Morphological difference of Escherichia coli non-heme ferritin iron cores reconstituted in the presence and absence of inorganic phosphate , Journal of Biological Inorganic Chemistry, 27( 6), 583- 594, Sep. 2022, https://doi.org/10.1007/s00775-022-01952-5 

Structure, Function, Folding, and Aggregation of a Neuroferritinopathy-Related Ferritin Variant. , Biochemistry, 58( 18), 2318- 2325, May. 2019, https://doi.org/10.1021/acs.biochem.8b01068 

β-strand twisting/bending in soluble and transmembrane β-barrel structures. , Proteins, ,   , Jul. 2018, https://doi.org/10.1002/prot.25576 

Optimization of Haemophilus influenzae adhesin transmembrane domain expression in Escherichia coli , Protein Expression and Purification, 145,  19- 24, May. 1, 2018, https://doi.org/10.1016/j.pep.2017.12.009 

Electrostatic Repulsion between Unique Arginine Residues Is Essential for the Efficient in Vitro Assembly of the Transmembrane Domain of a Trimeric Autotransporter , BIOCHEMISTRY, 56( 15), 2139- 2148, Apr. 2017, https://doi.org/10.1021/acs.biochem.6b01130 

Electrostatic Repulsion during Ferritin Assembly and Its Screening by Ions , BIOCHEMISTRY, 55( 3), 482- 488, Jan. 2016, https://doi.org/10.1021/acs.biochem.5b01197 

Ferritin Assembly Revisited: A Time-Resolved Small-Angle X-ray Scattering Study , BIOCHEMISTRY, 55( 2), 287- 293, Jan. 2016, https://doi.org/10.1021/acs.biochem.5b01152 

The origin of beta-strand bending in globular proteins , BMC STRUCTURAL BIOLOGY, 15,  21- , Oct. 2015, https://doi.org/10.1186/s12900-015-0048-y 

Role of a non-native alpha-helix in the folding of equine beta-lactoglobulin , PROTEIN SCIENCE, 24,  94- 94, Oct. 2015,  

Role of electrostatic repulsion between unique arginine residues on the assembly of a trimeric autotransporter translocator domain , PROTEIN SCIENCE, 24,  89- 90, Oct. 2015,  

Repulsion between net charges of subunits during ferritin assembly , PROTEIN SCIENCE, 24,  87- 88, Oct. 2015,  

A Physicochemical and Mutational Analysis of Intersubunit Interactions of Escherichia coli Ferritin A , BIOCHEMISTRY, 54( 40), 6243- 6251, Oct. 2015, https://doi.org/10.1021/acs.biochem.5b00723 

Effect of non-native helix destabilization on the folding of equine beta-lactoglobulin , JOURNAL OF BIOCHEMISTRY, 156( 5), 291- 297, Nov. 2014, https://doi.org/10.1093/jb/mvu043 

Local sequence of protein beta-strands influences twist and bend angles , PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 82( 7), 1484- 1493, Jul. 2014, https://doi.org/10.1002/prot.24518 

Delineation of Solution Burst-Phase Protein Folding Events by Encapsulating the Proteins in Silica Gels , BIOCHEMISTRY, 53( 23), 3858- 3866, Jun. 2014, https://doi.org/10.1021/bi5003647 

Relationship Between Chain Collapse and Secondary Structure Formation in a Partially Folded Protein , BIOPOLYMERS, 101( 6), 651- 658, Jun. 2014, https://doi.org/10.1002/bip.22433 

3P050 Construction of ferritin hetero-oligomer(01C. Protein: Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) , Seibutsu Butsuri, 54( 1), S257- , 2014, https://doi.org/10.2142/biophys.54.S257_2 

1P065 Local sequence of protein β-strands influences twist and bend angles(01C. Protein : Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) , Seibutsu Butsuri, 54( 1), S151- , 2014, https://doi.org/10.2142/biophys.54.S151_5 

1P063 A study of ferritin assembly mechanism(01C. Protein : Property,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) , Seibutsu Butsuri, 54( 1), S151- , 2014, https://doi.org/10.2142/biophys.54.S151_3 

1P114 Role of a unique arginine residue on the assembly of the translocator domain in a trimeric autotransporter(03. Membrane proteins,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) , Seibutsu Butsuri, 54( 1), S159- , 2014, https://doi.org/10.2142/biophys.54.S159_6 

