H. Masai, Taku Tanaka, 2010, BioEssays : news and reviews in molecular, cellular and developmental biology.

Two conformations of DNA polymerase D-PCNA-DNA, an archaeal replisome complex, revealed by cryo-electron microscopy

D. Kohda, Y. Ishino, K. Morikawa, 2020, BMC biology.

Conformational ensemble of an intrinsically flexible loop in mitochondrial import protein Tim21 studied by modeling and molecular dynamics simulations.

F. Tama, O. Miyashita, D. Kohda, 2020, Biochimica et biophysica acta. General subjects.

Lipopolysaccharide binding of the mite allergen Der f 2

D. Kohda, H. Hatanaka, K. Okumura, 2009, Genes to cells : devoted to molecular & cellular mechanisms.

Complete Covalent Structure of Nisin Q, New Natural Nisin Variant, Containing Post-Translationally Modified Amino Acids

D. Kohda, J. Nakayama, M. Fukao, 2008, Bioscience, biotechnology, and biochemistry.

VHL-box and SOCS-box domains determine binding specificity for Cul2-Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases.

Keiichi I Nakayama, Daisuke Kohda, R. Conaway, 2004, Genes & development.

Crystal structure of measles virus hemagglutinin provides insight into effective vaccines

D. Kohda, M. Takeda, Y. Yanagi, 2007, Proceedings of the National Academy of Sciences.

Two Novel NKG2D Ligands of the Mouse H60 Family with Differential Expression Patterns and Binding Affinities to NKG2D1

M. Kasahara, D. Kohda, H. Chiba, 2008, The Journal of Immunology.

Patterns and Binding Affinities to NKG2D H60 Family with Differential Expression Two Novel NKG2D Ligands of the Mouse

M. Kasahara, D. Kohda, H. Chiba, 2008 .

Diverse recognition of non‐PxxP peptide ligands by the SH3 domains from p67phox, Grb2 and Pex13p

Daisuke Kohda, D. Kohda, H. Sumimoto, 2002, The EMBO journal.

Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases*

Daisuke Kohda, D. Kohda, Nobuo Maita, 2009, The Journal of Biological Chemistry.

Structure‐guided identification of a new catalytic motif of oligosaccharyltransferase

D. Kohda, K. Maenaka, T. Obita, 2008, The EMBO journal.

Peptide library approach with a disulfide tether to refine the Tom20 recognition motif in mitochondrial presequences.

D. Kohda, T. Muto, T. Endo, 2003, Journal of molecular biology.

NMR identification of the Tom20 binding segment in mitochondrial presequences.

D. Kohda, T. Muto, T. Endo, 2001, Journal of molecular biology.

Structural Basis of Presequence Recognition by the Mitochondrial Protein Import Receptor Tom20

D. Kohda, S. Nishikawa, T. Muto, 2000, Cell.

Thermostable valyl‐tRNA, isoleucyl‐tRNA and methionyl‐tRNA synthetases from an extreme thermophile Thermus thermophilus HB8: protein structure and Zn2+ binding

S. Yokoyama, D. Kohda, T. Miyazawa, 1984, FEBS letters.

Disulfide Bond Structure of Human Epidermal Growth Factor Receptor*

I. Lax, J. Schlessinger, D. Kohda, 1998, The Journal of Biological Chemistry.

Extensive polymorphisms of LILRB1 (ILT2, LIR1) and their association with HLA-DRB1 shared epitope negative rheumatoid arthritis.

Hiroshi Hashimoto, Katsushi Tokunaga, Masafumi Takiguchi, 2005, Human molecular genetics.

Crystallographic snapshots of Tom20-mitochondrial presequence interactions with disulfide-stabilized peptides.

D. Kohda, T. Saitoh, T. Ose, 2011, Biochemistry.

A region C-terminal to the proline-rich core of p47phox regulates activation of the phagocyte NADPH oxidase by interacting with the C-terminal SH3 domain of p67phox.

