{"id":857,"date":"2018-01-26T17:16:12","date_gmt":"2018-01-26T08:16:12","guid":{"rendered":"https:\/\/wp.bs-lab.ks.service.cloud.teu.ac.jp\/?page_id=857"},"modified":"2026-03-11T17:23:48","modified_gmt":"2026-03-11T08:23:48","slug":"publications","status":"publish","type":"page","link":"https:\/\/yoshida-lab.bs.teu.ac.jp\/?page_id=857&lang=en","title":{"rendered":"Publications"},"content":{"rendered":"\n

Research Articles<\/strong><\/h2>\n\n\n\n

[2025]<\/strong><\/strong><\/h3>\n\n\n\n

[66] Shoji Y.#, Ikeda Y.#, Rin R., Doi K., Tanaka M., Yoshida W.*<\/u>
Global DNA methylation level sensing using methyl-CpG binding domain-fused luciferase and fluorescent protein<\/a>
Sens. Actuators B Chem.<\/strong><\/strong> (2025) 438, 137797 (#Co-first authors, *Corresponding author)<\/p>\n\n\n\n

[65] Moriya M.#, Oyama T.#, Goto M., Ikebukuro K., Yoshida W.*<\/u>
Protocol for circular dichroism spectral\u00a0analysis\u00a0of\u00a0the\u00a0thermal stability of\u00a0CpG-methylated\u00a0quadruplex structures<\/a>
STAR Protoc.<\/strong> (2025) 6, 103646 (#Co-first authors, *Corresponding author)<\/p>\n\n\n\n

[2024]<\/strong><\/h3>\n\n\n\n

[64] Tanaka M., Kiriki Y., Kiyohara N., Hayashi M., Tamang A., Nakamura T., Vacha M., Choi Y., Choi J., Yoshida W.<\/u>, Critchley K., Evans S.D., Okochi M.
Small Au nanoparticles synthesized by peptide-based biomineralization for catalytic applications<\/a>
ACS Appl. Nano Mater.<\/strong> (2024) 7, 11258-11266<\/p>\n\n\n\n

[2023]<\/strong><\/h3>\n\n\n\n

[63] Fujita M.#, Goto M.#, Tanaka M., Yoshida W.*
<\/u>Detection of CpG methylation level using methyl-CpG-binding domain-fused fluorescent protein<\/a>
Anal. Methods<\/strong> (2023) 15, 2294-2299 (#Co-first authors, *Corresponding author) (Selected as a front cover<\/a>)<\/strong><\/p>\n\n\n\n

[62] Goto A., Yoshida W.*
<\/u>Hybridization-based CpG methylation level detection using methyl-CpG-binding domain\u2013fused luciferase<\/a>
Anal. Bioanal. Chem.<\/strong> (2023) 415, 2329 (*Corresponding author)
free access to the view-only version<\/a><\/p>\n\n\n\n

[61] Miyata T., Shimamura H., Asano R., Yoshida W.*
<\/u>Universal design of luciferase fusion proteins for epigenetic modifications detection based on bioluminescence resonance energy transfer<\/a>
Anal. Chem.<\/strong> (2023) 95, 3799 (*Corresponding author) (Selected as ACS Editors’ Choice<\/a>)<\/strong><\/p>\n\n\n\n

[2022]<\/strong><\/h3>\n\n\n\n

[60] Goto M., Baba Y., Yoshida W.*
<\/u>Quantitative detection of CpG methylation level on G-quadruplex and i-motif-forming DNA by recombinase polymerase amplification<\/a>
Anal. Bioanal. Chem.<\/strong> (2022) 414, 6223 (*Corresponding author)
free access to the view-only version<\/a><\/p>\n\n\n\n

