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IKEGUCHI Masamichi

Profile Research field Education Activities Research achievement On-Campus Activities Off-Campus Activities

 

Books etc
No.Title URL, Autour Type, Publisher, Publication date, Range, ISBN 
1
Time-Resolved Small-Angle X-Ray Scattering of Protein Cage Assembly. , , , 2023, ,  

 

Published Papers
No.Title URL, Journal, Vol( Number), From Page- To Page, Publication date, DOI 
1
Time-Resolved Small-Angle X-Ray Scattering of Protein Cage Assembly. , Methods in molecular biology (Clifton, N.J.), 2671,  211- 218, 2023, https://doi.org/10.1007/978-1-0716-3222-2_12 
2
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 
3
In vitro assembly of Haemophilus influenzae adhesin transmembrane domain and studies on the electrostatic repulsion at the interface , Biophysical Reviews, 11,  303- 309, Jun. 1, 2019, https://doi.org/10.1007/s12551-019-00535-0 
4
Mechanisms of ferritin assembly studied by time-resolved small-angle X-ray scattering , Biophysical Reviews, 11,  449- 455, Jun. 1, 2019, https://doi.org/10.1007/s12551-019-00538-x 
5
Structure, Function, Folding, and Aggregation of a Neuroferritinopathy-Related Ferritin Variant , BIOCHEMISTRY, 58( 18), 2318- 2325, May. 7, 2019, https://doi.org/10.1021/acs.biochem.8b01068 
6
β-Strand twisting/bending in soluble and transmembrane β-barrel structures , Proteins: Structure, Function and Bioinformatics, 86,  1231- 1241, Dec. 1, 2018, https://doi.org/10.1002/prot.25576 
7
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 
8
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 
9
Residual structures in the unfolded state of starch-binding domain of glucoamylase revealed by near-UV circular dichroism and protein engineering techniques , BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1864( 10), 1464- 1472, Oct. 2016, https://doi.org/10.1016/j.bbapap.2016.05.002 
10
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 
11
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 
12
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 
13
The origin of beta-strand bending in globular proteins , BMC STRUCTURAL BIOLOGY, 15,   , Oct. 2015, https://doi.org/10.1186/s12900-015-0048-y 
14
Proliferation assay of mouse embryonic stem (ES) cells exposed to atmospheric-pressure plasmas at room temperature , JOURNAL OF PHYSICS D-APPLIED PHYSICS, 47( 44),  , Nov. 2014, https://doi.org/10.1088/0022-3727/47/44/445402 
15
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 
16
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 
17
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 
18
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 
19
Transient non-native helix formation during the folding of β-lactoglobulin , Biomolecules, 4( 1), 202- 216, Mar. 1, 2014, https://doi.org/10.3390/biom4010202 
20
α-helix formation rate of oligopeptides at subzero temperatures , Biophysics (Japan), 10,  9- 13, 2014, https://doi.org/10.2142/biophysics.10.9 
21
Dependence of alpha-helical and beta-sheet amino acid propensities on the overall protein fold type , BMC STRUCTURAL BIOLOGY, 12,   , Aug. 2012, https://doi.org/10.1186/1472-6807-12-18 
22
Importance of polypeptide chain length for the correct local folding of a beta-sheet protein , BIOPHYSICAL CHEMISTRY, 168,  40- 47, Jul. 2012, https://doi.org/10.1016/j.bpc.2012.06.002 
23
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 
24
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 
25
Structure and stability of Gyuba, a beta-lactoglobulin chimera , PROTEIN SCIENCE, 20( 11), 1867- 1875, Nov. 2011, https://doi.org/10.1002/pro.720 
26
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 
27
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 
28
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 
29
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 
30
Non-native alpha-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and beta-lactoglobulin (vol 76, pg 226, 2009) , PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 77( 4), 1015- 1015, Dec. 2009, https://doi.org/10.1002/prot.22593 
31
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 
32
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 
33
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 
34
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 
35
