Yuji Goto, Kichitaro Nakajima, Suguru Yamamoto, Keiichi Yamaguchi.
Supersaturation, a Critical Factor Underlying Proteostasis of Amyloid Fibril Formation Journal of Molecular Biology , , (2024) [DOI:10.1016/j.jmb.2024.168475]
2023
Keiichi Yamaguchi, Kichitaro Nakajima, Yuji Goto.
Mechanisms of polyphosphate-induced amyloid fibril formation triggered by breakdown of supersaturation Biophysics and Physicobiology 20,1 , (2023) [DOI:10.2142/biophysico.bppb-v20.0013]
2022
Kichitaro Nakajima, Keiichi Yamaguchi, Masahiro Noji, César Aguirre, Kensuke Ikenaka, Hideki Mochizuki, Lianjie Zhou, Hirotsugu Ogi, Toru Ito, Ichiei Narita, Fumitake Gejyo, Hironobu Naiki, Suguru Yamamoto and Yuji Goto.
Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis nature communications13, 5689 , (2022) [DOI:10.1038/s41467-022-33247-3]
Yuji Goto, Masahiro Noji, Kichitaro Nakajima and Keiichi Yamaguchi.
Supersaturation-Dependent Formation of Amyloid Fibrils Molecules 27(14), 4588 , (2022) [DOI:10.3390/molecules27144588]
Yuki Yoshikawa, Keisuke Yuzu, Naoki Yamamoto, Ken Morishima, Rintaro Inoue, Masaaki Sugiyama, Tetsushi Iwasaki, Masatomo So, Yuji Goto, Atsuo Tamura and Eri Chatani .
Pathway Dependence of the Formation and Development of Prefibrillar Aggregates in Insulin B Chain Molecules 27 (13), 3964 , (2022) [DOI:10.3390/molecules27133964]
Henrietta Vadászi, Bence Kiss, András Micsonai, Gitta Schlosser, Tamás Szaniszló, Réka Á.Kovács, Balázs A.Györffy, Katalin A.Kékesi1, Yuji Goto, Barbara Uzonyi, Károly Liliom and József Kardos.
Competitive inhibition of the classical complement pathway using exogenous single-chain C1q recognition proteins Journal of Biological Chemistry 298,7 , (2022) [DOI:10.1016/j.jbc.2022.102113]
Kentaro Noi, Kichitaro Nakajima, Keiichi Yamaguchi, Masatomo So, Kensuke Ikenaka, Hideki Mochizuki, Yuji Goto and Hirotsugu Ogi.
Acceleration of amyloid fibril formation by multichannel sonochemical reactor Japanese Journal of Applied Physics 61 SG1002 , (2022) [DOI:10.35848/1347-4065/ac4142]
András Micsonai, Éva Moussong, Frank Wien, Eszter Boros, Henrietta Vadászi, Nikoletta Murvai, Young-Ho Lee, Tamás Molnár, Matthieu Réfrégiers, Yuji Goto, Ágnes Tantos, and József Kardos.
BeStSel: webserver for secondary structure and fold prediction for protein CD spectroscopy Nucleic Acids Research , (2022) [hal-03670788]
Yuji Goto , Kichitaro Nakajima, Keiichi Yamaguchi, Masatomo So, Kensuke Ikenaka, Hideki Mochizuki, and Hirotsugu Ogi.