[59] Taka N., Asami S., Sakamoto M., Matsui T., Yoshida W.*<\/u>
Quantification of global DNA hydroxymethylation level using UHRF2 SRA-luciferase based on bioluminescence resonance energy transfer<\/a>
Anal. Chem.<\/strong> (2022) 94, 8618 (*Corresponding author) (highlighted as the supplementary cover<\/a>)<\/strong><\/p>\n\n\n\n

[58] Iwasaki Y., Ookuro Y., Iida K., Nagasawa K., Yoshida W.*
<\/u>Destabilization of DNA and RNA G-quadruplex structures formed by GGA repeat due to N<\/em>6<\/sup>-methyladenine modification<\/a>
Biochem. Biophys. Res. Commun.<\/strong> (2022) 597, 134 (*Corresponding author)<\/p>\n\n\n\n

[57] Kimura K., Oshikawa D., Ikebukuro K.*, Yoshida W.*
<\/u>Stabilization of VEGF<\/em> i-motif structure by CpG methylation<\/a>
Biochem. Biophys. Res. Commun.<\/strong> (2022) 594, 88 (*Co-corresponding authors)<\/p>\n\n\n\n

[2021]<\/strong><\/h3>\n\n\n\n

[56] Laddachote S.#, Ishii R.#, Yoshida W.*<\/u>
Effects of CpG methylation on the thermal stability of c-kit<\/em>2, c-kit<\/em>*, and c-kit<\/em>1 G-quadruplex structures<\/a>
BBA Advances<\/strong> (2021) 1, 100007 (#Co-first authors, *Corresponding author)<\/p>\n\n\n\n

[55] Wada R., Yoshida W.*<\/u>,
Thermal stability changes in telomeric G-quadruplex structures due to N6<\/sup>-methyladenine modification<\/a>
Epigenomes<\/strong> (2021) 5, 5 (*Corresponding author) (Selected as<\/strong> a cover picture<\/a>, and Editor\u2019s Choice Articles<\/a><\/strong>)<\/strong><\/strong><\/p>\n\n\n\n

[2020]<\/strong><\/h3>\n\n\n\n

[54] Taka N., Yoshida W.*<\/u>,
Quantification of global DNA methylation level using 5-methylcytosine dioxygenase<\/a>
Anal. Bioanal. Chem.<\/strong> (2020) 412, 5299 (*Corresponding author)
free access to the view-only version<\/a><\/p>\n\n\n\n

[53] Laddachote S., Nagata M., Yoshida W.*<\/u>
Destabilisation of the c-kit<\/em>1 G-quadruplex structure by N6<\/sup>-methyladenosine modification<\/a>
Biochem. Biophys. Res. Commun.<\/strong> (2020) 524, 472 (*Corresponding author)<\/p>\n\n\n\n

[2019]<\/strong><\/h3>\n\n\n\n

[52] Islam I., Baba Y., Witarto A.B., Yoshida W.*<\/u>
G-quadruplex\u2013forming GGA repeat region functions as a negative regulator of the Ccnb1ip1<\/em> enhancer<\/a>
Biosci. Biotechnol. Biochem.<\/strong> (2019) 83, 1697 (*Corresponding author)<\/p>\n\n\n\n

[51] Baba Y., Yamamoto K., Yoshida W.*<\/u>
Multicolor bioluminescence resonance energy transfer assay for quantification of global DNA methylation<\/a>
Anal. Bioanal. Chem.<\/strong> (2019) 411, 4765 (*Corresponding author)
Biosketch (published in Anal. Bioanal. Chem.)<\/a>
free access to the view-only version<\/a><\/p>\n\n\n\n

[50] Taka N., Karube I., Yoshida W.*<\/u>
Direct detection of hemi-methylated DNA by SRA-fused luciferase based on bioluminescence resonance energy transfer<\/a>
Anal. Lett.<\/strong> (2019) 8, 1258 (*Corresponding author)<\/p>\n\n\n\n