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 
36
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 
37
OLIGAMI: OLIGomer Architecture and Molecular Interface , The Open Bioinformatics Journal, 2( 1), 50- 53, Sep. 2008,  
38
Helix-rich transient and equilibrium intermediates of equine beta-lactoglobulin in alkaline buffer , BIOPHYSICAL CHEMISTRY, 134( 1-2), 84- 92, Apr. 2008, https://doi.org/10.1016/j.bpc.2008.01.010 
39
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 
40
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 
41
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 
42
Degradation of DNA into 5 '-monodeoxyribonucleotides in the presence of Mn2+ ions , BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, 71( 11), 2670- 2679, Nov. 2007, https://doi.org/10.1271/bbb.70260 
43
An alpha-helical burst in the src SH3 folding pathway , BIOCHEMISTRY, 46( 17), 5072- 5082, May. 2007, https://doi.org/10.1021/bi0618262 
44
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 
45
Chloride-ion concentration dependence of molecular dimension in the acid-denatured state of equine beta-lactoglobulin , JOURNAL OF APPLIED CRYSTALLOGRAPHY, 40,  S213- S216, Apr. 2007, https://doi.org/10.1107/S0021889807008278 
46
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 
47
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 
48
3P066 Molecular basis of beta-lactoglobulin dimerization(Proteins-stability, folding, and other physicochemical properties,Poster Presentations) , Seibutsu Butsuri, 47,  S219- , 2007, https://doi.org/10.2142/biophys.47.S219_3 
49
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 
50
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 
51
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 
52
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 
53
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 
54
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 
55
1P086 Structural stability of human tear lipocalin mutants , Seibutsu Butsuri, 45,  S53- , 2005, https://doi.org/10.2142/biophys.45.S53_2 
56
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 
57
Thermal stabilization of penicillolysin, a thermolabile 19 kDa Zn2+-protease, obtained by site-directed mutagenesis , PROTEIN ENGINEERING DESIGN & SELECTION, 17( 3), 261- 266, Mar. 2004, https://doi.org/10.1093/protein/gzh034 
58
Substrate specificities of deuterolysin from aspergillus oryzae and electron paramagnetic resonance measurement of cobalt-substituted deuterolysin , Bioscience, Biotechnology and Biochemistry, 67( 2), 264- 270, Jan. 1, 2003, https://doi.org/10.1271/bbb.67.264 
59
Construction and characterization of beta-lactoglobulin chimeras , PROTEINS-STRUCTURE FUNCTION AND GENETICS, 49( 3), 297- 301, Nov. 2002, https://doi.org/10.1002/prot.10223 
60
1I1000 Cold denaturation of equine beta-lactoglobulin , Seibutsu Butsuri, 42( 2), S47- , 2002, https://doi.org/10.2142/biophys.42.S47_3 
61
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 
62
The correlation between amino acide sequence and cooperativity of helix formation in trifluoroethanol , Seibutsu Butsuri, 41,  S170- , 2001, https://doi.org/10.2142/biophys.41.S170_3 
63
A partially unfolded state of equine β-lactoglobulin at pH 8.7 , Journal of Protein Chemistry, 20( 2), 131- 137, 2001, https://doi.org/10.1023/A:1011029524100 
64
Molten globule structure of equine beta-lactoglobulin probed by hydrogen exchange , JOURNAL OF MOLECULAR BIOLOGY, 299( 3), 757- 770, Jun. 2000, https://doi.org/10.1006/jmbi.2000.3761 
65
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 
66
Molecular and enzymic properties of recombinant 1,2-alpha-mannosidase from Aspergillus saitoi overexpressed in Aspergillus oryzae cells , BIOCHEMICAL JOURNAL, 339,  589- 597, May. 1999, https://doi.org/10.1042/0264-6021:3390589 
67
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 
68
Disulfide-coupled folding and unfolding of equine β -lactogloblin , Seibutsu Butsuri, 39,  S160- , 1999, https://doi.org/10.2142/biophys.39.S160_2 
69
Phase diagram of equine β-lactoglobulin conformation , Seibutsu Butsuri, 39,  S160- , 1999, https://doi.org/10.2142/biophys.39.S160_3 
70
Characteristic properties of equine milk proteins , International Journal of Food Science and Technology, 34( 5-6), 437- 443, 1999, https://doi.org/10.1046/j.1365-2621.1999.00328.x 
71
