Yagi H, Mizuno A, So M, Hirano M, Adachi M, Akazawa-Ogawa Y, Hagihara Y, Ikenoue T, Lee YH, Kawata Y, Goto Y.
Ultrasonication-dependent formation and degradation of α-synuclein amyloid fibrils.
Biochim. Biophys. Acta. 1854, 209-17 (2014) [PMID:25528988]

Terakawa MS, Yagi H, Adachi M, Lee YH, Goto Y.
Small Liposomes Accelerate the Fibrillation of Amyloid β (1-40).
J Biol Chem. 290, 815-826 (2014) [PMID:25406316]

Ogi H, Fukukshima M, Hamada H, Noi K, Hirao M, Yagi H, Goto Y.
Ultrafast propagation of β-amyloid fibrils in oligomeric cloud.
Sci Rep. 4, 6960 (2014) [PMID:25376301]

Yagi H, Abe Y, Takayanagi N, Goto Y.
Elongation of amyloid fibrils through lateral binding of monomers revealed by total internal reflection fluorescence microscopy.
Biochim. Biophys. Acta. 1844, 1881-8 (2014) [PMID:25125372]

Umemoto A, Yagi H, So M, Goto Y.
High-throughput analysis of the ultrasonication-forced amyloid fibrillation reveals the mechanism underlying the large fluctuation in the lag time.
J Biol Chem. 289, 27290-9 (2014) [PMID:25118286]

Nokwe CN, Zacharias M, Yagi H, Hora M, Reif B, Goto Y, Buchner J.
A Residue-specific Shift in Stability and Amyloidogenicity of Antibody Variable Domains.
J Biol Chem. 289, 26829-46 (2014) [PMID:25096580]

Chen J, Yagi H, Furutani Y, Nakamura T, Inaguma A, Guo H, Kong Y, Goto Y.
Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergent.
Sci Rep. 4, 5614 (2014) [PMID:25000956]

Ikenoue T, Lee YH, Kardos J, Saiki M, Yagi H, Kawata Y, Goto Y.
Cold Denaturation of Alpha-Synuclein Amyloid Fibrils.
Angew Chem Int Ed Engl. 53, 7799-804 (2014) [PMID:24920162]

Mizushima R, Kim JY, Suetake I, Tanaka H, Takai T, Kamiya N, Takano Y, Mishima Y, Tajima S, Goto Y, Fukui K, Lee YH.
NMR Characterization of the Interaction of the Endonuclease Domain of MutL with Divalent Metal Ions and ATP.
PLoS One. 9, e98554 (2014) [PMID:24901533]

Muta H, Lee YH, Kardos J, Lin Y, Yagi H, Goto Y.
Supersaturation-limited amyloid fibrillation of insulin revealed by ultrasonication.
J Biol Chem. 289, 18228-38 (2014) [PMID:24847058]

Ikenoue T, Lee YH, Kardos J, Yagi H, Ikegami T, Naiki H, Goto Y.
Heat of supersaturation-limited amyloid burst directly monitored by isothermal titration calorimetry.
Proc Natl Acad Sci U S A. 111, 6654-9 (2014) [PMID:24753579]

高齢化社会の深刻な病気の治療・予防の進展に期待

Akazawa-Ogawa Y, Takashima M, Lee YH, Ikegami T, Goto Y, Uegaki K, Hagihara Y.
Heat-Induced Irreversible Denaturation of the Camelid Single Domain VHH Antibody is Governed by Chemical Modifications.
J Biol Chem. 289, 15666-79 (2014) [PMID:24739391]

Lin Y, Lee YH, Yoshimura Y, Yagi H, Goto Y.
Solubility and supersaturation-dependent protein misfolding revealed by ultrasonication.
Langmuir. 30, 1845-54 (2014) [PMID:24059752]

Kume S, Lee YH, Nakatsuji M, Teraoka Y, Yamaguchi K, Goto Y, Inui T.
Fine-tuned broad binding capability of human lipocalin-type prostaglandin D synthase for various small lipophilic ligands.
FEBS Lett. 588, 962-9 (2014) [PMID:24530534]

Okazaki H, Ohori Y, Komoto M, Lee YH, Goto Y, Tochio N, Nishimura C.
Remaining structures at the N- and C-terminal regions of alpha-synuclein accurately elucidated by amide-proton exchange NMR with fitting..
FEBS Lett. 587, 3709-14 (2013) [PMID:24113654]

Kitayama H, Yoshimura Y, So M, Sakurai K, Yagi H, Goto Y.
A common mechanism underlying amyloid fibrillation and protein crystallization revealed by the effects of ultrasonication.
Biochim. Biophys. Acta. 1834, 2640-6 (2013) [PMID:24096102]

Yagi H, Hasegawa K, Yoshimura Y, Goto Y.
Acceleration of the depolymerization of amyloid β fibrils by ultrasonication.
Biochim. Biophys. Acta. 1834, 2480-2485 (2013) [PMID:24041501]

Mangione PP, Esposito G, Relini A, Raimondi S, Porcari R, Giorgetti S, Corazza A, Fogolari F, Penco A, Goto Y, Lee YH, Yagi H, Cecconi C, Naqvi MM, Gillmore JD, Hawkins PN, Chiti F, Rolandi R, Taylor GW, Pepys MB, Stoppini M, Bellotti V.
Structure, folding dynamics and amyloidogenesis of Asp76Asn β2-microglobulin: roles of shear flow, hydrophobic surfaces and α crystallin.
J. Biol. Chem. 288, 30917-30 (2013) [PMID:24014031]

Kato Y, Yagi H, Kaji Y, Oshika T, Goto Y.
Benzalkonium chloride accelerates the formation of the amyloid fibrils of corneal dystrophy-associated peptides.
J. Biol. Chem. 288, 25109-18 (2013) [PMID:23861389]

Yuichi Yoshimura, Masatomo So, Hisashi Yagi, Yuji Goto
Ultrasonication, an efficient agitation for accelerating the supersaturation-limited amyloid fibrillation of proteins
Japanese Journal of Applied Physics 52, 07HA01-1 (2013) [DOI:10.7567/JJAP.52.07HA01]

Mukaiyama A, Nakamura T, Makabe K, Maki K, Goto Y, Kuwajima K.
The molten globule of β(2)-microglobulin accumulated at pH 4 and its role in protein folding.
J. Mol. Biol. 425, 273-291 (2013) [PMID:23154171]

Mukaiyama A, Nakamura T, Makabe K, Maki K, Goto Y, Kuwajima K.
Native-state heterogeneity of β2-microglobulin as revealed by kinetic folding and real-time NMR experiments.
J. Mol. Biol. 425, 257-272 (2013) [PMID:23154167]

Konuma T., Lee YH., Goto Y., Sakurai K.
Principal component analysis of chemical shift perturbation data of a multiple-ligand-binding system for elucidation of respective binding mechanism.
Proteins. 81, 107-118 (2013) [PMID:22927212]

Ogi H., Fukushima M., Uesugi K., Yagi H., Goto Y., Hirao M.
Acceleration of deposition of Aβ(1-40) peptide on ultrasonically formed Aβ(1-42) nucleus studied by wireless quartz-crystal-microbalance biosensor.
Biosens. Bioelectron. 40, 200-205 (2013) [PMID:22857904]

Lee YH., Goto Y.
Kinetic intermediates of amyloid fibrillation studied by hydrogen exchange methods with nuclear magnetic resonance.
Biochim. Biophys. Acta. 1824, 1307-1323 (2012) [PMID:22885025]