[49] Iida K., Tsushima Y., Ma Y., Sedghi Masoud S., Sakuma M., Yokoyama T., Yoshida W.<\/u>, Ikebukuro K., Nagasawa K.
Model studies for isolation of G-quadruplex-forming DNA sequences through a pull-down strategy with macrocyclic polyoxazole<\/a>
Bioorg. Med. Chem.<\/strong> (2019) 27, 1742<\/p>\n\n\n\n

[48] Baba Y., Karube I., Yoshida W.*<\/u>
Global DNA methylation level monitoring by methyl-CpG binding domain-fused luciferase<\/a>
Anal. Lett.<\/strong> (2019) 52, 754 (*Corresponding author)<\/p>\n\n\n\n

[2018]<\/strong><\/h3>\n\n\n\n

[47] Tsukakoshi K.#, Yoshida W.#<\/u>, Kobayashi M., Kobayashi N., Kim J., Kaku T., Iguchi T., Nagasawa K., Asano R., Ikebukuro K., Sode K.
Esterification of PQQ enhances blood-brain barrier permeability and inhibitory activity against amyloidogenic protein fibril formation<\/a>
ACS Chem. Neurosci.<\/strong> (2018) 9, 2898 (#Co-first authors)<\/p>\n\n\n\n

[46] Yoshida W.*<\/u>, Terasaka M., Laddachote S., Karube I.
Stabilization of G-quadruplex structure on vascular endothelial growth factor gene promoter depends on CpG methylation site and cation type<\/a>
BBA General Subjects<\/strong> (2018) 1862, 1933 (*Corresponding author)<\/p>\n\n\n\n

[45] Tsukakoshi K.#, Saito S.#, Yoshida W.<\/u>#<\/u>, Goto S., Ikebukuro K.
CpG methylation changes G-quadruplex structures derived from gene promoters and interaction with VEGF and SP1<\/a>
Molecules<\/strong> (2018) 23, 944 (#Co-first authors)<\/p>\n\n\n\n

[44] Yoshida W.*<\/u>, Saikyo H., Nakabayashi K., Yoshioka H., Bay D.H., Iida K., Kawai T., Hata K., Ikebukuro K., Nagasawa K., Karube I.
Identification of G-quadruplex clusters by high-throughput sequencing of whole-genome amplified products with a G-quadruplex ligand<\/a>
Scientific Reports <\/strong>(2018) 8, 3116 (*Corresponding author)<\/p>\n\n\n\n

[2017]<\/strong><\/h3>\n\n\n\n

[43] Yoshida W.*<\/u>, Baba Y., Banzawa K., Karube I.
A quantitative homogeneous assay for global DNA methylation levels using CpG-binding domain- and methyl-CpG-binding domain-fused luciferase<\/a>
Anal. Chim. Acta<\/strong> (2017) 990, 168 (*Corresponding author)<\/p>\n\n\n\n

[42] Bay D.H.#, Busch A.#, Lisdat F., Iida K., Ikebukuro K., Nagasawa K., Karube I., Yoshida W.*<\/u>
Identification of G-quadruplex structures that possess transcriptional regulating functions in the Dele and Cdc6 CpG islands<\/a>
BMC Molecular Biology<\/strong> (2017) 18, 17 (#Co-first authors, *Corresponding author)<\/p>\n\n\n\n

[41] Yokoyama T., Tsukakoshi K., Yoshida W.<\/u>, Saito T., Teramoto K., Savory N., Abe K. Ikebukuro K.
Development of HGF-binding aptamers with the combination of G4 promoter-derived aptamer selection and in silico maturation<\/a>
Biotechnol. Bioeng.<\/strong> (2017) 114, 2196<\/p>\n\n\n\n

[40] Lee J., Yoshida W.<\/u>, Abe K., Nakabayashi K., Wakeda H., Hata K., Marquette C.A., Blum L.J., Sode K., Ikebukuro K.
Development of an electrochemical detection system for measuring DNA methylation levels using methyl CpG-binding protein and glucose dehydrogenase-fused zinc finger protein<\/a>
Biosens. Bioelectron.<\/strong> (2017) 93, 118<\/p>\n\n\n\n