Remarkable destabilization of recombinant alpha-lactalbumin by an extraneous N-terminal methionyl residue , PROTEIN ENGINEERING, 11( 5), 333- 335, May. 1998,  
72
The region of α-lactalbumin recognized by GroEL , Journal of Biochemistry, 124( 2), 319- 325, 1998, https://doi.org/10.1093/oxfordjournals.jbchem.a022114 
73
Conformational studies of peptides spanning the helical sequence in the molten globule alpha-lactalbumin , PEPTIDES, ,  94- 95, 1998,  
74
Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond , Protein Science, 7( 7), 1564- 1574, 1998, https://doi.org/10.1002/pro.5560070710 
75
Molten globule state of equine β-lactoglobulin , Proteins: Structure, Function and Genetics, 27( 4), 567- 575, 1997, https://doi.org/10.1002/(SICI)1097-0134(199704)27:4<567::AID-PROT9>3.0.CO;2-7 
76
Studies of Disulfide Bond Reduction of Pigeon and Japanese Quail Lysozymes. , Reports on Progress in Polymer Physics in Japan, 40,  617- 618, 1997,  
77
Molten globule state of equine β-lactoglobulin , Proteins: Structure, Function and Genetics, 27( 4), 567- 575, 1997, https://doi.org/10.1002/(SICI)1097-0134(199704)27:4<567::AID-PROT9>3.0.CO;2-7 
78
A synthetic peptide study on the molten globule of α-lactalbumin , Journal of Biochemistry, 119( 5), 947- 952, 1996, https://doi.org/10.1093/oxfordjournals.jbchem.a021334 
79
Interation of GroEL and α-lactalbumin Molten Globule , Reports on Progress in Polymer Physics in Japan, 39,  625- 628, 1996,  
80
The superreactive disulfide bonds in alpha-lactalbumin and lysozyme , JOURNAL OF PROTEIN CHEMISTRY, 14( 8), 731- 737, Nov. 1995, https://doi.org/10.1007/BF01886912 
81
Structure of GL-1a, A Major Neutral Glycolipid, from Sulfolobus acidocaldarius N-8 , J. Jpn. Oil Chem. Soc. (YUKAGAKU), 44( 12), 1099- 1102, 1995, https://doi.org/10.5650/jos1956.44.1099 
82
APPROPRIATENESS OF DSS AND TSP AS INTERNAL REFERENCES FOR H-1-NMR STUDIES OF MOLTEN GLOBULE PROTEINS IN AQUEOUS-MEDIA , JOURNAL OF BIOMOLECULAR NMR, 4( 6), 859- 862, Nov. 1994, https://doi.org/10.1007/BF00398414 
83
CONFORMATIONAL COMPARISON BETWEEN ALPHA-LACTALBUMIN AND LYSOZYME , ADVANCES IN BIOPHYSICS, VOL 30, 1994, 30,  37- 84, 1994, https://doi.org/10.1016/0065-227X(94)90010-8 
84
ESSENTIAL ROLE OF THE ARG112 RESIDUE OF CYTOCHROME-P450CAM FOR ELECTRON-TRANSFER FROM REDUCED PUTIDAREDOXIN , FEBS LETTERS, 331( 1-2), 109- 113, Sep. 1993, https://doi.org/10.1016/0014-5793(93)80307-G 
85
Unfolding of the Molten Globule State of α-Lactalbumin Studied by 1H NMR , Biochemistry, 32( 48), 13198- 13203, 1993, https://doi.org/10.1021/bi00211a031 
86
Contribution of the 6-120 Disulfide Bond of β-Lactalbumin to the Stabilities of its Native and Molten Globule States , Biochemistry, 31( 50), 12695- 12700, Feb. 1, 1992, https://doi.org/10.1021/bi00165a021 
87
Conformational Study of Lactoferricin in Aqueous Solutions , Reports on Progress in Polymer Physics in Japan, 35,  665- 666, 1992,  
88
Two-Dimensional 1H-NMR Studies on -Lactalbumin in the Native and Molten Globule States , Reports on Progress in Polymer Physics in Japan, 35,  663- 664, 1992,  
89
KINETICS OF DISULFIDE BOND REDUCTION IN ALPHA-LACTALBUMIN BY DITHIOTHREITOL AND MOLECULAR-BASIS OF SUPERREACTIVITY OF THE CYS6-CYS120 DISULFIDE BOND , BIOCHEMISTRY, 29( 36), 8240- 8249, Sep. 1990, https://doi.org/10.1021/bi00488a007 
90
Contribution of disulfide bonds to stability of the folding intermediate of α‐lactalbumin , International Journal of Peptide and Protein Research, 33( 4), 289- 297, 1989, https://doi.org/10.1111/j.1399-3011.1989.tb01284.x 
91
INNOCUOUS CHARACTER OF [ETHYLENEBIS(OXYETHYLENENITRILO)]TETRAACETIC ACID AND EDTA AS METAL-ION BUFFERS IN STUDYING CA-2+ BINDING BY ALPHA-LACTALBUMIN , JOURNAL OF BIOLOGICAL CHEMISTRY, 261( 19), 8824- 8829, Jul. 1986,  
92
Evidence for Identity between the Equilibrium Unfolding Intermediate and a Transient Folding Intermediate: A Comparative Study of the Folding Reactions of α-Lactalbumin and Lysozyme , Biochemistry, 25( 22), 6965- 6972, 1986, https://doi.org/10.1021/bi00370a034 
93
Ca2+ alteration in the unfolding behavior of α-lactalbumin , Journal of Biochemistry, 99( 4), 1191- 1201, 1986, https://doi.org/10.1093/oxfordjournals.jbchem.a135582 
94
COMPARISON OF THE TRANSIENT FOLDING INTERMEDIATES IN LYSOZYME AND ALPHA-LACTALBUMIN , BIOCHEMISTRY, 24( 4), 874- 881, 1985, https://doi.org/10.1021/bi00325a010 