3P089 Construction and characterization of ferritin mutants having different net charges(01F. Protein: Engineering,Poster) , Seibutsu Butsuri, 53( 1), S226- , 2013, https://doi.org/10.2142/biophys.53.S226_5 

3P062 Effect of non-native α-helix in the early intermediate on folding kinetics of equine β-lactoglobulin(01C. Protein: Property,Poster) , Seibutsu Butsuri, 53( 1), S222- , 2013, https://doi.org/10.2142/biophys.53.S222_2 

Dependence of alpha-helical and beta-sheet amino acid propensities on the overall protein fold type , BMC STRUCTURAL BIOLOGY, 12,  18- , Aug. 2012, https://doi.org/10.1186/1472-6807-12-18 

Important role of methionine 145 in dimerization of bovine beta-lactoglobulin , JOURNAL OF BIOCHEMISTRY, 151( 3), 329- 334, Mar. 2012, https://doi.org/10.1093/jb/mvr142 

A Native Disulfide Stabilizes Non-Native Helical Structures in Partially Folded States of Equine beta-Lactoglobulin , BIOCHEMISTRY, 50( 49), 10590- 10597, Dec. 2011, https://doi.org/10.1021/bi2013239 

3P059 Structural analysis of a peptide fragment of equine, β-lactoglobulin using CD and NMR spectroscopies(Protein: Property,The 48th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 50( 2), S155- , 2010, https://doi.org/10.2142/biophys.50.S155_2 

2P072 Ultracentrifuge analysis of folding intermediate analogues of &beta-lactoglobulin(The 48th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 50( 2), S94- , 2010, https://doi.org/10.2142/biophys.50.S94_5 

2P027 Requirement for dimer-formation of retinol binding protein-like family(The 48th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 50( 2), S86- , 2010, https://doi.org/10.2142/biophys.50.S86_4 

3P027 Fold dependency of the amino acid occurrence in the β-strand(Protein: Structure,The 48th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 50( 2), S149- , 2010, https://doi.org/10.2142/biophys.50.S149_5 

Correction to the article "non-native α-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and β-lactoglobulin" (Proteins: Structute, Function and Bioformatics (2009) 76, (226-236)) , Proteins: Structure, Function and Bioinformatics, 77,  1015- , Nov. 25, 2009, https://doi.org/10.1002/prot.22593 

Fatty Acids Bound to Recombinant Tear Lipocalin and Their Role in Structural Stabilization , JOURNAL OF BIOCHEMISTRY, 146( 3), 343- 350, Sep. 2009, https://doi.org/10.1093/jb/mvp076 

Non-native alpha-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and beta-lactoglobulin , PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 76( 1), 226- 236, Jul. 2009, https://doi.org/10.1002/prot.22340 

2P-043 A stopped-flow anaiysis of beta-lactoglobulin folding(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 49,  S113- , 2009, https://doi.org/10.2142/biophys.49.S113_3 

2P-044 Key residues for β-lactoglobulin dimerization(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 49,  S113- , 2009, https://doi.org/10.2142/biophys.49.S113_4 

2P-046 CONFORMATIONAL FLUCTUATION OF β-LACTOGLOBULIN MONITORED BY HYDROGEN EXCHANGE(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 49,  S113- S114, 2009, https://doi.org/10.2142/biophys.49.S113_6 

2P-045 Structural analysis of equine β-lactoglobulin folding core using heteronuclear NMR(Protein:Property,The 47th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 49,  S113- , 2009, https://doi.org/10.2142/biophys.49.S113_5 

OLIGAMI: OLIGomer Architecture and Molecular Interface , The Open Bioinformatics Journal, 2( 1), 50- 53, Sep. 2008,  

2P-013 Fold dependency of the amino acid occurrence in the beta-strand(The 46th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 48,  S77- , 2008, https://doi.org/10.2142/biophys.48.S77_1 

3P-028 Analysis of near-UV circular dichroism spectrum by the aromatic residue substitution(The 46th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 48,  S132- , 2008, https://doi.org/10.2142/biophys.48.S132_1 

2P-085 Peptide analyses of equine beta-lactoglobulin folding core(The 46th Annual Meeting of the Biophysical Society of Japan) , Seibutsu Butsuri, 48,  S88- , 2008, https://doi.org/10.2142/biophys.48.S88_3 