Development of HANABI, an ultrasonication-forced amyloid fibril inducer Neurochemistry International 153 , (2022) [DOI:10.1016/j.neuint.2021.105270]
Éva Bulyáki, Judit Kun, Tamás Molnár, Alexandra Papp, András Micsonai, Henrietta Vadászi, Borbála Márialigeti, Attila István Kovács, Gabriella Gellén, Keiichi Yamaguchi, Yuxi Lin, Masatomo So, Mihály Józsi, Gitta Schlosser, Young-Ho Lee, Károly Liliom, Yuji Goto, József Kardos
Pathogenic D76N Variant of β2-Microglobulin: Synergy of Diverse Effects in Both the Native and Amyloid States Biology10(11) ,1197 (2021) [DOI:10.3390/biology10111197]
Keiichi Yamaguchi, Kenshiro Hasuo, Masatomo So, Kensuke Ikenaka, Hideki Mochizuki, and Yuji Goto
Strong acids induce amyloid fibril formation of β2-microglobulin via an anion-binding mechanism Journal of Biological Chemistry, (2021) [DOI:10.1016/j.jbc.2021.101286]
Kichitaro Nakajima, Hajime Toda, Keiichi Yamaguchi, Masatomo So,Kensuke Ikenaka, Hideki Mochizuki, Yuji Goto, and Hirotsugu Ogi
Half-Time Heat Map Reveals Ultrasonic Effects on Morphology and Kinetics of Amyloidogenic Aggregation Reaction ACS Chem. Neurosci.12,18 ,3456-3466 (2021) [DOI:10.1021/acschemneuro.1c00461]
Kentaro Noi, Kensuke Ikenaka, Hideki Mochizuki, Yuji Goto, and Hirotsugu Ogi.
Disaggregation Behavior of Amyloid β Fibrils by Anthocyanins Studied by Total-Internal-Reflection-Fluorescence Microscopy Coupled with a Wireless Quartz-Crystal Microbalance Biosensor Analytical Chemistry93(32),11176-11183 (2021) [DOI:10.1021/acs.analchem.1c01720]
Masatomo So, Yuto Kimura, Keiichi Yamaguchi, Toshihiko Sugiki, Toshimichi Fujiwara, César Aguirre, Kensuke Ikenaka, Hideki Mochizuki, Yasushi Kawata, and Yuji Goto.
Polyphenol-solubility alters amyloid fibril formation of α-synuclein Protein Science30(8),1701-1713 (2021) [DOI:10.1002/pro.4130]
Eri Chatani, Keisuke Yuzu, Yumiko Ohhashi, and Yuji Goto.
Current Understanding of the Structure, Stability and Dynamic Properties of Amyloid Fibrils International Journal of Molecular Sciences22(9), 4349 (2021) [DOI:10.3390/ijms22094349]
Keiichi Yamaguchi, Masatomo So, César Aguirre, Kensuke Ikenaka, Hideki Mochizuki, Yasushi Kawata, and Yuji Goto.
Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners Journal of Biological Chemistry296, (2021) [DOI:10.1016/j.jbc.2021.100510]
Kichitaro Nakajima, Kentaro Noi, Keiichi Yamaguchi, Masatomo So, Kensuke Ikenaka, Hideki Mochizuki, Hirotsugu Ogi, and Yuji Goto.
Optimized sonoreactor for accelerative amyloid-fibril assays through enhancement of primary nucleation and fragmentation Ultrasonics Sonochemistry73, (2021) [DOI:10.1016/j.ultsonch.2021.105508]
Masahiro Noji, Tatsushi Samejima, Keiichi Yamaguchi, Masatomo So, Keisuke Yuzu, Eri Chatani, Yoko Akazawa-Ogawa, Yoshihisa Hagihara, Yasushi Kawata, Kensuke Ikenaka, Hideki Mochizuki, József Kardos, Daniel E. Otzen,Vittorio Bellotti, Johannes Buchner, and Yuji Goto.
Breakdown of supersaturation barrier links protein folding to amyloid Communications Biology4, 120 (2021) [DOI:10.1038/s42003-020-01641-6]pressrelease
2020
Hiroki Mizuno, Junichi Hoshino, Masatomo So, Yuta Kogure, Takeshi Fujii, Yoshifumi Ubara, Kenmei Takaichi, Tetsuko Nakaniwa, Hideaki Tanaka, Genji Kurisu, Fuyuki Kametani, Mayuko Nakagawa,Tsuneaki Yoshinaga, Yoshiki Sekijima, Keiichi Higuchi, Yuji Goto, and Masahide Yazaki.