Yoshimura Y., Lin Y., Yagi H., Lee YH., Kitayama H., Sakurai K., So M., Ogi H., Naiki H., Goto Y.
Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation.
Proc. Natl. Acad. Sci. 109, 14446-14451 [PMID:22908252]

Shimanouchi T., Shimauchi N., Ohnishi R., Kitaura N., Yagi H., Goto Y., Umakoshi H., Kuboi R.
Formation of spherulitic amyloid β aggregate by anionic liposomes.
Biochem. Biophys. Res. Commun. 426, 165-171 (2012) [PMID:22842466]

Suzuki M., Sakurai K., Lee YH., Ikegami T., Yokoyama K., Goto Y.
A Back Hydrogen Exchange Procedure via the Acid-Unfolded State for a Large Protein.
Biochemistry 51, 5564-5570 (2012) [PMID:22738018]

Kamagata K., Kawaguchi T., Iwahashi Y., Baba A., Fujimoto K., Komatsuzaki T., Sambongi Y., Goto Y., Takahashi S.
Long-term observation of fluorescence of free single molecules to explore protein-folding energy landscapes.
J. Am. Chem. Soc. 134, 11525-11532 (2012) [PMID:22690958]

Yanagi, K., Sakurai, K., Yoshimura, Y., Konuma, T., Lee, YH., Sugase, K., Ikegami, T., Naiki, H., Goto, Y.
The monomer-seed interaction mechanism in the formation of the β2-microglobulin amyloid fibril clarified by solution NMR techniques.
J. Mol. Biol. in press (2012) [PMID:22683352]

Kume S., Lee YH., Miyamoto Y., Fukada H., Goto Y., Inui T.
Systematic Interaction Analysis of Human Lipocalin-type Prostaglandin D Synthase with Small Lipophilic Ligands.
Biochem. J. in press (2012) [PMID:22677050]

Chen J., Yagi H., Sormanni P., Vendruscolo M., Makabe K., Nakamura T., Goto Y., Kuwajima K.
Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone.
FEBS Lett. 586, 1120-1127 (2012) [PMID:22575645]

Chatani E., Yagi H., Naiki H., Goto Y.
Polymorphism of β2-Microglobulin Amyloid Fibrils Manifested by Ultrasonication-enhanced Fibril Formation in Trifluoroethanol.
J. Biol. Chen. 287, 22827-22837 (2012) [PMID:22566695]

Fukuhara A., Nakajima H., Miyamoto Y., Inoue K., Kume S., Lee YH., Noda M., Uchiyama S., Shimamoto S., Nishimura S., Ohkubo T., Goto Y., Takeuchi T., Inui T.
Drug delivery system for poorly water-soluble compounds using lipocalin-type prostaglandin D synthase.
J. Control. Release. 159, 143-150 (2012) [PMID:22226778]

Negoro S., Shibata N., Tanaka Y., Yasuhira K., Shibata H., Hashimoto H., Lee YH., Oshima S., Santa R., Oshima S., Mochiji K., Goto Y., Ikegami T., Nagai K., Kato D., Takeo M., Higuchi Y.
Three-dimensional structure of nylon hydrolase and mechanism of nylon-6 hydrolysis.
J. Biol. Chem. 287, 5079-5090 (2011) [PMID:22187439]

Suzuki M., Yokoyama K., Lee YH., Goto Y.
A Two-Step Refolding of Acid-Denatured Microbial Transglutaminase Escaping from the Aggregation-Prone Intermediate.
Biochemistry 50, 10390-10398 (2011) [PMID:22032733]

So, M., Yagi, H., Sakurai, K., Ogi, H., Naiki, H., Goto, Y.
Ultrasonication-Dependent Acceleration of the Formation of Amyloid Fibrils.
J. Mol. Biol. 412, 568-577 (2011) [PMID:21839746]

Babenko, V., Harada, T., Yagi, H., Goto, Y., Kuroda, R., Dzwolak, W.
Chiral superstructures of insulin amyloid fibrils.
Chirality. 8, 638-646 (2011) [PMID:21786341]

Lee, YH., Ikegami, T., Standley, DM., Sakurai, K., Hase, T., Goto, Y.
A Binding Energetics of Ferredoxin-NADP(+) Reductase with Ferredoxin and Its Relation to Function.
Chembiochem. 12,2062-2070 (2011) [PMID:21739557]

Sakurai, K., Fujioka, S., Konuma, T., Yagi, M., Goto, Y.,
A Circumventing Role for the Non-Native Intermediate in the Folding of β-Lactoglobulin.
Biochemistry 56, 6498-6507 (2011) [PMID:21678970 ]

Yanagi, K., Ashizaki, M., Yagi, H., Sakurai, K., Lee, YH., Goto, Y.,
Hexafluoroisopropanol induces amyloid fibrils of islet amyloid polypeptide by enhancing both hydrophobic and electrostatic interactions.
J. Biol. Chem. 286, 23959-23966 (2011) [PMID:21566116]

Ogi, H., Fukunishi, Y., Yanagida, T., Yagi, H., Goto, Y., Fukushima, M., Uesugi, K., Hirao, M.,
Seed-dependent deposition behavior of Aβ peptides studied with wireless quartz-crystal-microbalance biosensor.
Anal. Chem. 83, 4982-4988 (2011) [PMID:21557621]

Suetake, I., Mishima, Y., Kimura, H., Lee, YH., Goto, Y., Takeshima, H., Ikegami, T., Tajima, S.,
Characterization of DNA-binding activity in the N-terminal domain of DNA methyltransferase Dnmt3a.
Biochem. J. 437, 141-148 (2011) [PMID:21510846]

Kardos, J., Micsonai, A., Pai-Gabor, H., Petrik, E., Graf, Kovacs., Lee, YH., Naiki, H., Goto, Y.,
Reversible Heat-Induced Dissociation of β(2)-Microglobul Amyloid Fibrils.
Biochemistry 50, 3211-3220 (2011) [PMID:21388222]

Ozawa, D., Kaji, Y., Yagi, H., Sakurai, K., Kawakami, T., Naiki, H., Goto, Y.,
Destruction of amyloid fibrils of keratoepithelin peptides by laser irradiation coupled with amyloid-specific thiofravin T
J. Biol. Chem. 286, 10856-10863 (2011) [PMID:21300800]

Ozawa, D., Hasegawa, K., Lee, YH., Sakurai, K., Yanagi, K., Ookoshi, T., Goto, Y., Naiki, H.,
Inhibition of beta-2-Microglobulin amyloid fibril formation by alpha-2-Macroglobulin.
J. Biol. Chem. 286, 9668-9676 (2011) [PMID:21216953]

Konuma, T., Kimura, T., Matsumoto, S., Goto, Y., Fujisawa, T., Fersht, AR., Takahashi, S.,
Time-Resolved Small-Angle X-ray Scattering Study of the Folding Dynamics of Barnase.
J. Mol. Biol. 405, 1284-1294 (2011) [PMID:21146541]

Konuma, T., Chatani, E., Yagi, M., Sakurai, K., Ikegami, T., Naiki, H., Goto, Y.,
Kinetic Intermediates of β(2)-Microglobulin Fibril Elongation Probed by Pulse-Labeling H/D Exchange Combined with NMR Analysis.
J. Mol. Biol. 405, 851-862 (2011) [PMID:21108949]

