{"id":34,"date":"2015-06-30T07:50:34","date_gmt":"2015-06-30T07:50:34","guid":{"rendered":"http:\/\/cheme.eng.shizuoka.ac.jp\/wordpress\/ferri\/?page_id=34"},"modified":"2016-04-06T04:06:04","modified_gmt":"2016-04-06T04:06:04","slug":"publication","status":"publish","type":"page","link":"http:\/\/cheme.eng.shizuoka.ac.jp\/wordpress\/ferri\/publication\/","title":{"rendered":"Publications"},"content":{"rendered":"

List of Publications:<\/strong><\/p>\n

    \n
  1. Shiota M, Yamazaki T, Yoshimatsu K, Kojima K, Tsugawa W, Ferri S<\/u><\/strong>, Sode K (2016) An Fe-S cluster in the conserved Cys-rich region in the catalytic subunit of FAD-dependent dehydrogenase complexes. Bioelectrochemistry<\/em>. Feb 2. pii: S1567-5394(16)30010-X. doi: 10.1016\/j.bioelechem.2016.01.010. [Epub ahead of print]<\/li>\n
  2. Nakajima M, Abe K, Ferri S<\/u><\/strong>, Sode K (2016) Development of a light-regulated cell-recovery system for non-photosynthetic bacteria. Microb Cell Fact<\/em>. Feb 15;15(1):31.<\/li>\n
  3. Ferri S<\/u><\/strong>, Nakamura M, Ito A, Nakajima M, Abe K, Kojima K, Sode K (2015) Efficient surface-display of autotransporter proteins in cyanobacteria Algal Research<\/em> 12: 337\u2013340.<\/li>\n
  4. \u00a0Fukaya T, Abe K, Savory N, Tsukakoshi K, Yoshida W, Ferri S<\/u><\/strong>, Sode K, Ikebukuro K. (2015) Improvement of the VEGF binding ability of DNA aptamers through in silico maturation and multimerization strategy. J Biotechnol 212:99-105.<\/li>\n
  5. Sakai Y, Abe K, Nakashima S, Ellinger JJ, Ferri S<\/u><\/strong>, Sode K, Ikebukuro K. (2015) Scaffold-fused riboregulators for enhanced gene activation in Synechocystis sp. PCC 6803 Microbiologyopen 4(4):533-540.<\/li>\n
  6. Badary A, Abe K, Ferri S<\/u><\/strong>, Kojima K, Sode K (2015) The development and characterization of an exogenous green-light regulated gene expression system in marine cyanobacteria. Mar Biotechnol (NY)<\/em>. Jun;17(3):245-51.<\/li>\n
  7. Kameya M, Sakaguchi-Mikami A, Ferri S<\/u><\/strong>, Tsugawa W, Sode K (2015) Advancing the Development of Glycated Protein Biosensing Technology: Next-Generation Sensing Molecules. J Diabetes Sci Technol.<\/em> Mar;9(2):183-91.<\/li>\n
  8. Savory N, Nzakizwanayo J, Abe K, Yoshida W, Ferri S<\/u><\/strong>, Dedi C, Jones BV, Ikebukuro K (2014) Selection of DNA aptamers against uropathogenic Escherichia coli<\/em> NSM59 by quantitative PCR controlled Cell-SELEX. J Microbiol Methods<\/em>. Sep;104:94-100.<\/li>\n
  9. Sakai Y, Abe K, Nakashima S, Yoshida W, Ferri S<\/u><\/strong>, Sode K, Ikebukuro K. (2014) Improving the Gene-Regulation Ability of Small RNAs by Scaffold Engineering in Escherichia coli<\/em>. ACS Synth Biol<\/em>. Mar 21;3(3):152-62.<\/li>\n
  10. Horaguchi Y, Saito S, Kojima K, Tsugawa W, Ferri S<\/u><\/strong>, Sode K (2014) Engineering glucose oxidase to minimize the influence of oxygen on sensor response. Electrochimica Acta<\/em>, Volume 126, issue April 20, p. 158-161.<\/li>\n
  11. Miyake K, Abe K, Ferri S<\/u><\/strong>, Nakajima M, Nakamura M, Yoshida W, Kojima K, Ikebukuro K, Sode K. (2014) A green-light inducible lytic system for cyanobacterial cells. Biotechnol Biofuels<\/em> 7(1):56.<\/li>\n