[2016]<\/strong><\/h3>\n\n\n\n

[39] Tsukakoshi K., Ikuta Y., Abe K., Yoshida W.<\/u>, Iida K., Ma Y., Nagasawa K., Sode K. Ikebukuro K.
Structural regulation by a G-quadruplex ligand increases binding abilities of G-quadruplex-forming aptamers<\/a>
Chem. Commun. <\/strong>(2016) 52, 12646<\/p>\n\n\n\n

[38] Yoshida W.*<\/u>, Baba Y., Karube I.
Global DNA methylation detection system using MBD-fused luciferase based on bioluminescence resonance energy transfer assay<\/a>
Anal. Chem.<\/strong> (2016) 88, 9264 (*Corresponding author)<\/p>\n\n\n\n

[37] Yoshida W.*<\/u>, Yoshioka H., Bay D.H., Iida K., Ikebukuro K., Nagasawa K., Karube I.
Detection of DNA methylation of G-quadruplex and i-motif-forming sequences by measuring the initial elongation efficiency of polymerase chain reaction<\/a>
Anal. Chem.<\/strong> (2016) 88, 7101 (*Corresponding author)<\/p>\n\n\n\n

[36] Matsumoto D., Nishio M., Kato Y., Yoshida W., <\/u>Abe K., Fukazawa K., Ishihara K., Iwata F., Ikebukuro K., Nakamura C.
ATP-mediated Release of a DNA-binding Protein from a Silicon Nanoneedle Array<\/a>
Electrochemistry<\/strong> (2016) 84, 305<\/p>\n\n\n\n

[2015]<\/strong><\/h3>\n\n\n\n

[35] Saito T.#, Yoshida W.#<\/u>, Yokoyama T., Abe K., Ikebukuro K.
Identification of RNA oligonucleotides binding to several proteins from potential G-quadruplex forming regions in transcribed pre-mRNA<\/a>
Molecules<\/strong> (2015) 20, 20832 (#Co-first authors)<\/p>\n\n\n\n

[34] Fukaya T., Abe K., Savory N., Tsukakoshi K., Yoshida W.<\/u>, Ferri S., Sode K., Ikebukuro K.
Improvement of the VEGF binding ability of DNA aptamers through in silico maturation and multimerization strategy<\/a>
J. Biotechnol.<\/strong> (2015) 212, 99<\/p>\n\n\n\n

[33] Ogihara K., Savory N., Abe K., Yoshida W.<\/u>, Arakawa M., Asahi M., Kamohara S., Ikebukuro K.
Inhibition of an allergen\u2013antibody reaction related to Japanese cedar pollinosis using DNA aptamers against the Cry j 2 allergen<\/a>
Nucleic Acid Ther.<\/strong> (2015) 25, 311<\/p>\n\n\n\n

[32] Yoshida W.*<\/u>, Tomikawa J., Inaki M., Kimura H., Onodera M., Hata K., Nakabayashi K.*
An insulator element located at the cyclin B1 interacting protein 1 gene locus is highly conserved among mammalian species<\/a>
PLOS ONE<\/strong> (2015) 10, e0131204 (*Corresponding authors)<\/p>\n\n\n\n

[31] Ogihara K., Savory N., Abe K., Yoshida W.<\/u>, Asahi M., Kamohara S., Ikebukuro K.
DNA aptamers against the Cry j 2 allergen of Japanese cedar pollen for biosensing applications<\/a>
Biosens. Bioelectron.<\/strong> (2015) 63, 159<\/p>\n\n\n\n

