The Residual Structure of Unfolded Proteins was Elucidated from the Standard Deviation of NMR Intensity Differences

Authors: Mizuno, Fuko, Aoki, Saeko, Matsugami, Akimasa, Hayashi, Fumiaki, Nishimura, Chiaki

Source: Protein & peptide letters. 30(2):103-107

Availability: http://explore.bl.uk/primo_library/libweb/action/display.do?tabs=detailsTab&gathStatTab=true&ct=display&fn=search&doc=ETOCvdc_100179646236.0x000001&indx=1&recIds=ETOCvdc_100179646236.0x000001

Changes in dynamic and static structures of the HIV‐1 p24 capsid protein N‐domain caused by amino‐acid substitution are associated with its viral viability

Authors: Sato, Yusuke, Matsugami, Akimasa, Watanabe, Satoru, Hayashi, Fumiaki, Arai, Munehito, Kigawa, Takanori, Nishimura, Chiaki

Source: Protein science. 30(11):2233-2245

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Distinct residual and disordered structures of alpha-synuclein analyzed by amide-proton exchange and NMR signal intensity

Authors: Okuwaki, Rina, Shinmura, Iori, Morita, Shiki, Matsugami, Akimasa, Hayashi, Fumiaki, Goto, Yuji, Nishimura, Chiaki

Source: In BBA - Proteins and Proteomics September 2020 1868(9)

Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding.

Authors: Nishimura, Chiaki¹ (AUTHOR) cnishimura@thu.ac.jp, Kikuchi, Takeshi² (AUTHOR) tkikuchi@sk.ritsumei.ac.jp

Source: Molecules. May2023, Vol. 28 Issue 9, p3970. 13p.

Subject Terms: *MYOGLOBIN, *PROTEIN folding, *PROTEINS, *EIGENFUNCTIONS, *GLOBIN, *HYDROPHOBIC surfaces

Enhanced Picture of Protein-Folding Intermediates Using Organic Solvents in H/D Exchange and Quench-Flow Experiments

Authors: Nishimura, Chiaki, Dyson, H. Jane, Wright, Peter E., Bax, Adriaan

Source: Proceedings of the National Academy of Sciences of the United States of America, 2005 Mar . 102(13), 4765-4770.

Access URL: https://www.jstor.org/stable/3375124

Comparison of residual alpha- and beta-structures between two intrinsically disordered proteins by using NMR

Authors: Ono, Yu-ichi, Miyashita, Manami, Ono, Yumi, Okazaki, Honoka, Watanabe, Satoru, Tochio, Naoya, Kigawa, Takanori, Nishimura, Chiaki

Source: In BBA - Proteins and Proteomics March 2015 1854(3):229-238

Non-Native α-Helices in the Initial Folding Intermediate Facilitate the Ordered Assembly of the β-Barrel in β-Lactoglobulin

Authors: Sakurai, Kazumasa, Yagi, Masanori, Konuma, Tsuyoshi, Takahashi, Satoshi, Nishimura, Chiaki, Goto, Yuji

Source: Biochemistry. 56(36):4799-4807

Availability: http://explore.bl.uk/primo_library/libweb/action/display.do?tabs=detailsTab&gathStatTab=true&ct=display&fn=search&doc=ETOCRN612937371&indx=1&recIds=ETOCRN612937371

Long-range effects of tag sequence on marginally stabilized structure in HIV-1 p24 capsid protein monitored using NMR

Authors: Okazaki, Honoka, Kaneko, Chie, Hirahara, Miyuki, Watanabe, Satoru, Tochio, Naoya, Kigawa, Takanori, Nishimura, Chiaki

Source: In BBA - Proteins and Proteomics September 2014 1844(9):1638-1647

Flexible and rigid structures in HIV-1 p17 matrix protein monitored by relaxation and amide proton exchange with NMR