D. Kohda, H. Sumimoto, K. Takeshige, 2005, Archives of biochemistry and biophysics.

The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon

D. Kohda, K. Hirata, M. Mitani, 2021, Communications biology.

Structures of the prefusion form of measles virus fusion protein in complex with inhibitors

R. Plemper, K. Tsumoto, D. Kohda, 2018, Proceedings of the National Academy of Sciences.

Trisaccharide containing α2,3-linked sialic acid is a receptor for mumps virus

D. Kohda, T. Terada, K. Shimizu, 2016, Proceedings of the National Academy of Sciences of the United States of America.

Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos

A. Ullrich, J. Schlessinger, S. Ishii, 1994, Nature Structural Biology.

X‐ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation

D. Kohda, T. Katayama, T. Ueda, 2017, FEBS letters.

Tertiary structure of conotoxin GIIIA in aqueous solution.

Y. Yanagawa, T. Abe, D. Kohda, 1991, Biochemistry.

Solution Structure of the Link Module: A Hyaluronan-Binding Domain Involved in Extracellular Matrix Stability and Cell Migration

I. Campbell, C. Morton, D. Kohda, 1996, Cell.

Architecture of the DNA polymerase B-proliferating cell nuclear antigen (PCNA)-DNA ternary complex

D. Kohda, Y. Ishino, K. Morikawa, 2011, Proceedings of the National Academy of Sciences.

Nuclear-magnetic-resonance studies of human epidermal growth factor.

I. Campbell, R. Cooke, D. Kohda, 1990, European journal of biochemistry.

Crystallographic and functional studies of very short patch repair endonuclease.

N. Kunishima, D. Kohda, K. Morikawa, 1999, Molecular cell.

The RecJ2 protein in the thermophilic archaeon Thermoplasma acidophilum is a 3′-5′ exonuclease that associates with a DNA replication complex

D. Kohda, Y. Ishino, S. Ishino, 2017, The Journal of Biological Chemistry.

Disordered interdomain region of Gins is important for functional tetramer formation to stimulate MCM helicase in Thermoplasma acidophilum

D. Kohda, Y. Ishino, S. Ishino, 2015, Bioscience, biotechnology, and biochemistry.

Activation of the MCM helicase from the thermophilic archaeon, Thermoplasma acidophilum by interactions with GINS and Cdc6-2

D. Kohda, Y. Ishino, N. Birkeland, 2014, Extremophiles.

The Archaeal DNA Primase

D. Kohda, K. Komori, Y. Ishino, 2001, The Journal of Biological Chemistry.

Archaeal primase bridging the gap between RNA and DNA polymerases

D. Kohda, K. Komori, Y. Ishino, 2001, Current Biology.

Secondary structural features of modules M2 and M3 of barnase in solution by NMR experiment and distance geometry calculation

N Go, M Go, N. Go, 1993, Proteins.

Phagocytosis is mediated by two-dimensional assemblies of the F-BAR protein GAS7

A. Kitao, A. Shimada, D. Kohda, 2019, Nature Communications.

Solution structure of the epidermal growth factor‐like domain of heregulin‐alpha, a ligand for p180erbB‐4.

D. Kohda, K. Nagata, S. Matsuda, 1994, The EMBO journal.

Design of a Heterotrimeric α-Helical Bundle by Hydrophobic Core Engineering

D. Kohda, H. Hiroaki, Toshiki Tanaka, 2000 .

Trajectory analysis of NMR structure calculations

D. Kohda, F. Inagaki, 1995, Journal of biomolecular NMR.

Tom20 recognizes mitochondrial presequences through dynamic equilibrium among multiple bound states

D. Kohda, T. Endo, T. Saitoh, 2007, The EMBO journal.

Solution structure of the SH3 domain of phospholipase C-γ

J. Schlessinger, D. Kohda, V. Mandiyan, 1993, Cell.

Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2.

A. Ullrich, J. Schlessinger, D. Kohda, 1994, Structure.

Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions.

D. Kohda, F. Inagaki, 1994, Biochemistry.

TRPV4 channel activity is modulated by direct interaction of the ankyrin domain to PI(4,5)P2

A. Kitao, Y. Mori, A. Shimada, 2014, Nature Communications.

A Critical Role of the 3′ Terminus of Nascent DNA Chains in Recognition of Stalled Replication Forks*

Hisao Masai, Taku Tanaka, Daisuke Kohda, 2003, Journal of Biological Chemistry.

Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation

S. Matsumoto, A. Shimada, D. Kohda, 2013, Proceedings of the National Academy of Sciences.

Functions of outer membrane receptors in mitochondrial protein import.