[2014]<\/strong><\/h3>\n\n\n\n

[30] Savory N., Nzakizwanayo J., Abe K., Yoshida W.<\/u>, Ferri S., Dedi C., Jones B.V., Ikebukuro K.
Selection of DNA aptamers against uropathogenic Escherichia coli NSM59 by quantitative PCR controlled Cell-SELEX<\/a>
J. Microbiol. Methods<\/strong> (2014) 104, 94<\/p>\n\n\n\n

[29] Lee J., Tatsumi A., Abe K., Yoshida W.<\/u>, Sode K., Ikebukuro K.
Electrochemical detection of pathogenic bacteria by using a glucose dehydrogenase fused zinc finger protein<\/a>
Anal. Methods <\/strong>(2014) 6, 4991<\/p>\n\n\n\n

[28] Miyake K., Abe K., Ferri S., Nakajima M., Nakamura M., Yoshida W.<\/u>, Kojima K., Ikebukuro K. Sode K.
A green-light-inducible lytic system for cyanobacterial cells<\/a>
Biotechnology for Biofuels<\/strong> (2014) 7, 56<\/p>\n\n\n\n

[27] Sakai Y., Abe K., Nakashima S., Yoshida W.<\/u>, Ferri S., Sode K., Ikebukuro K.
Improving gene regulation ability of small RNAs by scaffold engineering in Escherichia coli<\/a>
ACS Synthetic Biology<\/strong> (2014) 3, 152<\/p>\n\n\n\n

[26] Abe K., Sakai Y., Nakashima S., Araki M., Yoshida W.<\/u>, Sode K., Ikebukuro K.
Design of riboregulators for control of cyanobacterial (Synechocystis) protein expression<\/a>
Biotechnol. Lett. <\/strong>(2014) 36, 287<\/p>\n\n\n\n

[25] Savory N., Takahashi Y., Tsukakoshi K., Hasegawa H., Takase M., Abe K., Yoshida W.<\/u>, Ferri S., Kumazawa S., Sode K., Ikebukuro K.
Simultaneous improvement of specificity and affinity of aptamers against Streptococcus mutans by in silico maturation for biosensor development<\/a>
Biotechnol. Bioeng.<\/strong> (2014) 111, 454<\/p>\n\n\n\n

[2013]<\/strong><\/h3>\n\n\n\n

[24] Abe K., Yoshida W.<\/u>, Terada K., Yagi-Ishii Y., Ferri S., Ikebukuro K., Sode K.
Screening of peptide ligands for pyrroloquinoline quinone glucose dehydrogenase using antagonistic template-based biopanning<\/a>
Int. J. Mol. Sci.<\/strong> (2013) 14, 23244<\/p>\n\n\n\n

[23] Iida K.#, Nakamura T.#, Yoshida W.#<\/u>, Tera M., Nakabayashi K., Hata K., Ikebukuro K. Nagasawa K.
Fluorescent ligand-mediated screening of G-quadruplex structure using a DNA microarray<\/a>
Angew. Chem. Int. Ed. Engl.<\/strong> (2013) 52, 12052 (#Co-first authors) (highlighted as an inside cover picture<\/a>)<\/strong><\/p>\n\n\n\n

[22] Yoshida W.<\/u>, Kezuka A., Murakami Y., Lee J., Abe K., Motoki H., Matsuo T., Shimura N., Noda M., Igimi S., Ikebukuro K.
Automatic polymerase chain reaction product detection system for food safety monitoring using zinc finger protein fused to luciferase<\/a>
Anal. Chim. Acta<\/strong> (2013) 801, 78<\/p>\n\n\n\n

[21] Savory N., Goto S., Yoshida W.<\/u>, Unuma Y., Nakamura M., Abe K., Ferri S., Ikebukuro K.
Two-dimensional electrophoresis based selection for aptamers against unidentified protein in tissue sample<\/a>
Anal. Lett.<\/strong> (2013) 46, 2954<\/p>\n\n\n\n