 

MISC
No.Title URL, Journal, Vol( Number), From Page- To Page, Publication date 
1
Role of a non-native alpha-helix in the folding of equine beta-lactoglobulin , PROTEIN SCIENCE, 24,  94- 94, Oct. 2015 
2
Role of electrostatic repulsion between unique arginine residues on the assembly of a trimeric autotransporter translocator domain , PROTEIN SCIENCE, 24,  89- 90, Oct. 2015 
3
Repulsion between net charges of subunits during ferritin assembly , PROTEIN SCIENCE, 24,  87- 88, Oct. 2015 
4
Self-catalyzing functions of DNA. , Nucleic acids symposium series (2004), ,  517- 518, Dec. 1, 2008 
5
Study on the mechanism of stabilization of the molten globule state of α-lactalbumin by using the peptide frangents , Biophysics, 38( 2), S178- , Sep. 7, 1998 
6
Temperature and pH dependence of the molten globule structure of equine β-lactoglobulin , Biophysics, 38( 2), S160- , Sep. 7, 1998 
7
Pressure effect on the molten globule state of cytochrome c , Biophysics, 37,  S25- , Oct. 1997 
8
Preparation and NMR Analysis of Recombinant Equine beta-Lactoglobulin , Biophysics, 37,  S23- , Oct. 1997 
9
Folding intermediate of beta-lactoglobulin , Biophysics, 37,  S24- , Oct. 1997 
10
Structure of the two disulfide folding intermediate of bovine alpha-lactalbumin , PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY, 65,  PA431- PA431, 1996 

 

Conference Activities & Talks
No.Title, Conference, Publication date, Promoter, Venue 
1
Helix nucleation facilitated by the closed loop structure, , Nov. 26, 2021, ,  
2
Time-resolved small-angle X-ray scattering for monitoring the biomolecular assembly process, 10th International Conference on Biomolecular Engineering, Jan. 9, 2020, ,  

 

Research Grants & Projects
No.Offer organization, System name, Title, Fund classification, Date 
1
Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C), Molecular evolution of ferritin: Role of electric charges on iron storage function, ,  Apr. 2021 - Mar. 2024 
2
Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Young Scientists (B), Structure-activity relationship of carcinogenic factor, Tip-alpha, from Helicobacter pylori, ,  Apr. 2014 - Mar. 2016