Dialysis-Related Amyloidosis Associated with a Novel β2-Microglobulin Variant. Amyloid28, 42-49 (2020) [DOI:10.1080/13506129.2020.1813097]
Nakajima K, Yamazaki T, Kimura Y, So M, Goto Y, Ogi H.
Time-Resolved Observation of Evolution of Amyloid-β Oligomer with Temporary Salt Crystals. J Pyhs Chem Lett11, 6176-6184 (2020) [PMID: 32687370]
Okuwaki R, Shinmura I, Morita S, Matsugami A, Hayashi F, Goto Y, Nishimura C.
Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity. Biochim Biophys Acta - Proteins and Proteomics1868(9), 140464 (2020) [PMID: 32497661]
Sawada M, Yamaguchi K, Hirano M, Noji M, So M, Otzen D, Kawata Y, Goto Y.
Amyloid formation of α-synuclein based on the solubility-and supersaturation-dependent mechanism. Langmuir36, 4671-4681 (2020) [PMID: 32271585]
Furukawa K, Aguirre C, Ito T, Yamamoto S, Yamaguchi K, Sato M, Kaneko Y, Goto S, Goto Y, Narita I.
Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism. Curr Res Struct Biol2, 35-44 (2020) [DOI: 10.1016/j.crstbi.2020.03.001]
Ito T, Yamamoto S, Yamaguchi K, Sato M, Kaneko Y, Goto S, Goto Y, Narita I.
Inorganic polyphosphate potentiates lipopolysaccharide-induced macrophage inflammatory response. J Biol Chem295, 4014-4023 (2020) [PMID: 32041779]
Taricska N, Horvath D, Menyhard DK, Akontz-Kiss H, Noji M, So M, Goto Y, Fujiwara T, Perczel A.
The route from the folded to the amyloid state: exploring the potential energy surface of a drug‐like miniprotein. Chemistry26, 1968-1978 (2020) [PMID: 31647140]
2019
Muta H, So M, Sakurai K, Kardos J, Naiki H, Goto Y.
Amyloid Formation under Complicated Conditions in Which β2-Microglobulin Coexists with Its Proteolytic Fragments. Biochemistry58, 4925-4934 (2019) [PMID: 31724398]
Noji M, Sasahara K, Yamaguchi K, So M, Sakurai K, Kardos J, Naiki H, Goto Y.
Heating during agitation of β2-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pH. J Biol Chem294, 15826-15835 (2019) [PMID: 31495783]
Sasahara K, Yamaguchi K, So M, Goto Y.
Polyphosphates diminish solubility of a globular protein and thereby promote amyloid aggregation. J Biol Chem294, 15318-15329 (2019) [PMID: 31439662]
Araki K, Yagi N, Aoyama K, Choong CJ, Hayakawa H, Fujimura H, Nagai Y, Goto Y, Mochizuki H.
Parkinson's disease is a type of amyloidosis featuring accumulation of amyloid fibrils of α-synuclein. Proc Natl Acad Sci U S A116, 17963-17969 (2019) [PMID: 31427526]
Zhang C, Yamaguchi K, So M, Sasahara K, Ito T, Yamamoto S, Narita I, Kardos J, Naiki H, Goto Y.
Possible mechanisms of polyphosphate-induced amyloid fibril formation of β2-microglobulin. Proc Natl Acad Sci U S A116, 12833-12838 (2019) [PMID: 31182591]
Kakuda K, Ikenaka K, Araki K, So M, Aguirre C, Kajiyama Y, Konaka K, Noi K, Baba K, Tsuda H, Nagano S, Ohmichi T, Nagai Y, Tokuda T, El-Agnaf OMA, Ogi H, Goto Y, Mochizuki H.