[20] Yoshida W.<\/u>, Kezuka A., Abe K., Wakeda H., Nakabayashi K., Hata K., Ikebukuro K.
Detection of histone modification by chromatin immunoprecipitation combined zinc finger luciferase-based bioluminescence resonance energy transfer assa<\/a>
Anal. Chem.<\/strong> (2013) 85, 6485<\/p>\n\n\n\n

[19] Yoshida W.<\/u>, Saito T., Yokoyama T., Ferri S., Ikebukuro K.
Aptamer selection based on G4-forming promoter region<\/a>
PLOSONE<\/strong> (2013) 8, e65497<\/p>\n\n\n\n

[18] Savory N., Lednor D., Tsukakoshi K., Abe K., Yoshida W.<\/u>, Ferri S., Jones B.V., Ikebukuro K.
In silico maturation of binding-specificity of DNA aptamers against Proteus mirabilis<\/a>
Biotechnol. Bioeng.<\/strong> (2013) 110, 2573<\/p>\n\n\n\n

[17] Yoshida W.<\/u>, Kobayashi N., Sasaki Y., Ikebukuro K., Sode K.
Partial peptide of \u03b1-synuclein modified with small-molecule inhibitors specifically inhibits amyloid fibrillation of \u03b1-synuclein<\/a>
Int. J. Mol. Sci.<\/strong> (2013) 14, 2590<\/p>\n\n\n\n

[16] Nonaka Y., Yoshida W.,<\/u> Abe K., Ferri S., Schulze H., Bachmann T., Ikebukuro K.
Affinity improvement of a VEGF aptamer by in silico maturation for a sensitive VEGF-detection system<\/a>
Anal. Chem.<\/strong> (2013) 85, 1132<\/p>\n\n\n\n

[15] Kim J., Sasaki Y., Yoshida W.<\/u>, Kobayashi N., Veloso A.J., Kerman K., Ikebukuro K., Sode K.
Rapid cytotoxicity screening platform for amyloid inhibitors using a membrane-potential sensitive fluorescent probe<\/a>
Anal. Chem.<\/strong> (2013) 85, 185<\/p>\n\n\n\n

[14] Yoshida W.<\/u>, Yamamoto H., Ikebukuro K.
An optical biosensing system based on interference-enhanced reflection with aptameric enzyme subunits of thrombin<\/a>
Anal. Lett.<\/strong> (2013) 46, 242<\/p>\n\n\n\n

[2012]<\/strong><\/h3>\n\n\n\n

[13] Hiraoka D.#, Yoshida W.#<\/u>, Abe K., Wakeda H., Hata K., Ikebukuro K.
Development of a method to measure DNA methylation levels by using methyl CpG-binding protein and luciferase-fused zinc finger protein<\/a>
Anal. Chem.<\/strong> (2012) 84, 8259 (#Co-first authors)<\/p>\n\n\n\n

[2011]<\/strong><\/h3>\n\n\n\n

[12] Morita Y.#, Yoshida W.#<\/u>, Savory N., Han S., Tera M., Nagasawa K., Nakamura C., Sode K., Ikebukuro K.
Development of a novel biosensing system based on the structural change of a polymerized guanine-quadruplex DNA nanostructure<\/a>
Biosens. Bioelectron.<\/strong> (2011) 26, 4837 (#Co-first authors)<\/p>\n\n\n\n

[11] Nakabayashi K., Trujillo A.M., Tayama C., Camprubi C., Yoshida W.<\/u>, Lapunzina P., Sanchez A., Soejima H., Aburatani H., Nagae G., Ogata T., Hata K., Monk D.
Methylation screening of reciprocal genome-wide UPDs identifies novel human specific imprinted genes<\/a>
Hum. Mol. Genet.<\/strong> (2011) 20, 3188<\/p>\n\n\n\n