  12. Abe K, Miyake K, Nakamura M, Kojima K, Ferri S<\/u><\/strong>, Ikebukuro K, Sode K (2014) Engineering of a green-light inducible gene expression system in Synechocystis<\/em> sp. PCC6803. Microb Biotechnol<\/em>. Mar;7(2):177-83<\/li>\n
  13. Savory N, Takahashi Y, Tsukakoshi K, Hasegawa H, Takase M, Abe K, Yoshida W, Ferri S<\/u><\/strong>, Kumazawa S, Sode K, Ikebukuro K (2014) Simultaneous improvement of specificity and affinity of aptamers against Streptococcus mutans<\/em> by in silico<\/em> maturation for biosensor development. Biotechnol Bioeng<\/em>. Mar;111(3):454-61.<\/li>\n
  14. Savory N, Goto S, Yoshida W, Unuma Y, Nakamura M, Abe K, Ferri S<\/u><\/strong>, Ikebukuro K (2013) Two-Dimensional Electrophoresis-Based Selection of Aptamers against an Unidentified Protein in a Tissue Sample. Anal Lett.<\/em> Dec; 46(18):2954-2963<\/li>\n
  15. Abe K, Yoshida W, Terada K, Yagi-Ishii Y, Ferri S<\/u><\/strong>, Ikebukuro K, Sode K (2013) Screening of peptide ligands for pyrroloquinoline quinone glucose dehydrogenase using antagonistic template-based biopanning. Int J Mol Sci.<\/em> Nov 25;14(12):23244-56.<\/li>\n
  16. Savory N, Lednor D, Tsukakoshi K, Abe K, Yoshida W, Ferri S<\/u><\/strong>, Jones BV, Ikebukuro K (2013) In silico<\/em> maturation of binding-specificity of DNA aptamers against Proteus mirabilis<\/em>. Biotechnol Bioeng<\/em>. Oct;110(10):2573-80.<\/li>\n
  17. Ferri S<\/u><\/strong>, Miyamoto Y, Sakaguchi-Mikami A, Tsugawa W, Sode K (2013) Engineering fructosyl peptide oxidase to improve activity toward the fructosyl hexapeptide standard for HbA1c measurement. Mol Biotechnol<\/em>. Jul;54(3):939-43.<\/li>\n
  18. Sakaguchi-Mikami A, Kameya M, Ferri S<\/u><\/strong>, Tsugawa W, Sode K (2013) Cloning and characterization of fructosamine-6-kinase from Arthrobacter aurescens<\/em>. Appl Biochem Biotechnol<\/em>. Jun;170(3):710-7.<\/li>\n
  19. Yoshida W, Saito T, Yokoyama T, Ferri S<\/u><\/strong>, Ikebukuro K (2013) Aptamer selection based on g4-forming promoter region. PLoS One<\/em>. Jun 4;8(6):e65497.<\/li>\n
  20. Sakaguchi-Mikami A, Ferri S<\/u><\/strong>, Katayama S, Tsugawa W, Sode K (2013) Identification and functional analysis of fructosyl amino acid-binding protein from Gram-positive bacterium Arthrobacter<\/em> sp. J Appl Microbiol<\/em>. May;114(5):1449-56.<\/li>\n
  21. Kojima K, Kobayashi T, Tsugawa W, Ferri S<\/u><\/strong>, Sode K (2013) Mutational analysis of the oxygen-binding site of cholesterol oxidase and its impact on dye-mediated dehydrogenase activity. J Mol Catal B: Enzym<\/em>. April 2013, 88: 41\u201346<\/li>\n
  22. Yamashita Y, Ferri S<\/u><\/strong>, Huynh ML, Shimizu H, Yamaoka H, Sode K (2013) Direct electron transfer type disposable sensor strip for glucose sensing employing an engineered FAD glucose dehydrogenase. Enzyme Microb Technol<\/em>. Feb 5;52(2):123-8.<\/li>\n
  23. Kojima K, Mikami-Sakaguchi A, Kameya M, Miyamoto Y, Ferri S<\/u><\/strong>, Tsugawa W, Sode K (2013) Substrate specificity engineering of Escherichia coli<\/em> derived fructosamine 6-kinase. Biotechnol Lett<\/em>. Feb;35(2):253-8.<\/li>\n
