Publications
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Kuwata T, Sato D, Yanagida Y, Aoki E, Fujiwara K, Yoshimura H, Ikeguchi M.
Morphological difference of Escherichia coli non-heme ferritin iron cores reconstituted in the presence and absence of inorganic phosphate.
J Biol Inorg Chem. 2022 Sep;27(6):583-594. -
Aoki E, Ikeguchi M.
In vitro assembly of Haemophilus influenzae adhesin transmembrane domain and studies on the electrostatic repulsion at the interface.
Biophys Rev. 2019 Jun;11(3):303-309. -
Sato D, Ikeguchi M.
Mechanisms of ferritin assembly studied by time-resolved small-angle X-ray scattering.
Biophys Rev. 2019 Jun;11(3):449-455. -
Kuwata T, Okada Y, Yamamoto T, Sato D, Fujiwara K, Fukumura T, Ikeguchi M.
Structure, Function, Folding, and Aggregation of a Neuroferritinopathy-Related Ferritin Variant.
Biochemistry. 2019 May 7;58(18):2318-2325. -
Kikuchi N, Fujiwara K, Ikeguchi M.
β-strand twisting/bending in soluble and transmembrane β-barrel structures.
Proteins. 2018 Dec;86(12):1231-1241. -
Aoki E, Fujiwara K, Shimizu A, Takase-Yoden S, Ikeguchi M.
Optimization of Haemophilus influenzae adhesin transmembrane domain expression in Escherichia coli.
Protein Expr Purif. 2018 May;145:19-24. -
Aoki E, Sato D, Fujiwara K, Ikeguchi M.
Electrostatic Repulsion between Unique Arginine Residues Is Essential for the Efficient in Vitro Assembly of the Transmembrane Domain of a Trimeric Autotransporter.
Biochemistry. 2017 Apr 18;56(15):2139-2148. -
Sato D, Takebe S, Kurobe A, Ohtomo H, Fujiwara K, Ikeguchi M.
Electrostatic Repulsion during Ferritin Assembly and Its Screening by Ions.
Biochemistry. 2016 Jan 26;55(3):482-8. -
Sato D, Ohtomo H, Yamada Y, Hikima T, Kurobe A, Fujiwara K, Ikeguchi M.
Ferritin Assembly Revisited: A Time-Resolved Small-Angle X-ray Scattering Study.
Biochemistry. 2016 Jan 19;55(2):287-93. -
Fujiwara K, Ebisawa S, Watanabe Y, Fujiwara H, Ikeguchi M.
The origin of β-strand bending in globular proteins.
BMC Struct Biol. 2015 Oct 22;15:21. -
Ohtomo H, Ohtomo M, Sato D, Kurobe A, Sunato A, Matsumura Y, Kihara H, Fujiwara K, Ikeguchi M.
A Physicochemical and Mutational Analysis of Intersubunit Interactions of Escherichia coli Ferritin A.
Biochemistry. 2015 Oct 13;54(40):6243-51. -
Okabe T, Miyajima T, Nakagawa K, Tsukamoto S, Fujiwara K, Ikeguchi M.
Effect of non-native helix destabilization on the folding of equine β-lactoglobulin.
J Biochem. 2014 Nov;156(5):291-7. -
Okabe T, Tsukamoto S, Fujiwara K, Shibayama N, Ikeguchi M.
Delineation of solution burst-phase protein folding events by encapsulating the proteins in silica gels.
Biochemistry. 2014 Jun 17;53(23):3858-66. -
Fujiwara K, Ebisawa S, Watanabe Y, Toda H, Ikeguchi M.
Local sequence of protein β-strands influences twist and bend angles.
Proteins. 2014 Jul;82(7):1484-93. -
Ikeguchi M.
Transient non-native helix formation during the folding of β-lactoglobulin.
Biomolecules. 2014 Feb 13;4(1):202-16. -
Nakagawa K, Yamada Y, Matsumura Y, Tsukamoto S, Yamamoto-Ohtomo M, Ohtomo H, Okabe T, Fujiwara K, and Ikeguchi M.
Relationship between chain collapse and secondary structure formation in a partially folded protein.
Biopolymers. 2014 Jun;101(6):651-8.
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Fujiwara K, Toda H, Ikeguchi M.
Dependence of alpha-helical and beta-sheet amino acid propensities on the overall protein fold type.
BMC Struct Biol. 2012 Aug 2;12:18. -
Yamamoto M, Nakagawa K, Ikeguchi M.