Ultrasonication-based rapid amplification of α-synuclein aggregates in cerebrospinal fluid. Sci Rep9, 6001 (2019) [PMID: 309799351]
Kakuda K, Niwa A, Honda R, Yamaguchi KI, Tomita H, Nojebuzzaman M, Hara A, Goto Y, Osawa M, Kuwata K.
A DISC1 point mutation promotes oligomerization and impairs information processing in a mouse model of schizophrenia. J Biochem165, 369-378 (2019) [PMID: 30561706]
Iida M, Mashima T, Yamaoki Y, So M, Nagata T, Katahira M.
The anti-prion RNA aptamer R12 disrupts the Alzheimer's disease-related complex between prion and amyloid β. FEBS J286, 2355-2365 (2019) [PMID: 30916478]
Yamaguchi K, Kamatari YO, Ono F, Shibata H, Fuse T, Elhelaly AE, Fukuoka M, Kimura T, Hosokawa-Muto J, Ishikawa T, Tobiume M, Takeuchi Y, Matsuyama Y, Ishibashi D, Nishida N, Kuwata K.
A designer molecular chaperone against transmissible spongiform encephalopathy slows disease progression in mice and macaques. Nat Biomed Eng3, 206-219 (2019) [PMID: 30948810]
2018
Noji M, So M, Yamaguchi K, Hojo H, Onda M, Akazawa-Ogawa Y, Hagihara Y, Goto Y.
Heat-Induced Aggregation of Hen Ovalbumin Suggests a Key Factor Responsible for Serpin Polymerization. Biochemistry57, 5415-5426 (2018) [PMID: 30148614]
Adachi M, Noji M, So M, Sasahara K, Kardos J, Naiki H, Goto Y.
Aggregation-phase diagrams of β2-microglobulin reveal temperature and salt effects on competitive formation of amyloids versus amorphous aggregates. J Biol Chem293, 14775-14785 (2018) [PMID: 30077972]
Negoro S, Shibata N, Lee YH, Takehara I, Kinugasa R, Nagai K, Tanaka Y, Kato DI, Takeo M, Goto Y, Higuchi Y.
Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolase. Sci Rep8, 9725 (2018) [PMID: 29950566]
Micsonai A, Wien F, Bulyaki E, Kun J, Moussong E, Lee YH, Goto Y, Refregiers M, Kardos J.
BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra. Nucleic Acids Res46, W315-W322 (2018) [PMID: 29893907]
2017
Terakawa MS, Lee YH, Kinoshita M, Lin Y, Sugiki T, Fukui N, Ikenoue T, Kawata Y, Goto Y.
Membrane-induced initial structure of α-synuclein control its amyloidogenesis on model membranes. Biochim Biophys Acta. , (2017) [PMID: 29273335]
Goto Y, Adachi M, Muta H, So M.
Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism. Biophys Rev. , (2017) [PMID: 29256120]
Nitani A, Muta H, Adachi M, So M, Sasahara K, Sakurai K, Chatani E, Naoe K, Ogi H, Hall D, Goto Y.
Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation. J Biol Chem. , (2017) [PMID: 29101231]
Y. Matsushita, H. Sekiguchi, C. Jae Wong, M. Nishijima, K. Ikezaki, D. Hamada, Y. Goto & Y. C. Sasaki
Nanoscale Dynamics of Protein Assembly Networks in Supersaturated Solutions. Scientific Reports. , (2017) [PMID: 29093529]
Sakurai K, Yagi M, Konuma T, Takahashi S, Nishimura C, Goto Y.
Non-native α-Helices in the Initial Folding Intermediate Facilitate the Ordered Assembly of the β-Barrel in β-Lactoglobulin. Biochemistry. , (2017) [PMID: 28795569]
Kinoshita M, Kakimoto E, Terakawa MS, Lin Y, Ikenoue T, So M, Sugiki T, Ramamoorthy A, Goto Y, Lee YH.