  24. Nonaka Y, Yoshida W, Abe K, Ferri S<\/u><\/strong>, Schulze H, Bachmann TT, Ikebukuro K (2013) Affinity improvement of a VEGF aptamer by in silico<\/em> maturation for a sensitive VEGF-detection system. Anal Chem<\/em>. 2013 Jan 15;85(2):1132-7.<\/li>\n
  25. Horaguchi Y, Saito S, Kojima K, Tsugawa W, Ferri S<\/u><\/strong>, Sode K (2012) Construction of mutant glucose oxidases with increased dye-mediated dehydrogenase activity. Int J Mol Sci<\/em>. Nov 2;13(11):14149-57.<\/li>\n
  26. Ferri S<\/u><\/strong>, Sode K (2012) Biomolecular engineering of biosensing molecules – The challenges in creating sensing molecules for glycated protein biosensing. Electrochemistry<\/em> 80(5):293-298.<\/li>\n
  27. Kim S, Nibe E, Tsugawa W, Kojima K, Ferri S<\/u><\/strong>, Sode K (2012) Construction of engineered fructosyl peptidyl oxidase for enzyme sensor applications under normal atmospheric conditions. Biotechnol Lett.<\/em> Mar;34(3):491-7.<\/li>\n
  28. Ferri S<\/u><\/strong>, Kojima K, Sode K (2011) Review of Glucose Oxidases and Glucose Dehydrogenases: A Bird\u2019s Eye View of Glucose Sensing Enzymes. J Diabetes Sci Technol<\/em> 5(5):1068-1076.<\/li>\n
  29. Mori K, Nakajima M, Kojima K, Murakami K, Ferri S<\/u><\/strong>, Sode K (2011) Screening of Aspergillus<\/em>-derived FAD glucose dehydrogenases from fungal genome database. Biotechnol Lett.<\/em> 33(11):2255-63.<\/li>\n
  30. Ferri S<\/u><\/strong>, Nibe E, Miyamoto Y, Kim S, Tsugawa W, Sode K (2011) Tuning Fructosyl Peptidyl Oxidase into Dehydrogenase and Its Application for the Construction of an Enzyme Electrode. ECS Transactions<\/em> 35(7):113-116.<\/li>\n
  31. Kim S, Nibe E, Ferri S<\/u><\/strong>, Tsugawa W, Sode K (2010) Engineering of dye-mediated dehydrogenase property of fructosyl amino acid oxidases by site-directed mutagenesis studies of its putative proton relay system. Biotechnol Lett.<\/em> 32(8):1123-1129.<\/li>\n
  32. Kim S, Ferri S<\/u><\/strong>, Tsugawa W, Mori K, Sode K (2010) Motif-based search for a novel fructosyl peptide oxidase from genome databases. Biotechnol Bioeng.<\/em> 106(3):358-366.<\/li>\n
  33. Desriani, Ferri S<\/u><\/strong>, Sode K (2010) Functional expression of Phanerochaete chrysosporium<\/em> cellobiose dehydrogenase flavin domain in Escherichia coli<\/em>. Biotechnol. Lett.<\/em> 32(6):855-859.<\/li>\n
  34. Desriani, Ferri S<\/u><\/strong>, Sode K (2010) Amino acid substitution at the substrate-binding subsite alters the specificity of the Phanerochaete chrysosporium<\/em> cellobiose dehydrogenase. Biochem.<\/em> Biophys. Res. Com<\/em>. 391(2): 1246-1250<\/li>\n
  35. Ferri S<\/u><\/strong>, Kim S, Tsugawa W, Sode K (2009) Review of Fructosyl Amino Acid Oxidase Engineering Research: A Glimpse into the Future of Hemoglobin A1c Biosensing. J Diabetes Sci Technol<\/em> 3(3):585-592.<\/li>\n
  36. Hanashi T, Yamazaki T, Tsugawa W, Ferri S<\/u><\/strong>, Nakayama D, Tomiyama M, Ikebukuro K, Sode K (2009) BioCapacitor – a novel category of biosensor. Biosens Bioelectron.<\/em> Mar 15;24(7):1837-42.<\/li>\n