Daisuke Kohda, D. Kohda, T. Endo, 2002, Biochimica et biophysica acta.

Computational investigation of the conformational dynamics in Tom20‐mitochondrial presequence tethered complexes

F. Tama, O. Miyashita, D. Kohda, 2018, Proteins.

“Multiple partial recognitions in dynamic equilibrium” in the binding sites of proteins form the molecular basis of promiscuous recognition of structurally diverse ligands

D. Kohda, 2017, Biophysical Reviews.

Selective Control of Oligosaccharide Transfer Efficiency for the N-Glycosylation Sequon by a Point Mutation in Oligosaccharyltransferase*

D. Kohda, Mayumi Igura, 2011, The Journal of Biological Chemistry.

Structural basis of the 3′‐end recognition of a leading strand in stalled replication forks by PriA

D. Kohda, T. Shirai, H. Masai, 2007, The EMBO journal.

Structural elucidation of an asparagine-linked oligosaccharide from the hyperthermophilic archaeon, Archaeoglobus fulgidus.

S. Matsumoto, D. Kohda, J. Nyirenda, 2015, Carbohydrate research.

Escherichia coli PriA Protein, Two Modes of DNA Binding and Activation of ATP Hydrolysis*

D. Kohda, H. Masai, T. Mizukoshi, 2007, Journal of Biological Chemistry.

DNA Binding of PriA Protein Requires Cooperation of the N-terminal D-loop/Arrested-fork Binding and C-terminal Helicase Domains*

K. Arai, D. Kohda, H. Masai, 2002, The Journal of Biological Chemistry.

Analysis of NMR spectra of sugar chains of glycolipids by multiple relayed COSY and 2D homonuclear

D. Kohda, F. Inagaki, A. Suzuki, 1987, FEBS letters.

Detection of weak ligand interactions of leukocyte Ig-like receptor B1 by fluorescence correlation spectroscopy.

D. Kohda, M. Shiroishi, K. Maenaka, 2007, Journal of immunological methods.

CHLOROPLAST UNUSUAL POSITIONING 1 is a new type of actin nucleation factor in plants

K. Hirose, A. Shimada, D. Kohda, 2020, bioRxiv.

Activation of the MCM helicase from the thermophilic archaeon, Thermoplasma acidophilum by interactions with GINS and Cdc6-2

D. Kohda, Y. Ishino, N. Birkeland, 2014, Extremophiles.

Structural basis for the recognition of two consecutive mutually interacting DPF motifs by the SGIP1 μ homology domain

A. Shimada, D. Kohda, A. Yamaguchi, 2016, Scientific Reports.

Solution structure of human insulin‐like growth factor II; recognition sites for receptors and binding proteins.

D. Kohda, K. Nagata, F. Inagaki, 1994, The EMBO journal.

The structure of an archaeal oligosaccharyltransferase provides insight into the strict exclusion of proline from the N-glycosylation sequon

D. Kohda, K. Hirata, T. Yamasaki, 2021, Communications Biology.

Two-State Exchange Dynamics in Membrane-Embedded Oligosaccharyltransferase Observed in Real-Time by High-Speed AFM.

T. Ando, D. Kohda, Y. Kawasaki, 2020, Journal of molecular biology.

Tethering an N-Glycosylation Sequon-Containing Peptide Creates a Catalytically Competent Oligosaccharyltransferase Complex.

S. Matsumoto, A. Shimada, D. Kohda, 2017, Biochemistry.

Crystal structure of the PX domain of Vps17p from Saccharomyces cerevisiae.

D. Kohda, K. Inaka, T. Obita, 2022, Acta crystallographica. Section F, Structural biology communications.

Functions of isolated domains of methionyl-tRNA synthetase from an extreme thermophile, Thermus thermophilus HB8.

S. Yokoyama, D. Kohda, T. Miyazawa, 1987, The Journal of biological chemistry.

Crystal structure of the human monocyte-activating receptor,

D. Kohda, M. Shiroishi, K. Maenaka, 2006 .

Residue-Specific Kinetic Insights into the Transition State in Slow Polypeptide Topological Isomerization by NMR Exchange Spectroscopy.

D. Kohda, D. Fujinami, Seiichiro Hayashi, 2021, The journal of physical chemistry letters.

Structure of epidermal growth factor bound to perdeuterated dodecylphosphocholine micelles determined by two-dimensional NMR and simulated annealing calculations.