Teoh, CL., Yagi, H., Griffin, MD., Goto, Y., Howlett, GJ.,
Visualization of polymorphism in apolipoprotein C-II amyloid fibrils
J. Biochem. 149, 67-74 (2011) [PMID:20889492]

Lee Y.-H., Kume S., Inui T. Goto Y.
A Calorimetric Approach with Structure-Based Thermodynamics for Molecular Interactions.
Netsu Sokutei 38, 165-173 (2011) [PMID:]

Yoshimura, Y., Sakurai, K., Lee, YH., Ikegami, T., Chatani, E., Naiki, H., Goto, Y.,
Direct Observation of Minimum-Sized Amyloid Fibrils Using Solution NMR Spectroscopy
Protein Sci. 12, 2347-2355 (2010) [PMID:20936689]

Ferkinghoff-Borg, J., Fonslet, J., Andersen, CB., Krishna, S., Pigolotti, S., Yagi, H., Goto, Y., Otzen, D., Jensen, MH.,
Stop-and-go kinetics in amyloid fibrillation
Phys. Rev. E 82, 010901(R) (2010) [PMID:20866557 ]

Yamaguchi, T., Yagi, H., Goto, Y., Matsuzaki, K., Hoshino, M.,
A Disulfide-Linked Amyloid-beta Peptide Dimer Forms a Protofibril-like Oligomer through a Distinct Pathway from Amyloid Fibril Formation.
Biochemistry 49, 7100-7107 (2010) [PMID:20666485]

Yagi, H., Takeuchi, H., Ogawa, S., Ito, N., Sakane, I., Hongo, K., Mizobata, T., Goto, Y., Kawata, Y.,
Isolation of short peptide fragments from alpha-synuclein fibril core identifies a residue important for fibril nucleation: A possible implication for diagnostic applications.
Biochim. Biophys. Acta 1804, 2077-2087 (2010) [PMID:20637318]

Chatani, E., Ohnishi, R., Konuma, T., Sakurai, K., Naiki, H., Goto, Y.,
Pre-Steady-State Kinetic Analysis of the Elongation of Amyloid Fibrils of beta(2)-Microglobulin with Tryptophan Mutagenesis.
J. Mol. Biol. 400, 1057-1066 (2010) [PMID:20595042]

Yamamoto, K., Yagi, H., Lee, YH., Kardos, J., Hagihara, Y., Naiki, H., Goto, Y.,
The amyloid fibrils of the constant domain of immunoglobulin light chain
FEBS Lett. 584, 3348-3353 (2010) [PMID:20580354]

Yagi, H., Ozawa, D., Sakurai, K., Kawakami, T.., Kuyama, H., Nishimura, O., Shimanouchi, T., Kuboi, R., Naiki, H., Goto, Y.,
Laser-induced propagation and destruction of amyloid beta fibrils
J. Biol. Chem. 285, 19660-19667 (2010) [PMID:20406822]

Hiramatu, H., Lu, M., Goto, Y., Kitagawa, T.
The beta-sheet structure pH dependence of the core fragments of bete2-microglobulin amyloid fibrils
Bul. Chem. Soci. Japan 83, 495-504 (2010)

Huong, VT., Shimanouchi, T., Shimauchi, N., Yagi, H., Umakoshi, H., Goto, Y., Kuboi, R.
Catechol derivatives inhibit the fibril formation of amyloid-beta peptides
J. Biosci Bioeng. 109, 629-634 (2010) [PMID: 20471605]

Shimanouchi, T., Shimauchi, N., Nishiyama, K., Huong, VT., Yagi, H., Goto, Y., Umakoshi, H., Kuboi, R.
Characterization of Amyloid β Fibrils with An Aqueous Two-Phase System: Implications of Fibril Formation
Sol. Extra. Res. Develop., Japan 17, 121-128 (2010)

Morinaga, A., Hasegawa, K., Nomura, R., Ookoshi, T., Goto, Y., Yamada, M. and Naiki, H.
Critical role of interfaces and agitation on the nucleation of Abeta amyloid fibrils at low concentrations of Abeta monomers. [Abstract]
Biochim. Biophys. Acta. 4, 986-995 (2010) [PMID: 20406822]

Hiramatsu, H., Lu, M., Matsuo, K., Gekko, K., Goto, Y. and Kitagawa, T.
Differences in the molecular structure of β₂-microglobulin between two morphologically different amyloid fibrils. [Abstract]
Biochemistry 49, 742-751 (2010) [PMID:20028123]

Chatani, E., Lee, YH., Yagi, H., Yoshimura, Y., Naiki, H. and Goto, Y.
Ultrasonication-dependent production and breakdown lead to minimum-sized amyloid fibrils. [Abstract]
Proc. Natl. Acad. Sci. 106, 11119-11124 (2009) [PMID:19564620]

Kameda, A., Morita, EU., Sakurai, K., Naiki, H. and Goto, Y.
NMR-based characterization of a refolding intermediate of β₂-microglobulin labeled using a wheat germ cell-free system. [Abstract]
Protein Sci. 18, 1592-1601 (2009) [PMID: 19606503]

Uversky, VN. and Goto, Y.
Acid denaturation and anion-induced folding of globular proteins: multitude of equilibium partially folded intermediates. [Abstract]
Curr. Protein Pept. Sci. 10, 447-455 (2009) [PMID: 19538151]

Pa?l-Ga?bor, H., Gombos, L., Micsonai, A., Kova?cs, E., Petrik, E., Kova?cs, J., Gra?f, L., Fidy, J., Naiki, H., Goto, Y., Liliom, K. and Kardos, J.
Mechanism of lysophosphatidic acid-induced amyloid fibril formation of β₂-microglobulin in vitro under physiological conditions. [Abstract]
Biochemistry 48, 5689-5699 (2009) [PMID: 19432419]

Sasahara, K., Yagi, H., Naiki, H. and Goto, Y.
Thermal response with exothermic effects of β₂-microglobulin amyloid fibrils and fibrillation. [Abstract]
J. Mol. Biol. 389, 584-594 (2009) [PMID: 19376758]

Sakurai, K., Konuma, T., Yagi, M. and Goto, Y.
Structural dynamics and folding of β-lactoglobulin probed by heteronuclear NMR. [Abstract]
Biochim. Biophys. Acta. 1790, 527-537 (2009)

Andersen, CB., Yagi, H., Manno, M., Mastorana, V., Ban, T., Christiansen, G., Otzen, DE., Goto, Y. and Rischel, C.
Branching in amyloid fibril growth. [Abstract]
Biophys. J. 96, 1529-1536 (2009) [PMID: 19217869]

Lee, YH., Chatani, E., Sasahara, K., Naiki, H. and Goto, Y.
A comprehensive model for packing and hydration for amyloid fibrils of β₂-microglobulin. [Abstract]
J. Biol. Chem. 284, 2169-2175 (2009) [PMID: 19017634]

Ozawa, D., Yagi, H., Ban, T., Kameda, A., Kawakami, T., Naiki, H. and Goto, Y.
Destruction of amyloid fibrils of A β₂-microgobulin fragment by laser beam irradiation. [Abstract]
J. Biol. Chem. 284, 1009-1017 (2009) [PMID:19010783]

Goto, Y., Yagi, H., Yamaguchi, K., Chatani, E. and Ban, T.
Structure, formation and propagation of amyloid fibrils. [Abstract]
Curr. Pharm. Des. 14, 3205-3218 (2008) [PMID:19075701]