  37. Kim S, Miura S, Ferri S<\/u><\/strong>, Tsugawa W, Sode K (2009) Cumulative effect of amino acid substitution at the putative active site of fructosyl amine oxidase. Enzyme and Microbial Technology<\/em> 44: 52\u201356.<\/li>\n
  38. Yamaoka H, Yamashita Y, Ferri S<\/u><\/strong>, Sode K. (2008) Site directed mutagenesis studies of FAD-dependent glucose dehydrogenase catalytic subunit of Burkholderia cepacia<\/em>. Biotechnol Lett.<\/em> 30(11):1967-72.<\/li>\n
  39. Sakaguchi-Mikami A, Taneoka A, Yamoto R, Ferri S<\/u><\/strong>, Sode K (2008) Engineering of Ligand Specificity of Periplasmic Binding Protein for Glucose Sensing. Biotechnol. Lett<\/em>. 30(8):1453-60<\/li>\n
  40. Miura S, Ferri S<\/u><\/strong>, Tsugawa W, Kim S, Sode K (2008) Development of fructosyl amine oxidase specific to fructosyl valine by site-directed mutagenesis. Protein Eng Des Sel<\/em>. 21: 233-239<\/li>\n
  41. Chino S, Sakaguchi A, Yamoto R, Ferri S<\/u><\/strong>, Sode K (2007) Branched-chain Amino Acid Biosensing Using Fluorescent Modified Engineered Leucine\/Isoleucine\/Valine Binding Protein. Int J Mol Sci.<\/em> 8: 513-525.<\/li>\n
  42. Sakaguchi A, Ferri S<\/u><\/strong>, Tsugawa W, Sode K (2007) Novel fluorescent nanosensor for a-fructosyl amino acids based on engineered fructosyl amino acid binding protein. Biosens Bioelectron<\/em> 22(9-10):1933-8.<\/li>\n
  43. Miura S, Ferri S<\/u><\/strong>, Tsugawa W, Kim S, Sode K (2006) Active site analysis of fructosyl amine oxidase using homology modeling and site-directed mutagenesis. Biotechnol. Lett<\/em>. 23:1895-900.<\/li>\n
  44. Tsuya T, Ferri S<\/u><\/strong>, Fujikawa M, Yamaoka H, Sode K (2006) Cloning and functional expression of glucose dehydrogenase complex of Burkholderia<\/em> cepacia<\/em> in Escherichia coli. J. Biotechnol<\/em>. 123 (2), 127\u2013136.<\/li>\n
  45. Sakaguchi A, Ferri S<\/u><\/strong>, Sode K (2005) SocA is a novel periplasmic binding protein for fructosyl amino acid. Biochem. Biophys. Res.<\/em> Com<\/em>. 336(4):1074-1080.<\/li>\n
  46. Tanaka S, Igarashi S, Ferri S<\/u><\/strong>, Sode K (2005) Increasing stability of water-soluble PQQ glucose dehydrogenase by increasing hydrophobic interaction at dimeric interface. BMC Biochemistry<\/em>. 6; 1.<\/li>\n
  47. Ferri S<\/u><\/strong>, Sakaguchi A, Goto H, Tsugawa W, Sode K (2005) Isolation and Characterization of a Fructosyl-amine Oxidase from Arthrobacter <\/em>Sp FV1-1. Biotechnol. Lett<\/em>. 27(1):27-32.<\/li>\n
  48. Ferri S<\/u><\/strong>, Miura S, Sakaguchi A, Ishimura F, Tsugawa W, and Sode K (2004) Cloning and Expression of a Fructosyl-amine Oxidase from the Marine Yeast Pichia <\/em>Sp N1-1. Mar Biotechnol <\/em>(NY) 6(6):625-32.<\/li>\n
  49. Yamaoka H, Ferri S<\/u><\/strong>, Fujikawa M, Sode K (2004) Essential role of the small subunit of thermostable glucose dehydrogenase from Burkholderia cepacia.<\/em> Biotechnol. Lett<\/em>. 26(22):1757-61.<\/li>\n
  50. Tamada T, Feese MD, Ferri SR<\/u><\/strong>, Kato Y, Yajima R, Toguri T, Kuroki R (2004) Substrate recognition and selectivity of plant glycerol-3-phosphate acyltransferases (GPATs) from Cucurbita moscata<\/em> and Spinacea oleracea.<\/em> Acta Cryst<\/em>. D60, 13-21.<\/li>\n
