Faculty Profiles - HIROAKI Hidekazu

Papers - HIROAKI Hidekazu

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Synthesis of selenomethylene-locked nucleic acids (SeLNA) nucleoside unit bearing an adenine base Reviewed International journal

Moai, Y; Hiroaki, H; Obika, S; Kodama, T

NUCLEOSIDES NUCLEOTIDES & NUCLEIC ACIDS Vol. 39 ( 1-3 ) page： 131 - 140 2020.2

Discovery of Cryoprotective Activity in Human Genome-Derived Intrinsically Disordered Proteins.

Matsuo N, Goda N, Shimizu K, Fukuchi S, Ota M, Hiroaki H

International journal of molecular sciences Vol. 19 ( 2 ) 2018.2

Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis. Reviewed

Shigemitsu Y, Hiroaki H

Journal of biochemistry Vol. 163 ( 1 ) page： 11-18 2018.1

Ecl1 is a zinc-binding protein involved in the zinc-limitation-dependent extension of chronological life span in fission yeast. Reviewed

Shimasaki T, Ohtsuka H, Naito C, Azuma K, Tenno T, Hiroaki H, Murakami H, Aiba H

Molecular genetics and genomics : MGG Vol. 292 ( 2 ) page： 475-481 2017.4

Benzene-Glycol Nucleic Acid (BGNA)-DNA Chimeras: Synthesis, Binding Properties, and Ability to Elicit Human RNase H Activity. Reviewed

Niwa, N., Shimizu, S., Maeda, Y., Hiroaki, H., Ueno, Y.

Vol. 7 page： 25378-25386 2017.1

Nuclear magnetic resonance evidence for the dimer formation of beta amyloid peptide 1-42 in 1,1,1,3,3,3-hexafluoro-2-propanol. Reviewed

Shigemitsu Y, Iwaya N, Goda N, Matsuzaki M, Tenno T, Narita A, Hoshi M, Hiroaki H

Analytical biochemistry Vol. 498 page： 59-67 2016.4

Na, K-ATPase α3 is a death target of Alzheimer patient amyloid-β assembly. Reviewed

Vol. 112 ( 32 ) page： E4465-74 2015.8

用語解説「天然変性蛋白質」 Invited

廣明秀一

再生医療（日本再生医療学会雑誌） Vol. 14 ( 3 ) page： 52-53 2015.8

A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR. Reviewed

Goda N, Shimizu K, Kuwahara Y, Tenno T, Noguchi T, Ikegami T, Ota M, Hiroaki H

International journal of molecular sciences Vol. 16 ( 7 ) page： 15743-60 2015.7

Crystal structure of afadin PDZ domain-nectin-3 complex shows the structural plasticity of the ligand-binding site. Reviewed

Fujiwara Y, Goda N, Tamashiro T, Narita H, Satomura K, Tenno T, Nakagawa A, Oda M, Suzuki M, Sakisaka T, Takai Y, Hiroaki H

Protein science : a publication of the Protein Society Vol. 24 ( 3 ) page： 376-85 2015.3

An optimized Npro-based method for the expression and purification of intrinsically disordered proteins for an NMR study Reviewed

Natsuko Goda, Naoki Matsuo, Takeshi Tenno, Sonoko Ishino, Yoshizumi Ishino, Satoshi Fukuchi, Motonori Ota & Hidekazu Hiroaki*

ntrinsically Disordered Proteins Vol. 3 ( 1 ) page： 1-6 2015.2

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal)

Intrinsically disordered proteins (IDPs) are an emerging concept. IDPs have high flexibility in their polypeptide chains, lacking a stable 3-dimensional structure. Because of the difficulty in performing X-ray crystallography for IDPs, nuclear magnetic resonance (NMR) spectroscopy is the first choice for atomic-level investigation of their nature. Given that isotopically labeled IDP samples are necessary for NMR study, a robust and cost-effective protocol for bacterial expression and purification of IDP is also needed. We employed the Npro (EDDIE)-autoprotease fusion protein system. Although IDPs are believed to be readily degraded by endogenous proteases when expressed in Escherichia coli, Npro-fused IDPs showed excellent resistance to degradation. Seven IDPs of uncharacterized function sampled from the human genome as well as 3 constructs from IDP regions derived from human FancM and Thermococcus kodakarensis Hef were prepared. We improved the protocol of refolding of Npro (EDDIE) to use dialysis, which is convenient for subsequent purification using reversed-phase (RP) HPLC. The method is robust and widely applicable to any IDP sample, promoting the acquisition of experimental data for IDPs in a high-throughput manner.

DOI： 10.1080/21690707.2015.1011004

Decreased amyloidogenicity caused by mutational modulation of surface properties of the immunoglobulin light chain BRE variable domain. Reviewed

Kobayashi Y, Tsutsumi H, Abe T, Ikeda K, Tashiro Y, Unzai S, Kamikubo H, Kataoka M, Hiroaki H, Hamada D.

Biochemistry Vol. 53 ( 31 ) page： 5162-5173 2014.8

Multiple interactions of the intrinsically disordered region between the helicase and nuclease domains of the archaeal Hef protein. Reviewed

Ishino S, Yamagami T, Kitamura M, Kodera N, Mori T, Sugiyama S, Ando T, Goda N, Tenno T, Hiroaki H, Ishino Y.

J Biol Chem. Vol. 289 ( 31 ) page： 21627-21639 2014.8

IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners. Reviewed

Fukuchi S, Amemiya T, Sakamoto S, Nobe Y, Hosoda K, Kado Y, Murakami SD, Koike R, Hiroaki H, Ota M.

Nucleic Acids Res. Vol. 42 ( Database issue ) page： D320-325 2014.1

特集「タンパク質構造機能相関再考」~ NMRで見るタンパク質－低分子相互作用 (2013) Invited

廣明秀一

生化学 Vol. 85 ( 8 ) page： 679-686 2013.8

Accidental Interaction between PDZ Domains and Diclofenac Revealed by NMR-Assisted Virtual Screening. Reviewed

Tenno T, Goda N, Umetsu Y, Ota M, Kinoshita K, Hiroaki H.

Molecules Vol. 18 ( 8 ) page： 9567-9581 2013.8

Recent applications of isotopic labeling for protein NMR in drug discovery. Invited Reviewed

Hiroaki, H*

Expert Opinion on Drug Discovery Vol. 8 ( 5 ) page： 523-536 2013.3

Effect of Ca(2+) on the microtubule-severing enzyme p60-katanin. Insight into the substrate-dependent activation mechanism. Reviewed

Iwaya N, Akiyama K, Goda N, Tenno T, Fujiwara Y, Hamada D, Ikura T, Shirakawa M, Hiroaki H.

FEBS J. Vol. 279 ( 7 ) page： 1339-1352. 2012.3

IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature. Reviewed

Fukuchi S, Sakamoto S, Nobe Y, Murakami SD, Amemiya T, Hosoda K, Koike R, Hiroaki H, Ota M.

Nucleic Acids Res. Vol. 40 page： D507-511. 2011.11

A simplified recipe for assigning amide NMR signals using combinatorial 14N amino acid inverse-labeling. Reviewed

Hiroaki H, Umetsu Y, Nabeshima Y, Hoshi M, Kohda D.

J Struct Funct Genomics. Vol. 12 ( 3 ) page： 167-174 2011.8

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