Importance of polypeptide chain length for the correct local folding of a β-sheet protein.
Biophys Chem. 2012 Jul;168-169:40-7. -
Ohtomo H, Fujiwara K, Ikeguchi M.
Important Role of Methionine 145 in Dimerization of Bovine β-Lactoglobulin.
J Biochem. 2012 Mar;151(3):329-34. -
Yamamoto M, Nakagawa K, Fujiwara K, Shimizu A, Ikeguchi M, Ikeguchi M.
A native disulfide stabilizes non-native helical structures in partially folded states of equine β-lactoglobulin.
Biochemistry. 2011 Dec 13;50(49):10590-7. -
Ohtomo H, Konuma T, Utsunoiya H, Tsuge H, Ikeguchi M.
Structure and stability of Gyuba, a β-lactoglobulin chimera.
Protein Sci. 2011 Nov;20(11):1867-75. -
Tsukamoto S, Fujiwara K, Ikeguchi M.
Fatty acids bound to recombinant tear lipocalin and their role in structural stabilization.
J Biochem. 2009 Sep;146(3):343-50. -
Tsukamoto S, Yamashita T, Yamada Y, Fujiwara K, Maki K, Kuwajima K, Matsumura Y, Kihara H, Tsuge H, Ikeguchi M.
Non-native alpha-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and beta-lactoglobulin.
Proteins. 2009 Jul;76(1):226-36. -
Fujiwara K, Ikeguchi M.
OLIGAMI: OLIGomer Architecture and Molecular Interface.
The Open Bioinformatics Journal, 2008, 2, 50-53. -
Nakagawa K, Yamada Y, Fujiwara K, Ikeguchi M.
Interactions Responsible for Secondary Structure Formation during Folding of Equine beta-Lactoglobulin.
J Mol Biol. 2007 April 6;367(4):1205-1214. -
Nakagawa K, Tokushima A, Fujiwara K, Ikeguchi M.
Proline Scanning Mutagenesis Reveals Non-Native Fold in the Molten Globule State of Equine beta-Lactoglobulin.
Biochemistry. 2006 Dec 26;45(51):15468-15473. -
Yamada Y, Nakagawa K, Yajima T, Saito K, Tokushima A, Fujiwara K, Ikeguchi M.
Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine beta-lactoglobulin.
Proteins. 2006 May 15;63(3):595-602. -
Yamada Y, Yajima T, Fujiwara K, Arai M, Ito K, Shimizu A, Kihara H, Kuwajima K, Amemiya Y, Ikeguchi M.
Helical and Expanded Conformation of Equine beta-Lactoglobulin in the Cold-denatured State.
J Mol Biol. 2005 Jul 8;350(2):338-48. -
Kobayashi T, Ikeguchi M, Sugai S.
Construction and characterization of beta-lactoglobulin chimeras.
Proteins. 2002 Nov 15;49(3):297-301. -
Fujiwara K, Ikeguchi M, Sugai S.
A partially unfolded state of equine beta-lactoglobulin at pH 8.7.
J Protein Chem. 2001 Feb;20(2):131-7. -
Kobayashi T, Ikeguchi M, Sugai S.
Molten globule structure of equine beta-lactoglobulin probed by hydrogen exchange.
J Mol Biol. 2000 Jun 9;299(3):757-70. -
Maeda H, Suzuki S, Ikeguchi M, Sakai T, Shibata K.
Enzymatic synthesis of L-[4-13C]aspartic acid.
J Biosci Bioeng. 2000;89(4):392-5. -
Fujiwara K, Arai M, Shimizu A, Ikeguchi M, Kuwajima K, Sugai S.
Folding-unfolding equilibrium and kinetics of equine beta-lactoglobulin: equivalence between the equilibrium molten globule state and a burst-phase folding intermediate.
Biochemistry. 1999 Apr 6;38(14):4455-63. -
Ikeguchi M, Fujino M, Kato M, Kuwajima K, Sugai S.
Transition state in the folding of alpha-lactalbumin probed by the 6-120 disulfide bond.
Protein Sci. 1998 Jul;7(7):1564-74. -
Ishikawa N, Chiba T, Chen LT, Shimizu A, Ikeguchi M, Sugai S.
Remarkable destabilization of recombinant alpha-lactalbumin by an extraneous N-terminal methionyl residue.
Protein Eng. 1998 May;11(5):333-5. -
Ikeguchi M, Kato S, Shimizu A, Sugai S.
Molten globule state of equine beta-lactoglobulin.
Proteins. 1997 Apr;27(4):567-75.