  51. Sakaguchi A, Tsugawa W, Ferri S<\/u><\/strong>, Sode K (2003) Development of a highly sensitive fructosyl-valine enzyme sensor employing recombinant fructosyl amine oxidase. Electrochemistry<\/em> 76(6): 442-445.<\/li>\n
  52. Ogawa K, St\u00f6llner D, Scheller F, Warsinke A, Ishimura F, Tsugawa W, Ferri S<\/u><\/strong>, Sode K (2002) Development of a flow injection analysis (FIA) enzyme sensor for fructosyl amine monitoring. Anal. Bioanal. Chem<\/em>. 373: 211-214.<\/li>\n
  53. Tamada T, Ferri SR<\/u><\/strong>, Toguri T, Kuroki R (2001) Structure and Function of Glycerol-3-Phosphate Acyltransferase. The Journal of Structural Biology SAKABE Project<\/em> 7(3) 1-10 [Japanese<\/em>]<\/li>\n
  54. Ferri SR,<\/u><\/strong> Toguri T (1997) Substrate Specificity Modification of the Stromal Glycerol-3-phosphate Acyltransferase. Arch. Biochem. Biophys<\/em>. 337(2):202-208.<\/li>\n
  55. Ferri SR<\/u><\/strong>, Oshizaki-Nishizawa O, Azuma M, Toguri T (1997) Identification of a Region in Stromal Glycerol 3-phosphate Acyltransferase which Controls Acyl Chain Specificity. in<\/em> Physiology, Biochemistry and Molecular Biology of Plant Lipids (Williams JP, Khan MU, Lem NW, eds.) pp. 137-139, Kluwer Academic Publishers, Netherlands.<\/li>\n
  56. Lawson DM, Derewenda U, Serre L, Ferri S<\/u><\/strong>, Szittner R, Wei Y, Meighen EA, Derewenda ZS (1994) Structure of a Myristoyl-ACP-specific Thioesterase from Vibrio harveyi<\/em>. Biochemistry<\/em>. 33(32): 9382-8.<\/li>\n
  57. Ferri SR,<\/u><\/strong> Meighen EA (1994) An Essential Histidine Residue Required for Fatty Acylation and Acyl Transfer by Myristoyltransferase from Luminescent Bacteria. J. Biol. Chem<\/em>. 269(9):6683-8.<\/li>\n
  58. Swenson L, Ferri SR<\/u><\/strong>, Green R, Sharp AM, Meighen EA, Derewenda ZS (1992) Expression, Purification and Crystallization of the Vibrio harveyi<\/em> Acyltransferase. J. Mol. Biol<\/em>. 227(2):572-4.<\/li>\n
  59. Ferri SR,<\/u><\/strong> Meighen EA (1991) A Lux<\/em>-specific Myristoyl Transferase in Luminescent Bacteria Related to Eukaryotic Serine Esterases. J. Biol. Chem<\/em>. 266(20):12852-12857.<\/li>\n
  60. Ferri S<\/u><\/strong>, Soly RR, Miyamoto C, Meighen E (1991) Complementation In Vivo<\/em> of the Lux<\/em>-specific Fatty Acid Reductase Subunits from Different Luminescent Bacteria. in<\/em> Bioluminescence and Chemiluminescence: Current Status (PE Stanley & LJ Kricka, eds.) pp. 39-42, John Wiley & Sons.<\/li>\n
  61. Ferri SR<\/u><\/strong>, Soly RR, Szittner RB, Meighen EA (1991) Structure and Properties of Luciferase from Photobacterium phosphoreum<\/em>. Biochem. Biophys. Res.<\/em> Com<\/em>. 176(1):541-548.<\/li>\n
  62. Mancini J, Boylan M, Soly R, Ferri S<\/u><\/strong>, Szittner R, Meighen E (1989) Organization of the Lux<\/em> Genes of Photobacterium phosphoreum<\/em>. J.<\/em> Biolumin. Chemilumin<\/em>. 3: 201-205.<\/li>\n
  63. Soly RR, Mancini JA, Ferri SR<\/u><\/strong>, Boylan M, Meighen EA (1988) A New Lux<\/em> Gene in Bioluminescent Bacteria Codes for a Protein Homologous to the Bacterial Luciferase Subunits. Biochem.<\/em> Biophys. Res. Com<\/em>. 155(1): 351-358.<\/li>\n<\/ol>\n

