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Rchr
J-GLOBAL ID：200901065276970804
Update date: Oct. 09, 2024 Sakurai Kazumasa
サクライ カズマサ | Sakurai Kazumasa
ClipsPapers (45)
- Ryosuke Tomiyama, Masatomo So, Yohei Miyanoiri, Kazumasa Sakurai. The Residual Structure of Acid-Denatured Β2-Microglobulin is Relevant to an Ordered Fibril Morphology. SSRN Electronic Journal. 2022. 32. 1
- Kazumasa Sakurai, Ryosuke Tomiyama. Enhanced accessibility and hydrophobicity of amyloidogenic intermediates of the β2-microglobulin D76N mutant revealed by high-pressure experiments. Journal of Biological Chemistry. 2021. 296. 100333-100333
- Koki Furukawa, Cesar Aguirre, Masatomo So, Kenji Sasahara, Yohei Miyanoiri, Kazumasa Sakurai, Keiichi Yamaguchi, Kensuke Ikenaka, Hideki Mochizuki, Jozsef Kardos, et al. Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism. Current Research in Structural Biology. 2020. 2. 35-44
- Hiroya Muta, Masatomo So, Kazumasa Sakurai, Jozsef Kardos, Hironobu Naiki, Yuji Goto. Amyloid Formation under Complicated Conditions in Which β2-Microglobulin Coexists with Its Proteolytic Fragments. Biochemistry. 2019
- 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. The Journal of biological chemistry. 2019. in press. 43. 15826-15835
- Sakurai K, Tomiyama R, Shiraki T, Yonezawa Y. Loosening of side-chain packing associated with perturbations in peripheral dynamics induced by the D76N mutation of β2-microglobulin revealed by pressure-NMR and molecular dynamic simulations. Biomolecules. 2019. 9. 9. 491-491
- Sakurai K, Maeno A, Lee YH, Akasaka K. Conformational Properties Relevant to the Amyloidogenicity of beta2-Microglobulin Analyzed Using Pressure- and Salt-Dependent Chemical Shift Data. The Journal of Physical Chemistry B. 2019. 123. 4. 836-844
- Ayame Nitani, Hiroya Muta, Masayuki Adachi, Masatomo So, Kenji Sasahara, Kazumasa Sakurai, Eri Chatani, Kazumitsu Naoe, Hirotsugu Ogi, Damien Hall, et al. Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation. JOURNAL OF BIOLOGICAL CHEMISTRY. 2017. 292. 52. 21219-21230
- 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. 56. 36. 4799-4807
- Tatsuya Ikenoue, Yuxi Lin, Misaki Kinoshita, Kazumasa Sakurai, Yuji Goto, Young-Ho Lee. Molecular structure of amyloid fibrils revealed by thermodynamics. Protein-Protein Interactions (PPIs): Types, Methods for Detection and Analysis. 2016. 81-96
- Satomi Inaba, Akihiro Maeno, Kazumasa Sakurai, Sunilkumar Puthenpurackal Narayanan, Takahisa Ikegami, Kazuyuki Akasaka, Masayuki Oda. Functional conformer of c-Myb DNA-binding domain revealed by variable temperature studies. FEBS JOURNAL. 2015. 282. 23. 4497-4514
- Tsuyoshi Konuma, Kazumasa Sakurai, Masanori Yagi, Yuji Goto, Tetsuro Fujisawa, Satoshi Takahashi. Highly Collapsed Conformation of the Initial Folding Intermediates of beta-Lactoglobulin with Non-Native alpha-Helix. JOURNAL OF MOLECULAR BIOLOGY. 2015. 427. 19. 3158-3165
- Masayuki Adachi, Masatomo So, Kazumasa Sakurai, Jozsef Kardos, Yuji Goto. Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid Fibrillation. JOURNAL OF BIOLOGICAL CHEMISTRY. 2015. 290. 29. 18134-18145
- 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. Biochimica et biophysica acta. 2015
- 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. Biochimica et biophysica acta. 2013. 1834. 12. 2640-2646
- Tsuyoshi Konuma, Young-Ho Lee, Yuji Goto, Kazumasa Sakurai. Principal component analysis of chemical shift perturbation data of a multiple-ligand-binding system for elucidation of respective binding mechanism. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS. 2013. 81. 1. 107-118
- Kotaro Yanagi, Kazumasa Sakurai, Yuichi Yoshimura, Tsuyoshi Konuma, Young-Ho Lee, Kenji Sugase, Takahisa Ikegami, Hironobu Naiki, Yuji Goto. The Monomer-Seed Interaction Mechanism in the Formation of the beta 2-Microglobulin Amyloid Fibril Clarified by Solution NMR Techniques. JOURNAL OF MOLECULAR BIOLOGY. 2012. 422. 3. 390-402
- Yuichi Yoshimura, Yuxi Lin, Hisashi Yagi, Young-Ho Lee, Hiroki Kitayama, Kazumasa Sakurai, Masatomo So, Hirotsugu Ogi, Hironobu Naiki, Yuji Goto. Distinguishing crystal-like amyloid fibrils and glass-like amorphous aggregates from their kinetics of formation. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2012. 109. 36. 14446-14451
- Mototaka Suzuki, Kazumasa Sakurai, Young-Ho Lee, Takahisa Ikegami, Keiichi Yokoyama, Yuji Goto. A Back Hydrogen Exchange Procedure via the Acid-Unfolded State for a Large Protein. BIOCHEMISTRY. 2012. 51. 28. 5564-5570
- Young-Ho Lee, Takahisa Ikegami, Daron M. Standley, Kazumasa Sakurai, Toshiharu Hase, Yuji Goto. Binding Energetics of Ferredoxin-NADP(+) Reductase with Ferredoxin and Its Relation to Function. CHEMBIOCHEM. 2011. 12. 13. 2062-2070
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