[10] Sato S., Yoshida W.<\/u>, Soejima H., Nakabayashi K., Hata K.
Methylation dynamics of IG-DMR and Gtl2-DMR during murine embryonic and placental development<\/a>
Genomics<\/strong> (2011) 98, 120<\/p>\n\n\n\n

 <\/strong>[9] Abe K., Ogasawara D., Yoshida W.<\/u>, Sode K., Ikebukuro K.
Aptameric sensors based on structural change for diagnosis<\/a>
Faraday Discuss.<\/strong> (2011) 149, 93<\/p>\n\n\n\n

[2009]<\/strong><\/h3>\n\n\n\n

[8] Fukasawa M., Yoshida W.<\/u>, Yamazaki H., Sode K., Ikebukuro K.
An aptamer-based bound\/free separation system for protein detection<\/a>
Electroanalysis<\/strong> (2009) 21, 1297<\/p>\n\n\n\n

[7] Yoshida <\/u>W., Mochizuki E., Takase M., Hasegawa H., Morita Y., Yamazaki H., Sode K., Ikebukuro K.
Selection of DNA aptamers against insulin and construction of an aptameric enzyme subunit for insulin sensing<\/a>
Biosens. Bioelectron.<\/strong> (2009) 24, 1116<\/p>\n\n\n\n

[2008]<\/strong><\/h3>\n\n\n\n

[6] Yoshida W.<\/u>, Sode K., Ikebukuro K.
Label-free homogeneous detection of immunoglobulin E by an aptameric enzyme subunit<\/a>
Biotechnol. Lett.<\/strong> (2008) 30, 421<\/p>\n\n\n\n

[5] Ikebukuro K.#, Yoshida W.#<\/u>, Sode K.
Aptameric enzyme subunit for homogeneous DNA sensing<\/a>
Biotechnol. Lett.<\/strong> (2008) 30, 243 (#Co-first authors)<\/p>\n\n\n\n

[2007]<\/strong><\/h3>\n\n\n\n

[4] Yoshida W.<\/u>, Yokobayashi Y.
Photonic Boolean logic gates based on DNA aptamers<\/a>
Chem. Commun.<\/strong> (2007) 195 (highlighted by Nature Nanotechnology, 2006, 1, 160<\/a>)<\/strong><\/p>\n\n\n\n

[2006]<\/strong><\/h3>\n\n\n\n

[3] Ikebukuro K., Yoshida W.<\/u>, Noma T., Sode K.
Analysis of the evolution of the thrombin-inhibiting DNA aptamers using a genetic algorithm<\/a>
Biotechnol. Lett.<\/strong> (2006) 28, 1933<\/p>\n\n\n\n

[2] Yoshida W.<\/u>, Sode K., Ikebukuro K.
Homogeneous DNA sensing using enzyme-inhibiting DNA aptamers<\/a>
Biochem. Biophys. Res. Commun.<\/strong> (2006) 348, 245<\/p>\n\n\n\n

[1] Yoshida W.<\/u>, Sode K., Ikebukuro K.
Aptameric enzyme subunit for biosensing based on enzymatic activity measurement<\/a>
Anal. Chem.<\/strong> (2006) 78, 3296<\/p>\n\n\n\n

Review Articles<\/strong><\/h2>\n\n\n\n

[2] Kumagai T., Abe K., Yoshida W<\/u>., Ikebukuro K.
DNA detection technology using zinc finger protein<\/a>
Journal of Microbial & Biochemical Technology<\/strong> (2015) 7, 278<\/p>\n\n\n\n

[1] Yoshida W.,<\/u> Abe K., Ikebukuro K.,
Emerging techniques employed in aptamer-based diagnostic tests<\/a>
Expert Rev. Mol. Diagn.<\/strong> (2014) 14, 143<\/p>\n\n\n\n

Book Chapters<\/strong><\/h2>\n\n\n\n

[7] Taka N., Baba Y., Iwasaki Y., Yoshida W.
<\/u>Bioluminescence resonance energy transfer for global DNA methylation quantification<\/a>
Bioluminescence. Methods in Molecular Biology<\/strong> (2022) 2525, 267<\/p>\n\n\n\n