Chloride-ion concentration dependence of molecular dimension in the acid-denatured state of equine β-lactoglobulin , Journal of Applied Crystallography, 40,   , Apr. 1, 2007, https://doi.org/10.1107/S0021889807008278 

Interactions responsible for secondary structure formation during folding of equine beta-lactoglobulin , JOURNAL OF MOLECULAR BIOLOGY, 367( 4), 1205- 1214, Apr. 2007, https://doi.org/10.1016/j.jmb.2007.01.053 

1P258 Database of biological molecules(OLIGAMI)(Bioinformatics-structural genomics,Poster Presentations) , Seibutsu Butsuri, 47,  S88- , 2007, https://doi.org/10.2142/biophys.47.S88_1 

2P088 Contribution of each tyrosine residue to the near-UV circular dichroism spectrum of equine β-lactoglobulin(Proteins-stability, folding, and other physicochemical properties,Poster Presentations) , Seibutsu Butsuri, 47,  S135- , 2007, https://doi.org/10.2142/biophys.47.S135_1 

3P065 Dimer formation of a disulfide-less mutant of equine β-lactoglobulin(Proteins-stability, folding, and other physicochemical properties,Poster Presentations) , Seibutsu Butsuri, 47,  S219- , 2007, https://doi.org/10.2142/biophys.47.S219_2 

Proline scanning mutagenesis reveals non-native fold in the molten globule state of equine beta-lactoglobulin , BIOCHEMISTRY, 45( 51), 15468- 15473, Dec. 2006, https://doi.org/10.1021/bi061420p 

Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine beta-lactoglobulin , PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 63( 3), 595- 602, May. 2006, https://doi.org/10.1002/prot.20905 

1P128 Role of an off-barrel strand for the structural stabilization of equine β-lactoglobulin(3. Protein folding and misfolding (1),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) , Seibutsu Butsuri, 46( 2), S178- , 2006, https://doi.org/10.2142/biophys.46.S178_4 

1P102 Comparison of burst phase folding intermediates of tear lipocalin and β-lactoglobulin(3. Protein folding and misfolding (I),Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) , Seibutsu Butsuri, 46( 2), S172- , 2006, https://doi.org/10.2142/biophys.46.S172_2 

Helical and expanded conformation of equine beta-lactoglobulin in the cold-denatured state , JOURNAL OF MOLECULAR BIOLOGY, 350( 2), 338- 348, Jul. 2005, https://doi.org/10.1016/j.jmb.2005.05.003 

3P054 Mechanism stabilizing non-native alpha-helical structure in partially folded states of equine beta-lactoglobulin , Seibutsu Butsuri, 45,  S217- , 2005, https://doi.org/10.2142/biophys.45.S217_2 

1P086 Structural stability of human tear lipocalin mutants , Seibutsu Butsuri, 45,  S53- , 2005, https://doi.org/10.2142/biophys.45.S53_2 

1I1000 Cold denaturation of equine beta-lactoglobulin , Seibutsu Butsuri, 42( 2), S47- , 2002, https://doi.org/10.2142/biophys.42.S47_3 

A partially unfolded state of equine β-lactoglobulin at pH 8.7 , Protein Journal, 20,  131- 137, Dec. 1, 2001, https://doi.org/10.1023/A:1011029524100 

The intermediate state of equine b-lactoglobulin in urea form a dimer at alkali pH , Seibutsu Butsuri, 40,  S12- , 2000, https://doi.org/10.2142/biophys.40.S12_1 

Folding-unfolding equilibrium and kinetics of equine beta-lactoglobulin: Equivalence between the equilibrium molten globule state and a burst-phase folding intermediate , BIOCHEMISTRY, 38( 14), 4455- 4463, Apr. 1999, https://doi.org/10.1021/bi982683p 

Phase diagram of equine β-lactoglobulin conformation , Seibutsu Butsuri, 39,  S160- , 1999, https://doi.org/10.2142/biophys.39.S160_3 

Temperature and pH dependence of the molten globule structure of equine β-lactoglobulin , Biophysics, 38( 2), S160- , Sep. 7, 1998 

Folding intermediate of beta-lactoglobulin , Biophysics, 37,  S24- , Oct. 1997