D. Kohda, F. Inagaki, Fuyuhiko Inagaki, 1992, Biochemistry.

The time-zero HSQC method improves the linear free energy relationship of a polypeptide chain through the accurate measurement of residue-specific equilibrium constants

D. Kohda, Seiichiro Hayashi, 2022, Journal of Biomolecular NMR.

Retrospective study for the universal applicability of the residue-based linear free energy relationship in the two-state exchange of protein molecules

D. Kohda, D. Fujinami, Seiichiro Hayashi, 2022, Scientific Reports.

Mosaic Cooperativity in Slow Polypeptide Topological Isomerization Revealed by Residue-specific NMR Thermodynamic Analysis.

Y. Sugita, D. Kohda, Hiraku Oshima, 2020, The journal of physical chemistry letters.

The lantibiotic nukacin ISK-1 exists in an equilibrium between active and inactive lipid-II binding states

D. Kohda, T. Zendo, K. Sonomoto, 2018, Communications Biology.

SOLUTION STRUCTURE OF THE SH3 DOMAIN OF PHOSPHOLIPASE CGAMMA

D. Kohda, F. Inagaki, H. Hatanaka, 1994 .

Structural elucidation of an asparagine-linked oligosaccharide from the hyperthermophilic archaeon, Pyrococcus furiosus.

D. Kohda, K. Sonomoto, Takuya Noguchi, 2014, Carbohydrate research.

Nonprotein amino acid furanomycin, unlike isoleucine in chemical structure, is charged to isoleucine tRNA by isoleucyl-tRNA synthetase and incorporated into protein.

S. Yokoyama, D. Kohda, T. Kohno, 1990, The Journal of biological chemistry.

A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance.

D. Kohda, A. Otaka, H. Tamamura, 1993, Biochimica et biophysica acta.

Three-dimensional nuclear magnetic resonance structures of mouse epidermal growth factor in acidic and physiological pH solutions.

D. Kohda, Fuyuhiko Inagaki, 1994, Biochemistry.

Characterization of pH titration shifts for all the nonlabile proton resonances a protein by two-dimensional NMR: the case of mouse epidermal growth factor.

D. Kohda, F. Inagaki, D Kohda, 1991, Biochemistry.

Complete sequence-specific 1H nuclear magnetic resonance assignments for mouse epidermal growth factor.

D. Kohda, F. Inagaki, 1988, Journal of Biochemistry (Tokyo).

Structural basis for the binding of the membrane‐proximal C‐terminal region of chemokine receptor CCR2 with the cytosolic regulator FROUNT

D. Kohda, K. Matsushima, I. Shimada, 2014, The FEBS journal.

Direct visualization of DNA baton pass between replication factors bound to PCNA

D. Kohda, Y. Ishino, K. Morikawa, 2018, Scientific Reports.

Distance Distribution between Two Iodine Atoms Derived from Small-Angle X-ray Scattering Interferometry for Analyzing a Conformational Ensemble of Heavy Atom-Labeled Small Molecules.

D. Kohda, T. Saio, Yuya Taguchi, 2020, The journal of physical chemistry letters.

Single-Pair SAXS for Analyzing a Conformational Ensemble of Heavy Atom-Labeled Small Molecules

D. Kohda, T. Saio, Yuya Taguchi, 2020 .

Structural basis for mRNA recognition by elongation factor SelB

Daisuke Kohda, D. Kohda, D. Fourmy, 2005, Nature Structural &Molecular Biology.

The lantibiotic nukacin ISK-1 exists in an equilibrium between active and inactive lipid-II binding states

D. Kohda, T. Zendo, K. Sonomoto, 2018, Communications Biology.

Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation

S. Matsumoto, A. Shimada, D. Kohda, 2013, Proceedings of the National Academy of Sciences.

Rational design of crystal contact‐free space in protein crystals for analyzing spatial distribution of motions within protein molecules

Y. Sugita, A. Shimada, D. Kohda, 2016, Protein science : a publication of the Protein Society.

Structural basis for dynamic interdomain movement and RNA recognition of the selenocysteine-specific elongation factor SelB.

D. Kohda, D. Fourmy, S. Yoshizawa, 2007, Structure.