Hasegawa, K., Tsutsumi-Yasuhara, S., Ookoshi, T., Ohhashi, Y., Kimura, H., Takahashi, N., Yoshida, H., Miyazaki, R., Goto, Y. and Naiki, H.
Growth of β₂-microglobulin-related amyloid fibrils by non-esterified fatty acids at a neutral pH. [Abstract]
Biochem. J. 416, 307-315 (2008) [PMID:18637792]

Sakata, M., Chatani, E., Kameda, A., Sakurai, K., Naiki, H. and Goto, Y.
Kinetic coupling of folding and prolyl isomerization of β₂-microglobulin studied by mutational analysis. [Abstract]
J. Mol. Biol. 382, 1242-1255 (2008) [PMID:18708068]

Ookoshi, T., Hasegawa, K., Ohhashi, Y., Kimura, H., Takahashi, N., Yoshida, H., Miyazaki, R., Goto, Y. and Naik, H.
Lysophospholipids induce the nucleation and extension of β₂-microglobulin-related amyloid fibrils at a neutral pH. [Abstract]
Nephrol Dial Transplant. 10, 3247-3255 (2008) [PMID:18467373]

Uzawa, T., Nishimura, C., Akiyama, S., Ishimori, K., Takahashi, S., Dyson, HJ. and Wright, PE.
Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H/D exchange coupled with 2D NMR. [Abstract]
Proc. Natl. Acad. Sci. 105, 13859-13864 (2008) [PMID:18779573]

Kimura, T., Maeda, A., Nishiguchi, S., Ishimori, K., Morishima, I., Konnno, T., Goto, Y. and Takahashi, S.
Dehydration of main-chain amides in the final folding step of single-chain monellin revealed by time-resolved infrared spectroscopy. [Abstract]
Proc. Natl. Acad. Sci. 105, 13391-13396 (2008) [PMID:18757727]

Yagi, M., Kameda, A., Sakurai, K., Nishimura, C. and Goto, Y.
Disulfide-linked bovine β-lactoglobulin dimers fold slowly navigating a glassy folding landscape. [Abstract]
Biochemistry 47, 5996-6006 (2008) [PMID:18465840]

Sasahara, K., Yagi, H., Sakai, M., Naiki, H. and Goto, Y.
Amyloid nucleation triggered by agitation of β₂-microglobulin under acidic and neutral pH conditions. [Abstract]
Biochemistry 47, 2650-2660 (2008) [PMID: 18211100]

Yamamoto, K., Yagi, H., Ozawa, D., Sasahara, K., Naiki, H. and Goto, Y.
Thiol compounds inhibit the formation of amyloid fibrils by β₂-microglobulin at neutral pH. [Abstract]
J. Mol. Biol. 376, 258-268 (2008) [PMID: 18155723]

Kardos, J., Harmat, V., Pallo, A., Barabas, O., Szilagyi, K., Graf, L., Naray-Szabo, G., Goto, Y., Zavodszky, P. and Gal, P.
Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r. [Abstract]
Mol. Immunol. 45, 1752-1760 (2008) [PMID: 17996945]

Kim, HJ., Chatani, E., Goto, Y. and Paik, SR.
Seed-dependent accelerated fibrillation of α-synuclein induced by periodic ultrasonication treatment. [Abstract]
J. Microbiol. Biotechnol. 17, 2027-2032 (2007) [PMID: 18167451]

Yagi, H., Ban, T., Morigaki, K., Naiki, H. and Goto, Y.
Visualization and classification of amyloid β supramolecular assemblies. [Abstract]
Biochemistry 46, 15009-15017 (2007) [PMID: 18044976]

Sakurai, K. and Goto, Y.
Principal component analysis of the pH-dependent conformational transitions of bovine β-lactoglobulin monitored by heteronuclear NMR. [Abstract]
Proc. Natl. Acad. Sci. 104, 15346-15351 (2007) [PMID: 17878316]

Nishiguchi, S., Goto, Y. and Takahashi, S.
Solvation and desolvation dynamics in apomyoglobin folding monitored by time-resolved infrared spectroscopy. [Abstract]
J. Mol. Biol. 373, 491-502 (2007) [PMID: 17850819]

Iwata, K., Matsuura, T., Sakurai, K., Nakagawa, A. and Goto, Y.
High-resolution crystal structure of β₂-microglobulin formed at pH 7.0. [Abstract]
J. Biochem. 142, 413-419 (2007) [PMID: 17646174]

Sasahara, K., Yagi, H., Naiki, H. and Goto, Y.
Heat-induced conversion of β₂-microglobulin and hen egg-white lysozyme into amyloid fibrils. [Abstract]
J. Mol. Biol. 372, 981-991 (2007). [PMID: 17681531]

Dzwolak, W., Loksztejn, A., Galinska-Rakoczy, A., Adachi, R., Goto, Y. and Rupnicki, L.
Conformational indeterminism in protein misfolding: chiral amplification on amyloidogenic pathway of insulin. [Abstract]
J. Am. Chem. Soc. 129, 7517-7522 (2007). [PMID: 17518465]

Hoshino, M., Katou, H., Yamaguchi, KI. and Goto, Y.
Dimethylsulfoxide-quenched hydrogen/deuterium exchange method to study amyloid fibril structure. [Abstract]
Biochim. Biophys. Acta. 1768, 1886-1899 (2007). [PMID: 17499210]

Kinoshita, M., Kamagata, K., Maeda, A., Goto, Y., Komatsuzaki, T. and Takahashi, S.
A new technique for the investigation of folding dynamics of proteins at the single molecule level for extended time periods. [Abstract]
Proc. Natl. Acad. Sci. 104, 10453-10458 (2007). [PMID: 17563378]

Kanekiyo, T., Ban, T., Aritake, K., Huang, ZL., Qu, WM., Okazaki, I., Mohri, I., Murayama, S., Ozono, K., Taniike, M., Goto, Y. and Urade, Y.
Lipocalin-type prostaglandin D synthase/beta-trace is a major amyloid β-chaperone in human cerebrospinal fluid. [Abstract]
Proc. Natl. Acad. Sci. 104, 6412-6417 (2007). [PMID: 17404210]

Matsumoto, S., Yane, A., Nakashima, S., Hashida, M., Fujita, M., Goto, Y. and Takahashi, S.
A rapid flow mixer with 11-μs mixing time microfabricated by a pulsed-laser ablation technique: observation of a barrier-limited collapse in cytochrome c folding. [Abstract]
J. Am. Chem. Soc. 129, 3840-3841 (2007). [PMID: 17375918]

Nagai, Y., Inui, T., Popiel, HA., Fujikake, N., Hasegawa, K., Urade, Y., Goto, Y., Naiki, H. and Toda, T.
A toxic monomeric conformer of the polyglutamine protein. [Abstract]
Nat. Struct. Mol. Biol. 14, 332-340 (2007).[PMID: 17369839]

Konuma, T., Sakurai, K. and Goto, Y.
Promiscuous binding of ligands by β-lactoglobulin involves hydrophobic interactions and plasticity. [Abstract]
J. Mol. Biol. 368, 209-218 (2007). [PMID: 17331535]

Sasahara, K., Yagi, H., Naiki, H. and Goto, Y.
Heat-triggered conversion of protofibrils into mature amyloid fibrils of β₂-microglobulin. [Abstract]
Biochemistry 46, 3286-3293 (2007). [PMID: 17316024]