Model membrane size-dependent amyloidogenesis of Alzheimer's amyloid-β peptides. Phys Chem Chem Phys. , (2017) [PMID: 28608875]
Kinoshita M, Lin Y, Nakatsuji M, Inui T, Lee YH.
Kinetics and polymorphs of yeast prion Sup35NM amyloidogenesis. Int J Biol Macromol. , (2017) [PMID: 28476595]
Nakajima K, So M, Takahashi K, Tagawa YI, Hirao M, Goto Y, Ogi H.
Optimized Ultrasonic Irradiation Finds Out Ultrastable Aβ1-40 Oligomers. J Phys Chem B. , (2017) [PMID: 28260388]
So M, Hata Y, Naiki H, Goto Y.
Heparin-induced amyloid fibrillation of β2 -microglobulin explained by solubility and a supersaturation-dependent conformational phase diagram. Protein Sci. , (2017) [PMID: 28249361]
Kinoshita M, Kim JY, Kume S, Lin Y, Mok KH, Kataoka Y, Ishimori K, Markova N, Kurisu G, Hase T, Lee YH.
Energetic basis on interactions between ferredoxin and ferredoxin NADP+ reductase at varying physiological conditions. Biochem Biophys Res Commun. , (2017) [PMID: 27894842]
Kinoshita M, Kim JY, Lin Y, Markova N, Hase T, Lee YH.
Biochemical and Biophysical Methods to Examine the Effects of Site-Directed Mutagenesis on Enzymatic Activities and Interprotein Interactions. Methods Mol Biol. , (2017) [PMID: 27709594]
2016
Nakajima K, Nishioka D, Hirao M, So M, Goto Y, Ogi H.
Drastic acceleration of fibrillation of insulin by transient cavitation bubble. Ultrason Sonochem. , (2016) [PMID: 28069203]
Zhao R, So M, Maat H, Ray NJ, Arisaka F, Goto Y, Carver JA, Hall D.
Measurement of amyloid formation by turbidity assay-seeing through the cloud. Biophys Rev. , (2016) [PMID: 28003859]
Kim JY, Kinoshita M, Kume S, Gt H, Sugiki T, Ladbury JE, Kojima C, Ikegami T, Kurisu G, Goto Y, Hase T, Lee YH.
Non-covalent forces tune the electron transfer complex between ferredoxin and sulfite reductase to optimize enzymatic activity. Biochem J. , (2016) [PMID: 27551107]
Noda S, So M, Adachi M, Kardos J, Akazawa-Ogawa Y, Hagahara Y, Goto Y.
Thioflavin T-Silent Denaturation Intermediates Support the Main-Chain-Dominated Architecture of Amyloid Fibrils. Biochemistry. , (2016) [PMID: 27345358]
So M, Hall D, Goto Y.
Revisiting supersaturation as a factor determining amyloid fibrillation. Curr Opin Struct Biol. , (2016) [PMID: 26774801]
Hall D, Zhao R, Dehlsen I, Bloomfield N, Williams SR, Arisaka F, Goto Y, Carver JA.
Protein aggregate turbidity: Simulation of turbidity profiles for mixed aggregation reactions. Anal Biochem. , (2016) [PMID: 26763936]
Lin Y, Kardos J, Imai M, Ikenoue T, Kinoshita M, Sugiki T, Ishimori K, Goto Y, Lee YH.
Amorphous aggregation of cytochrome c with inherently low amyloidogenicity is characterized by the metastability of supersaturation and the phase diagram. Langmuir., (2016) [PMID:26824789]
Aguirre C, Goto Y, Costas M.
Thermal and chemical unfolding pathways of PaSdsA1 sulfatase, a homo-dimer with topologically interlinked chains. FEBS Lett. 590(2) ,202-14 (2016) [PMID:26823168]
Masatomo So, Damien Hall, Yuji Goto.