Authors: Ohori, Yuka, Okazaki, Honoka, Watanabe, Satoru, Tochio, Naoya, Arai, Munehito, Kigawa, Takanori, Nishimura, Chiaki

Source: In BBA - Proteins and Proteomics March 2014 1844(3):520-526

Structure-Correlation NMR Spectroscopy for Macromolecules Using Repeated Bidirectional Photoisomerization of Azobenzene

Authors: Nagashima, Toshio, Ueda, Keisuke, Nishimura, Chiaki, Yamazaki, Toshio

Source: Analytical chemistry. 87(22):11544-11552

Availability: http://explore.bl.uk/primo_library/libweb/action/display.do?tabs=detailsTab&gathStatTab=true&ct=display&fn=search&doc=ETOCRN603853993&indx=1&recIds=ETOCRN603853993

Hierarchical Folding Mechanism of Apomyoglobin Revealed by Ultra-Fast H/D Exchange Coupled with 2D NMR

Authors: Uzawa, Takanori, Nishimura, Chiaki, Akiyama, Shuji, Ishimori, Koichiro, Takahashi, Satoshi, Dyson, H. Jane, Wright, Peter E.

Source: Proceedings of the National Academy of Sciences of the United States of America, 2008 Sep . 105(37), 13859-13864.

Access URL: https://www.jstor.org/stable/25464141

Consequences of Stabilizing the Natively Disordered F Helix for the Folding Pathway of Apomyoglobin

Authors: Nishimura, Chiaki, Dyson, H. Jane, Wright, Peter E.

Source: In Journal of Molecular Biology 5 August 2011 411(1):248-263

Serum adipokine profiles in Kawasaki disease

Authors: Kemmotsu, Yasushi, Saji, Tsutomu, Kusunoki, Natsuko, Tanaka, Nahoko, Nishimura, Chiaki, Ishiguro, Akira, Kawai, Shinichi

Source: Modern rheumatology. 22(1):66-72

Availability: http://explore.bl.uk/primo_library/libweb/action/display.do?tabs=detailsTab&gathStatTab=true&ct=display&fn=search&doc=ETOCvdc_100103751785.0x000001&indx=1&recIds=ETOCvdc_100103751785.0x000001

Energetic Frustration of Apomyoglobin Folding: Role of the B Helix

Authors: Nishimura, Chiaki, Dyson, H. Jane, Wright, Peter E.

Source: In Journal of Molecular Biology 12 March 2010 396(5):1319-1328

The Kinetic and Equilibrium Molten Globule Intermediates of Apoleghemoglobin Differ in Structure

Authors: Nishimura, Chiaki, Dyson, H. Jane, Wright, Peter E.

Source: In Journal of Molecular Biology 2008 378(3):715-725

Identification of Native and Non-native Structure in Kinetic Folding Intermediates of Apomyoglobin

Authors: Nishimura, Chiaki, Dyson, H.Jane, Wright, Peter E.

Source: In Journal of Molecular Biology 2006 355(1):139-156

Sequence Determinants of a Protein Folding Pathway

Authors: Nishimura, Chiaki, Lietzow, Michael A. ^†, Dyson, H. Jane, Wright, Peter E.

Source: In Journal of Molecular Biology 2005 351(2):383-392

Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway.

Authors: Cavagnero, Silvia, Nishimura, Chiaki, Schwarzinger, Stephan

Source: Biochemistry; December 4 2001, Vol. 40 Issue 48, p14459-14467, 9p

Effect of salts on the stability and folding of staphylococcal nuclease.

Authors: Nishimura, Chiaki, Uversky, Vladimir N., Fink, Anthony L.

Source: Biochemistry; February 20 2001, Vol. 40 Issue 7, p2113-2128, 16p

Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue.

Authors: Garcia, Carlos, Nishimura, Chiaki, Cavagnero, Silvia

Source: Biochemistry; September 19 2000, Vol. 39 Issue 37, p11227-11237, 11p