Adachi, R., Yamaguchi, K., Yagi, H., Sakurai, K., Naiki, H. and Goto. Y.
Flow-induced alignment of amyloid protofilaments revealed by linear dichroism. [Abstract]
J. Biol. Chem. 282, 8978-8983 (2007). [PMID: 17264078]

Lee, YH., Tamura, K., Maeda, M., Hoshino, M., Sakurai, K., Takahashi, S., Ikegami, T., Hase, T, and Goto, Y.
Cores and pH-dependent dynamics of ferredoxin-NADP⁺ reductase revealed by H/D exchange. [Abstract]
J. Biol. Chem. 282, 5959-5967 (2007). [PMID: 17192259]

Standley, D. M., Yonezawa, Y., Goto, Y. and Nakamura, H.
Flexible docking of an amyloid-forming peptide from β₂-microglobulin.[Abstract]
FEBS Lett. 580, 6199-6205 (2006). [PMID: 17069810]

Iwata, K., Fujiwara, T., Matsuki, Y., Akutsu, H., Takahashi, S., Naiki, H. and Goto, Y.
3D structure of amyloid protofilaments of β₂-microglobulin fragment probed by solid-state NMR. [Abstract]
Proc. Natl. Acad. Sci. 103, 18119-18124 (2006). [PMID: 17108084]

Lu, M., Hiramatsu, H., Goto, Y. and Kitagawa, T.
Structure of interacting segments in the growing amyloid fibril of β₂-microglobulin probed with IR spectroscopy. [Abstract]
J. Mol. Biol. 362, 355-364 (2006). [PMID: 16919295]

Ban, T., Yamaguchi, K. and Goto Y.
Direct observation of amyloid fibril growth, propagation, and adaptation. [Abstract]
Acc. Chem. Res. 39, 663-670 (2006). [PMID: 16981683]

Ban, T., Morigaki, K., Yagi, H., Kawasaki, T., Kobayashi, A., Yuba, S., Naiki, H. and Goto, Y.
Real-time and single fibril observation of the formation of amyloid β spherulitic structures. [Abstract]
J. Biol. Chem. 281, 33677-33683 (2006). [PMID: 16959773]

Kihara, M., Chatani, E., Iwata, K., Yamamoto, K., Matsuura, T. Nakagawa, A., Naiki, H. and Goto, Y.
Conformation of amyloid fibrils of β₂-microglobulin probed by tryptophan mutagenesis. [Abstract]
J. Biol. Chem. 281, 31061-31069 (2006). [PMID: 16901902]

Yamaguchi, M., Naiki, H. and Goto, Y.
Mechanism by which the amyloid-like fibrils of a β₂-microglobulin fragment are induced by fluorine-substituted alcohols.[Abstract]
J. Mol. Biol. 363, 279-288 (2006). [PMID: 16959264]

Sasahara, K., Naiki, H. and Goto, Y.
Exothermic effects oserved upon heating of β₂-microglobulin monomers in the presence of amyloid seeds. [Abstract]
Biochemistry 45, 8760-8769 (2006). [PMID: 16846219]

Chatani, E., Naiki, H. and Goto, Y.
Seeding-dependent propagation and maturation of β₂-microglobulin amyloid fibrils under high pressure. [Abstract]
J. Mol. Biol. 359,1086-1096 (2006). [PMID: 16697008]

Uzawa, T., Kimura, T., Ishimori, K., Morishima, I., Matsui, T., Ikeda-Saito, M., Takahashi, S., Akiyama, S. and Fujisawa, T.
Time-resolved small-angle X-ray scattering investigation of the folding dynamics of heme oxygenase: implication of the scaling relationship for the submillisecond intermediates of protein folding. [Abstract]
J. Mol. Biol. 357, 997-1008 (2006). [PMID: 16460755]

Sakurai, K. and Goto, Y.
Dynamics and mechanism of the Tanford transition of bovine β-lactoglobulin studied using heteronuclear NMR spectroscopy. [Abstract]
J. Mol. Biol. 356, 483-496 (2006). [PMID: 16368109]

Chatani, E. and Goto, Y.
Structural stability of amyloid fibrils ofmicroglobulin in comparison with its native fold. [Abstract]
Biochim. Biophys. Acta. 1753, 64-75 (2005). [PMID: 16213801]

Kardos, J., Okuno, D., Kawai, T., Hagihara, Y., Yumoto, N., Kitagawa, T., Zavodszky, P., Naiki, H. and Goto, Y.
Structural studies reveal that the diverse morphology of β₂-microglobulin aggregates is a reflection of different molecular architectures. [Abstract]
Biochim. Biophys. Acta. 1753, 108-120 (2005). [PMID: 16185940]

Yamaguchi, K., Takahashi, S., Kawai, T., Naiki, H. and Goto, Y.
Seeding-dependent propagation and maturation of amyloid fibril conformation. [Abstract]
J. Mol. Biol. 352, 952-960 (2005). [PMID: 16126222]

Chatani, E., Kato, M., Kawai, T., Naiki, H. and Goto, Y.
Main-chain dominated amyloid structures demonstrated by the effect of high pressure. [Abstract]
J. Mol. Biol. 352, 941-951 (2005). [PMID: 16122756]

Sasahara, K., Naiki, H. and Goto, Y.
Kinetically controlled thermal response of β₂-microglobulin amyloid fibrils. [Abstract]
J. Mol. Biol. 352, 700-711 (2005). [PMID: 16098535]

Yamamoto, S., Hasegawa, K., Yamaguchi, I., Goto, Y., Gejyo, F. and Naiki, H.
Kinetic analysis of the polymerization and depolymerization of β₂-microglobulin-related amyloid fibrils in vitro. [Abstract]
Biochim. Biophys. Acta. 1753, 34-43 (2005). [PMID: 16084781]

Naiki, H., Yamamoto, S., Hasegawa, K., Yamaguchi, I., Goto, Y. and Gejyo, F.
Molecular interactions in the formation and deposition of β₂-microglobulin-related amyloid fibrils. [Abstract]
Amyloid 12, 15-25 (2005). [PMID: 16076607]

Maeda, M., Lee, Y., Ikegami, T., Tamura, K., Hoshino, M., Yamazaki, T., Nakayama, M., Hase, T. and Goto, Y.
Identification of the N- and C-terminal substrate binding segments of ferredoxin-NADP⁺ reductase by NMR. [Abstract]
Biochemistry 44, 10644-10653 (2005). [PMID: 16060673]

Raman, B., Ban, T., Sakai, M., Pasta, S. Y., Ramakrishna, T., Naiki, H., Goto, Y. and Rao, C. M.
αB-crystallin, a small heat shock protein, prevents the amyloid fibril growth of an amyloid β-peptide and β₂-microglobulin. [Abstract]
Biochem. J. 392(3), 573-581 (2005). [PMID: 16053447]

Ohhashi, Y., Kihara, M., Naiki, H. and Goto, Y.
Ultrasonication-induced amyloid fibril formation of β₂-microglobulin. [Abstract]
J. Biol. Chem. 280, 32843-32848 (2005). [PMID: 16046408]

Kimura, T., Akiyama, S., Uzawa, T., Ishimori, K., Morishima, I., Fujisawa, T. and Takahashi, S.
Specifically collapsed intermediate in the early stage of the folding of ribonuclease A. [Abstract]
J. Mol. Biol. 350, 349-362 (2005). [PMID: 15935376]