Revisiting supersaturation as a factor determining amyloid fibrillation Current Opinion in Structural Biology., (2016) [doi:10.1016/j.sbi.2015.11.009]
Nokwe CN, Hora M, Zacharias M, Yagi H, Peschek J, Reif B, Goto Y, Buchner J.
Specific non-native interactions. J Mol Biol. , (2016) [PMID:]
Hall D, Zhao R, Dehlsen I, Bloomfield N, Williams SR, Arisaka F, Goto Y, Carver JA.
Protein aggregate turbidity: Simulation of turbidity profiles for mixed aggregation reactions. Anal Biochem. , (2016) [PMID:26763936]
2015
Matsushita Y, Sekiguchi H, Ichiyanagi K, Ohta N, Ikezaki K, Goto Y, Sasaki YC.
Time-resolved X-ray Tracking of Expansion and Compression Dynamics in Supersaturating Ion-Networks. Sci Rep. 5,17647 (2015) [doi: 10.1038/srep17647.]
Araki K, Yagi N, Ikemoto Y, Yagi H, Choong CJ, Hayakawa H, Beck G, Sumi H, Fujimura H, Moriwaki T, Nagai Y, Goto Y, Mochizuki H.
Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson's disease patients. Sci Rep. 5,17625 (2015) [doi: 10.1038/srep17625.]
Nokwe CN, Hora M, Zacharias M, Yagi H, John C, Reif B, Goto Y, Buchner J.
The Antibody Light-Chain Linker Is Important for Domain Stability and Amyloid Formation. J Mol Biol. 427(22),3572-86 (2016) [PMID: 26408269]
So M, Ishii A, Hata Y, Yagi H, Naiki H, Goto Y.
Supersaturation-limited and unlimited phase spaces compete to produce maximal amyloid fibrillation near the critical micelle concentration of sodium dodecyl sulfate. Langmuir. 31(36),9973-82 (2015) [PMID:26291985]
Konuma T, Sakurai K, Yagi M, Goto Y, Fujisawa T, Takahashi S.
Highly Collapsed Conformation of the Initial Folding Intermediates of β-Lactoglobulin with Non-Native α-Helix. J Mol Biol. 427,3158-65 (2015) [PMID:26232603]
Kinoshita M, Kim JY, Kume S, Sakakibara Y, Sugiki T, Kojima C, Kurisu G, Ikegami T, Hase T, Kimata-Ariga Y, Lee YH.
Physicochemical nature of interfaces controlling ferredoxin NADP+ reductase activity through its interprotein interactions with ferredoxin. Biochim Biophys Acta.-Bioenergetics 1847(10),1200-11 (2015) [PMID:26087388]
Adachi M, So M, Sakurai K, Kardos J, Goto Y.
Supersaturation-limited and unlimited phase transitions compete to produce the pathway complexity in amyloid fibrillation. J Biol Chem. 290,18134-45 (2015) [PMID:26063798]
Micsonai A, Wien F, Kernya L, Lee YH, Goto Y, Refregiers M, Kardos J.
Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy. Proc Natl Acad Sci U S A. 112(24),3095-103 (2015) [PMID:26038575]
Sakurai K, Nakahata R, Lee YH, Kardos J, Ikegami T, Goto Y.
Effects of a reduced disulfide bond on aggregation properties of the human IgG1 CH3 domain. Biochim Biophys Acta. , (2015) [PMID:25748879]
Kim J.Y., Ikegami T., Goto Y., Hase T. and Lee Y.-H.
Interactions of Ferredoxin and Sulfite Reductase under Different Sodium Chloride Concentrations by NMR spectroscopy and Isothermal Titration Calorimetry. Sulfur Metabolism in Plants (Springer) , (2015)
Hall D, Kardos J, Edskes H, Carver JA, Goto Y.
A multi-pathway perspective on protein aggregation: Implications for control of the rate and extent of amyloid formation. FEBS Lett. 589(2),672-9 (2015) [PMID:25647034]
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 (2015) [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 (2015) [PMID:25406316]
2014
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]
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]