     <\/p>\n

    Patents:<\/strong><\/p>\n

    Ferri SR<\/u><\/strong> and Toguri T (Kirin Brewery Co., Ltd.) DNA Strands Encoding Glycerol-3-Phosphate Acyltransferase. Patent filed in 1995: JP19950192123 (US6160203, EP0843007, WO9705246).<\/p>\n

    Ferri SR<\/u><\/strong> and Toguri T (Kirin Brewery Co., Ltd.) \u03b2-ketoacyl-ACP Synthase II enzymes and genes coding for same. Patent filed in 1997: JP19970011430 (US6200788, EP0969014, WO9832770).<\/p>\n

     <\/p>\n

    Invited Lectures:<\/strong><\/p>\n

    Ferri S<\/u><\/strong> (2011) The International Genetically Engineered Machine Competition – an overview of iGEM. \u9175\u7d20\u5de5\u5b66\u7814\u7a76\u4f1a \u7b2c66 \u56de\u8b1b\u6f14\u4f1a (invited lecture<\/strong>) Sept., Tokyo.<\/p>\n

    Ferri S<\/u><\/strong> (2011) The iGEM Jamboree – a great addition to a science student\u2019s training. \u7b2c63 \u56de\u65e5\u672c\u751f\u7269\u5de5\u5b66\u4f1a\u5927\u4f1a (invited lecture<\/strong>) Sept., Tokyo.<\/p>\n

     <\/p>\n

     <\/p>\n","protected":false},"excerpt":{"rendered":"

    List of Publications: Shiota M, Yamazaki T, Yoshimatsu K, Kojima K, Tsugawa W, Ferri S, Sode K (2016) An Fe-S cluster in the conserved Cys-rich region in the catalytic subunit of FAD-dependent dehydrogenase complexes. Bioelectrochemistry. Feb 2. pii: S1567-5394(16)30010-X. doi: 10.1016\/j.bioelechem.2016.01.010. [Epub ahead of print] Nakajima M, Abe K, Ferri S, Sode K (2016) Development of a light-regulated cell-recovery system for non-photosynthetic bacteria. Microb Cell Fact. Feb 15;15(1):31. Ferri S, Nakamura M, Ito A, Nakajima M, Abe K, Kojima K, Sode K (2015) Efficient surface-display of autotransporter proteins in cyanobacteria Algal Research 12: 337\u2013340. \u00a0Fukaya T, Abe K, Savory N, Tsukakoshi K, Yoshida W, Ferri S, Sode K, Ikebukuro K. […]<\/p>\n","protected":false},"author":7,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-34","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"http:\/\/cheme.eng.shizuoka.ac.jp\/wordpress\/ferri\/wp-json\/wp\/v2\/pages\/34","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/cheme.eng.shizuoka.ac.jp\/wordpress\/ferri\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"http:\/\/cheme.eng.shizuoka.ac.jp\/wordpress\/ferri\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"http:\/\/cheme.eng.shizuoka.ac.jp\/wordpress\/ferri\/wp-json\/wp\/v2\/users\/7"}],"replies":[{"embeddable":true,"href":"http:\/\/cheme.eng.shizuoka.ac.jp\/wordpress\/ferri\/wp-json\/wp\/v2\/comments?post=34"}],"version-history":[{"count":20,"href":"http:\/\/cheme.eng.shizuoka.ac.jp\/wordpress\/ferri\/wp-json\/wp\/v2\/pages\/34\/revisions"}],"predecessor-version":[{"id":137,"href":"http:\/\/cheme.eng.shizuoka.ac.jp\/wordpress\/ferri\/wp-json\/wp\/v2\/pages\/34\/revisions\/137"}],"wp:attachment":[{"href":"http:\/\/cheme.eng.shizuoka.ac.jp\/wordpress\/ferri\/wp-json\/wp\/v2\/media?parent=34"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}