Hiramatsu, H., Goto, Y., Naiki, H. and Kitagawa, T.
Structural model of the amyloid fibril formed by β₂-microglobulin #21-31 fragment based on vibrational spectroscopy. [Abstract]
J. Am. Chem. Soc. 127, 7988-7989 (2005). [PMID: 15926803]

Kameda, A., Hoshino, M., Higurashi, T., Takahashi, S., Naiki, H. and Goto, Y.
Nuclear magnetic resonance characterization of the refolding intermediate of β₂-microglobulin trapped by non-native prolyl peptide bond. [Abstract]
J. Mol. Biol. 348, 383-397 (2005). [PMID: 15811375]

Raman, B., Ban, T., Yamaguchi, K., Sakai, M., Kawai, T., Naiki, H. and Goto, Y.
Metal ion-dependent effects of clioquinol on the fibril growth of an amyloid β peptide. [Abstract]
J. Biol. Chem. 280, 16157-16162 (2005). [PMID: 15718230]

Furukawa, Y., Ban, T., Hamada, D., Ishimori, K., Goto, Y. and Morishima, I.
Electron transfer reaction in a single protein molecule observed by total internal reflection fluorescence microscopy. [Abstract]
J. Am. Chem. Soc. 127, 2098-2103 (2005). [PMID: 15713086]

Kimura, T., Uzawa, T., Ishimori, K., Morishima, I., Takahashi, S., Konno, T., Akiyama, S. and Fujisawa, T.
Specific collapse followed by slow hydrogen-bond formation of β-sheet in the folding of single-chain monellin. [Abstract]
Proc. Natl. Acad. Sci. 102, 2748-2753 (2005). [PMID: 15710881]

Kanno, T., Yamaguchi, K., Naiki, H., Goto, Y. and Kawai, T.
Association of thin filaments into thick filaments revealing the structural hierarchy of amyloid fibrils. [Abstract]
J. Struct. Biol. 149, 213-218 (2005). [PMID: 15681237]

Raman, B., Chatani, E., Kihara, M., Ban, T., Sakai, M., Hasegawa, K., Naiki, H., Rao, C. M. and Goto, Y.
Critical balance of electrostatic and hydrophobic interactions is required for β₂-microglobulin amyloid fibril growth and stability. [Abstract]
Biochemistryb>44, 1288-1299 (2005). [PMID: 15667222]

Kihara, M., Chatani, E., Sakai, M., Hasegawa, K., Naiki, H. and Goto, Y.
Seeding-dependent maturation of β₂-microglobulin amyloid fibrils at neutral pH. [Abstract]
J. Biol. Chem. 280, 12012-12018 (2005). [PMID: 15659393]

Wadai, H., Yamaguchi, K., Takahashi, S., Kanno, T., Kawai, T., Naiki, H. and Goto, Y.
Stereospecific amyloid-like fibril formation by a peptide fragment of β₂-microglobulin. [Abstract]
Biochemistry 44, 157-164 (2005). [PMID: 15628856]

Ban, T., Hoshino, M., Takahashi, S., Hamada, D., Hasegawa, K., Naiki, H. and Goto, Y.
Direct observation of Aβ amyloid fibril growth and inhibition. [Abstract]
J. Mol. Biol. 344, 757-767 (2004). [PMID: 15533443]

Narimoto, T., Sakurai, K., Okamoto, A., Chatani, E., Hoshino, M., Hasegawa, K., Naiki, H. and Goto, Y.
Conformational stability of amyloid fibrils of β₂-microglobulin probed by guanidine-hydrochloride-induced unfolding. [Abstract]
FEBS Lett. 576, 313-319 (2004). [PMID: 15498554]

Kardos, J., Yamamoto, K., Hasegawa, K., Naiki, H. and Goto, Y.
Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry. [Abstract]
J. Biol. Chem. 279, 55308-55314 (2004). [PMID: 15494406]

Yamamoto, S., Hasegawa, K., Yamaguchi, I., Tsutsumi, S., Kardos, J., Goto, Y., Gejyo, F. and Naiki, H.
Low concentrations of sodium dodecyl sulfate induce the extension of β₂-microglobulin-related amyloid fibrils at a neutral pH. [Abstract]
Biochemistry 43, 11075-11082 (2004). [PMID: 15323566]

Egawa, T., Hishiki, T., Ichikawa, Y., Kanamori, Y., Shimada, H., Takahashi, S., Kitagawa, T. and Ishimura, Y.
Refolding processes of cytochrome P450_cam from ferric and ferrous acid forms to the native conformation: formations of folding intermediates with non-native heme coordination state. [Abstract]
J. Biol. Chem. 279, 32008-32017 (2004). [PMID: 15128748]

Yamaguchi, K., Katou, H., Hoshino, M., Hasegawa, K., Naiki, H. and Goto, Y.
Core and heterogeneity of β₂-microglobulin amyloid fibrils as revealed by H/D exchange. [Abstract]
J. Mol. Biol. 338, 559-571 (2004). [PMID: 15081813]

Hiramatsu, H., Goto, Y., Naiki, H. and Kitagawa, T.
Core structure of amyloid fibril proposed from IR-microscope linear dichroism. [Abstract]
J. Am. Chem. Soc. 126, 3008-3009 (2004). [PMID: 15012104]

Villanueva, J., Hoshino, M., Katou, H., Kardos, J., Hasegawa, K., Naiki, H. and Goto, Y.
Increase in the conformational flexibility of β₂-microglobulin upon copper binding: a molecular role of copper in dialysis-related amyloidosis. [Abstract]
Protein Sci. 13, 797-809 (2004). [PMID: 14767076]

Uzawa, T., Akiyama, S., Kimura, T., Takahashi, S., Ishimori, K., Morishima, I. and Fujisawa, T.
Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of α-helical content and compactness. [Abstract]
Proc. Natl. Acad. Sci. 101, 1171-1176 (2004). [PMID: 14711991]

Ohhashi, Y., Hasegawa, K., Naiki, H. and Goto, Y.
Optimum amyloid fibril formation of a peptide fragment suggests the amyloidogenic preference of β₂-microglobulin under physiological conditions. [Abstract]
J. Biol. Chem. 279, 10814-10821 (2004). [PMID: 14699107]

Yamamoto, S., Yamaguchi, I., Hasegawa, K., Tsutsumi, S., Goto, Y., Gejyo, F. and Naiki, H.
Glycosaminoglycans enhance the trifluoroethanol-induced extension of β₂-microglobulin-related amyloid fibrils at a neutral pH. [Abstract]
J. Am. Soc. Nephrol. 15, 126-133 (2004). [PMID: 14694164]

Tokuriki, N., Kinjo, M., Negi, S., Hoshino, M., Goto, Y., Urabe, I. and Yomo, T.
Protein folding by the effects of macromolecular crowding. [Abstract]
Protein Sci. 13, 125-133 (2004). [PMID: 14691228]

Yagi, M., Sakurai, K., Kalidas, C., Batt, C. A. and Goto, Y.
Reversible unfolding of bovine β-lactoglobulin mutants without a free thiol group. [Abstract]
J. Biol. Chem. 278, 47009-47015 (2003). [PMID: 12963719]

Chiba, T., Hagihara, Y., Higurashi, T., Hasegawa, K., Naiki, H. and Goto, Y.
Amyloid fibril formation in the context of full-length protein: effects of proline mutations on the amyloid fibril formation of β₂-microglobulin. [Abstract]
J. Biol. Chem. 278, 47016-47024 (2003). [PMID: 12958308]