[6] Taka N., Yoshida W.<\/u>
Global DNA methylation analysis using methylcytosine dioxygenase<\/a>
DNA modification detection Methods (Springer Protocols Handbooks)<\/strong> (2021) 93<\/p>\n\n\n\n

[5] Nakanishi A., Yoshida W.<\/u>, Karube I.
Organic Matter BOD Biosensor Monitoring<\/a>
Handbook of Cell Biosensors<\/strong> (2019)<\/p>\n\n\n\n

[4] Yoshida W.<\/u>, Karube I.
Determination of lactates<\/a>
Flow Injection Analysis of Food Additives<\/strong> (2015) 273<\/p>\n\n\n\n

[3] Savory N., Abe K., Yoshida W.<\/u>, Ikebukuro K.
In silico maturation: processing sequences to improve biopolymer functions based on genetic algorithms<\/a>
Applications of Metaheuristics in Process Engineering<\/strong> (2014) 271<\/p>\n\n\n\n

[2] Abe K., Yoshida W.<\/u>, Ikebukuro K
Electrochemical biosensors using aptamers for theranostics<\/a>
Advances in Biochemical Engineering \/ Biotechnology<\/strong> (2014) 183<\/p>\n\n\n\n

[1] Ikebukuro K., Yoshida W.<\/u>, Sode K.
Biosensors using the aptameric enzyme subunit: The use of aptamers in the allosteric control of enzymes<\/a>
Aptamers in Bioanalysis<\/strong> (2009) 129<\/p>\n","protected":false},"excerpt":{"rendered":"

Research Articles [2025] [66] Shoji Y.#, Ikeda Y.#, Rin R., Doi K., Tanaka M., Yoshida W.*Global DNA methylati […]<\/p>\n","protected":false},"author":2,"featured_media":0,"parent":0,"menu_order":2,"comment_status":"closed","ping_status":"closed","template":"","meta":{"sns_share_botton_hide":"","vkExUnit_sns_title":"","_vk_print_noindex":"","sitemap_hide":"","vkExUnit_sitemap":"","vkExUnit_EyeCatch_disable":"","_veu_custom_css":"","veu_display_promotion_alert":"common","_exclude_from_list_pages":"","vkexunit_cta_each_option":"","vkExUnit_childPageIndex":"","vkExUnit_pageList_ancestor":"","vkExUnit_contact_enable":"","twitterCardType":"summary","cardImageID":0,"cardImage":"","cardTitle":"","cardDesc":"","cardImageAlt":"","cardPlayer":"","cardPlayerWidth":0,"cardPlayerHeight":0,"cardPlayerStream":"","cardPlayerCodec":"","_lightning_design_setting":{"layout":"default"},"footnotes":""},"categories":[],"tags":[],"class_list":["post-857","page","type-page","status-publish","hentry"],"veu_head_title_object":{"title":"","add_site_title":""},"_links":{"self":[{"href":"https:\/\/yoshida-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/pages\/857","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/yoshida-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/yoshida-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/yoshida-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"https:\/\/yoshida-lab.bs.teu.ac.jp\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=857"}],"version-history":[{"count":81,"href":"https:\/\/yoshida-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/pages\/857\/revisions"}],"predecessor-version":[{"id":3565,"href":"https:\/\/yoshida-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/pages\/857\/revisions\/3565"}],"wp:attachment":[{"href":"https:\/\/yoshida-lab.bs.teu.ac.jp\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=857"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/yoshida-lab.bs.teu.ac.jp\/index.php?rest_route=%2Fwp%2Fv2%2Fcategories&post=857"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/yoshida-lab.bs.teu.ac.jp\/index.php?rest_route=%2Fwp%2Fv2%2Ftags&post=857"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}