Hirota-Nakaoka, N., Hasegawa, K., Naiki, H. and Goto, Y.
Dissolution of β₂-microglobulin amyloid fibrils by dimethylsufloxide. [Abstract]
J. Biochem. 134, 159-164 (2003). [PMID: 12944383]

Gozu, M., Lee Y.-H., Ohhashi, Y., Hoshino, M., Naiki, H. and Goto, Y.
Reduction and reoxidation of the disulfide bond of β₂-microglobulin as a probe to monitor its conformational dynamics. [Abstract]
J. Biochem. 133, 731-736 (2003). [PMID: 12869529]

Moosavi-Movahedi, A. A., Chamani, J., Goto, Y. and Hakimelahi, G. H.
Formation of molten globule-like state of cytochrome c induced by n-alkyl sulfates at low concentrations. [Abstract]
J. Biochem. 133, 93-102 (2003). [PMID: 12761203]

Fernández, A., Kardos, J., Scott, L. R., Goto, Y. and Berry, R. S.
Structural defects and the diagnosis of amyloidogenic propensity. [Abstract]
Proc. Natl. Acad. Sci. 100, 6446-6451 (2003). [PMID: 12743379]

Hasegawa, K., Ohhashi, Y., Yamaguchi, I., Takahashi, N., Tsutsumi, S., Goto, Y., Gejyo, F. and Naiki, H.
Amyloidogenic synthetic peptides of β₂-microglobulin--a role of the disulfide bond. [Abstract]
Biochem. Biophys. Res. Commun. 304, 101-106 (2003). [PMID: 12705891]

Ban, T., Hamada, D., Hasegawa, K., Naiki, H. and Goto, Y.
Direct observation of amyloid fibril growth monitored by thioflavin T fluorescence. (Accelerated Publication) [Abstract]
J. Biol. Chem. 278, 16462-16465 (2003) [PMID: 12646572]

Fernández, A., Kardos, J. and Goto, Y.
Protein folding: could hydrophobic collapse be coupled with hydrogen-bond formation? [Abstract]
FEBS Lett. 536, 187-192 (2003). [PMID: 12586361]

Maeda, M., Takeuchi, K., Kojima, M., Tanokura, M., Kimura, K., Amemiya, Y., Kihara, H. and Takahashi, K.
Kinetic studies of unfolding process of aspergillopepsin II by pH-jump methods. [Abstract]
Biochem. Biophys. Res. Commun. 301, 745-750 (2003). [PMID: 12565843]

Gozu, M., Hoshino, M., Higurashi, T., Kato, H. and Goto, Y.
The interaction of β₂-glycoprotein I domain V with chaperonin GroEL: the similarity with the domain V and membrane interaction. [Abstract]
Protein Sci. 11, 2792-2803 (2002). [PMID: 12441378]

Katou, H., Kanno, T., Hoshino, M., Hagihara, Y., Tanaka, H., Kawai, T., Hasegawa, K., Naiki, H. and Goto, Y.
The role of disulfide bond in the amyloidogenic state of β₂-microglobulin studied by heteronuclear NMR. [Abstract]
Protein Sci. 11, 2218-2229 (2002). [PMID: 12192077]

Sakurai, K. and Goto, Y.
Manipulating monomer-dimer equilibrium of bovine β-lactoglobulin by amino acid substitution. [Abstract]
J. Biol. Chem. 277, 25735-25740 (2002). [PMID: 12006601]

Sakai, K., Hoshino, M. and Goto, Y.
Interaction of β-lactoglobulin with chaperonin GroEL. [Abstract]
Proc. Indian Natl. Sci. Acad., A 68, 341-347. (2002)

Hoshino, M., Katou, H., Hagihara, Y., Hasegawa, K., Naiki, H. and Goto, Y.
Mapping the core of the β₂-microglobulin amyloid fibril by H/D exchange. [Abstract]
Nat. Struct. Biol. 9, 332-336 (2002). [PMID: 11967567]

Hong, D.-P., Gozu, M., Hasegawa, K., Naiki, H. and Goto, Y.
Conformation of β₂-microglobulin amyloid fibrils analyzed by reduction of the disulfide bond. [Abstract]
J. Biol. Chem. 277, 21554-21560 (2002). [PMID: 11943769]

Martsev, S. P., Dubnovitsky, A. P., Vlasov, A. P., Hoshino, M., Hasegawa, K., Naiki, H. and Goto, Y.
Amyloid fibril formation of mouse V_L domain under acidic pH. [Abstract]
Biochemistry 41, 3389-3395 (2002). [PMID: 11876647]

Maeda, M., Hamada, D., Hoshino, M., Onda, Y., Hase, T. and Goto, Y.
Partially folded structure of flavin adenine dinucleotide-depleted ferredoxin NADP⁺ reductase with residual NADP⁺ binding domain. [Abstract]
J. Biol. Chem. 277, 17101-17107 (2002). [PMID: 11872744]

Hagihara, Y., Hong, D.-P., Hoshino, M., Enjyoji, K., Kato, H. and Goto, Y.
Aggregation of β₂-glycoprotein I induced by sodium lauryl sulfate and lysophospholipids. [Abstract]
Biochemistry 41, 1020-1026 (2002). [PMID: 11790126]

Ohhashi, Y., Hagihara, Y., Kozhukh, G., Hoshino, M., Hasegawa, K., Yamaguchi, I., Naiki, H. and Goto, Y.
The intrachain disulfide bond of β₂-microglobulin is not essential for the immunoglobulin fold at neutral pH, but is essential for amyloid fibril formation at acidic pH. [Abstract]
J. Biochem. 131, 45-52 (2002). [PMID: 11754734]

Kozhukh, G., Hagihara, Y. Kawakami, T., Hasegawa, K., Naiki, H. and Goto, Y.
Investigation of a peptide responsible for amyloid fibril formation of β₂-microglobulin by Acromobacter protease I. [Abstract]
J. Biol. Chem. 277, 1310-1315 (2002). [PMID: 11687582]

Sakurai, K., Oobatake, M. and Goto, Y.
Salt-dependent monomer-dimer equilibrium of bovine β-lactoglobulin at pH 3. [Abstract]
Protein Sci. 10, 2325-2335 (2001). [PMID: 11604538]

Szewczuk, Z., Konishi, Y. and Goto, Y.
A two-process model describes the hydrogen exchange behavior of cytochrome c in the molten globule state with various extents of acetylation. [Abstract]
Biochemistry 40, 9623-9630 (2001). [PMID: 11583162]

Hong, D.-P., Hagihara, Y., Katou, H. and Goto, Y.
Flexible loop of β₂-glycoprotein I domain V specifically interacts with hydrophobic ligands. [Abstract]
Biochemistry 40, 8092-8100 (2001). [PMID: 11434778]

Katou, H., Hoshino, M., Kamikubo, H., Batt, C. A. and Goto, Y.
Native-like β-hairpin retained in the cold-denatured state of bovine β-lactoglobulin. [Abstract]
J. Mol. Biol. 310, 471-484 (2001). [PMID: 11428901]

Kuwata, K., Shastry, R., Cheng, H., Hoshino, M., Batt, C. A., Goto, Y. and Roder, H.
Structural and kinetic characterization of early folding events in β-lactoglobulin. [Abstract]
Nat. Struct. Biol. 8, 151-155 (2001). [PMID: 11175905]

Kuwata, K., Li, H., Yamada, H., Batt, C. A., Goto, Y. and Akasaka, K.
High pressure NMR reveals a variety of fluctuating conformers in β-lactoglobulin. [Abstract]
J. Mol. Biol. 305, 1073-1083 (2001). [PMID: 11162115]

Hoshino, M., Hagihara, Y., Nishii, I., Yamazaki, T., Katou, H. and Goto, Y.
Identification of the phospholipid-binding site of human β₂-glycoprotein I. [Abstract]
J. Mol. Biol. 304, 927-939 (2000). [PMID: 11124037]

Sakai, K., Sakurai, K., Sakai, M., Hoshino, M. and Goto, Y.
Conformation and stability of thiol-modified bovine β-lactoglobulin. [Abstract]
Protein Sci. 9, 1719-1729 (2000). [PMID: 11045618]

Forge, V., Hoshino, M., Kuwata, K., Arai, M., Kuwajima, K., Batt, C. A. and Goto, Y.
Is folding of β-lactoglobulin non-hierarchic?: intermediate with native-like β-sheet and non-native α-helix. [Abstract]
J. Mol. Biol. 296, 1039-1051 (2000). [PMID: 10686102]

Kuwata, K., Hoshino, M., Forge, V., Era, S., Batt, C. A. and Goto, Y.
Solution structure and dynamics of bovine β-lactoglobulin A. [Abstract]
Protein Sci. 8, 2541-2545 (1999). [PMID: 10595563]

Yamasaki, R., Hoshino, M., Wazawa, T., Ishii, Y., Yanagida, T., Kawata, Y., Higurashi, T., Sakai, K., Nagai, J. and Goto, Y.
Single molecular observation of GroEL with substrate proteins. [Abstract]
J. Mol. Biol. 292, 965-972 (1999). [PMID: 10512696]

Hong, D.-P., Hoshino, M., Kuboi, R. and Goto, Y.
Clustering of fluorine-substituted alcohols as a factor responsible for their marked effects on proteins and peptides. [Abstract]
J. Am. Chem. Soc. 121, 8427-8433 (1999).

Kuwata, K., Hoshino, M., Era, S., Batt, C. A. and Goto, Y.
α -> β transition of β-lactoglobulin as evidenced by heteronuclear NMR. [Abstract]
J. Mol. Biol. 283, 731-739 (1998). [PMID: 9790836]

Hagihara, Y., Hoshino, M., Hamada, D., Kataoka, M. and Goto, Y.
Chain-like conformation of heat-denatured ribonuclease A and cytochrome c as evidenced by solution X-ray scattering.
Fold. Des. 3, 195-201 (1998). [PMID: 9562549]

後藤　祐児
「過飽和生命科学の開拓」
領域融合レビュー 2, e002 (2013). [DOI:10.7875/leading.author.2.e002]
〜要約〜
過飽和は自然界にきわめて普遍的な物理化学現象であり，氷や雪，生体における結石，タンパク質をはじめとするさまざまな物質の結晶化から，コンニャクイモのえぐみにまでかかわる．・・・タンパク質科学の重要なテーマであるアミロイド線維の形成も，過飽和により支配された原因タンパク質の析出現象であると考えるとわかりやすい．・・・
http://leading.lifesciencedb.jp/

宗　正智、吉村　優一、八木 寿梓、後藤 祐児
超音波によるタンパク質のアミロイド線維形成反応の促進
ケミカルエンジニヤリング 58, 55-61 (2013).

櫻井 一正、後藤 祐児
タンパク質の一生集中マスター
第一章：フォールディング入門−タンパク質の構造や機能の基盤（38-48ページ）
(2007年3月10日発行) 羊土社

後藤祐児, 李映昊
タンパク質のアミロイド形成
Medical Bio. 10, 38-43. (2010)

李映昊, 小澤大作, 後藤祐児
アミロイド科学の新世界
生化学 81, 677-687. (2009)

八木 寿梓、櫻井 一正、後藤 祐児
アミロイド構造生物学の台頭
蛋白質 核酸 酵素 52, 1445-1453 (2007). [PMID:17926553]

櫻井 一正、後藤 祐児
タンパク質の一生集中マスター
第一章：フォールディング入門−タンパク質の構造や機能の基盤（38-48ページ）
(2007年3月10日発行) 羊土社

笹原 健二、後藤 祐児
β₂ミクログロブリンアミロイド線維の形成および熱応答のカロリメトリーによる解析
熱測定 33, 83-88 (2006).

後藤 祐児、桑島 邦博、谷澤 克行 [編]
タンパク質科学−構造・物性・機能
(2005年10月25日発行) 化学同人

茶谷 絵理、後藤 祐児
アミロイド線維形成機構−裏の世界の構築原理
実験医学 23, 174-180 (2005)

櫻井 一正、後藤 祐児
in vitroフォールディング
細胞工学 23, 1364-1369 (2004).

山口 圭一、後藤 祐児
β₂ミクログロブリンのアミロイド線維の構造と形成機構
生物物理 44, 212-217 (2004).

後藤 祐児、伴 匡人、星野 大
アミロイド線維の構造安定性−ナノスケールの針
蛋白質 核酸 酵素 49, 1091-1095 (2004). [PMID: 15168535]

後藤 祐児、大橋 祐美子
アミロイド線維の構造物性と危険性
Molecular Medicine 41, 401-408 (2004).

高橋 聡、鵜澤 尊規、藤澤 哲郎
X線小角散乱を使った蛋白質の折りたたみ運動のリアルタイム観察
蛋白質 核酸 酵素 49, 135-140 (2004). [PMID: 14969105]

後藤 祐児
タンパク質のフォールディングとアミロイド線維形成−タンパク質、昼の顔と夜の顔
実験医学 21, 898-902 (2003)

星野 大
β₂ミクログロブリンのアミロイド線維の構造解析
生化学 75, 143-148 (2003). [PMID: 12692974]

高橋 聡
タンパク質の折り畳み研究の展開
生化学 75, 54-59 (2003). [PMID: 12645135]

後藤 祐児、星野 大
β₂ミクログロブリンのアミロイド線維形成
蛋白質 核酸 酵素 47, 663-669 (2002). [PMID: 11995332]

後藤 祐児
タンパク質の低温変性
バイオサイエンスとインダストリー 60, 235-238 (2002)

後藤 祐児、加藤 秀典、星野 大
β-ラクトグロブリンの低温変性状態の構造
蛋白質 核酸 酵素 46, 1527-1534 (2001). [PMID: 11579547]

後藤 祐児、谷澤 克行
タンパク質の分子設計
序章：立体構造と機能の精密さと柔軟性 (1-35ページ)
(2001年2月20日発行) 共立出版

後藤 祐児
タンパク質の一生
第2章：タンパク質フォールディングというパズル (19-30ページ)
(2000年10月5日発行) 共立出版

Bengt Nolting 著、後藤 祐児 訳
タンパク質フォールディングのキネティクス：生物物理学的解析
(2000年6月26日発行) シュプリンガー・フェアラーク東京

後藤 祐児
蛋白質のフォールディング反応の1分子測定
蛋白質 核酸 酵素 44, 2614-2616 (1999)

後藤 祐児、新延 道夫
タンパク質ものがたり−私たちの生命を支えるもの
第10章：タンパク質はからだをまもる (126-141ページ)
(1998年11月15日発行) 蛋白質研究奨励会編・化学同人

星野 大、後藤 祐児
タンパク質のかたちと物性
第2章[2-2]：フォールディング中間状態 (98-109ページ)
(1997年8月20日発行) 共立出版