{"id":183,"date":"2021-04-20T20:58:17","date_gmt":"2021-04-20T17:58:17","guid":{"rendered":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/?p=183"},"modified":"2021-05-12T10:54:37","modified_gmt":"2021-05-12T07:54:37","slug":"publications-2001-2005","status":"publish","type":"post","link":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/2021\/04\/20\/publications-2001-2005\/","title":{"rendered":"Publications 2001-2005"},"content":{"rendered":"\n<p><strong>2001<\/strong><\/p>\n\n\n\n<ol class=\"wp-block-list\"><li><strong>Stathopoulos C.,&nbsp;<\/strong>Jacquin-Becker C., Becker H.D., Li T., Ambrogelly A., Longman R. and S\u00f6ll D.&nbsp;<em>Methanococcus jannaschii<\/em>&nbsp;Prolyl-Cysteinyl-tRNA synthetase possesses overlapping amino acid binding sites.&nbsp;<em>Biochemistry<\/em>&nbsp;40: 46-52.<\/li><li><strong>Stathopoulos C.,<\/strong>&nbsp;Tekos A., Zarkadis, I. and Drainas D. (2001) Extensive deproteinization of<em>&nbsp;Dictyostelium discoideum<\/em>&nbsp;RNase \u03a1 reveals a new catalytic activity.&nbsp;<em>Eur. J. Biochem.<\/em>&nbsp;268: 2134-214<\/li><li>Ibba M.,&nbsp;<strong>Stathopoulos C.<\/strong>&nbsp;and S\u00f6ll D. . Protein Synthesis: 23 Amino&nbsp;acids and counting.&nbsp;<em>Current Biology<\/em>&nbsp;11: 563-565.<\/li><li>Ruan B., Ahel I., Ambrogelly A., Becker H. D., Bunjun S., Feng L., Tumbula D., Ibba M., Korencic D., Kobayashi H., Jacquin-Becker C., Mejlhede N., Min B., Raczniak G., Rinehart J.,&nbsp;<strong>Stathopoulos, C.<\/strong>, Li T. and S\u00f6ll<\/li><li><strong>Stathopoulos<\/strong><strong>C<\/strong><strong>.<\/strong>,&nbsp;KimW.,&nbsp;LiT.,&nbsp;AndersonI.,&nbsp;PaliouraS.,&nbsp;WhitmanW.&nbsp;andS\u00f6llD.&nbsp;Cysteinyl-tRNAsynthetaseisnotessentialfortheviabilitythearcheaon<em>Methanococcus<\/em><em>maripaludis<\/em>.&nbsp;.&nbsp;<em>USA<\/em><em>&nbsp;98<\/em>: 14292-14297.<\/li><\/ol>\n\n\n\n<p><strong>2002<\/strong><\/p>\n\n\n\n<ol class=\"wp-block-list\"><li>FengL.,&nbsp;<strong>Stathopoulos<\/strong><strong>C<\/strong><strong>.<\/strong>,&nbsp;AhelI.,&nbsp;MitraA.,&nbsp;HartschT.,&nbsp;TumbulaD.&nbsp;andS\u00f6llD. .&nbsp;Aminoacyl-tRNA formation in the hyperthermophile&nbsp;<em>Themus thermophilus. Extremophiles&nbsp;<\/em>6: 167-174.<\/li><li>Jacquin-Becker C., Ahel I., Ambrogelly A., Ruan B. S\u00f6ll D. and&nbsp;<strong>Stathopoulos C.<\/strong>&nbsp;Cysteinyl-tRNA formation and prolyl-tRNA synthetase<em>&nbsp;FEBS Letters<\/em>&nbsp;514: 34-36.<\/li><li><strong>Stathopoulos C.<\/strong>, Ahel I., Ambrogelly A., Becker H., Bunjun S., Feng L., Herring S., Jacquin-Becker C., Kobayashi H., Korencic D., Krett B., Mejlhede N., Min B., Nakano H., Namgoong S., Polycarpo C., Raczniak G., Rinehart J., Rosas-Sandoval G., Ruan B., Sabina J., Sauerwald A., Toogood H., Tumbula-Hansen D., Ibba M. and S\u00f6ll D. . Aminoacyl-tRNA synthesis: a post-genome perspective.<em>&nbsp;Cold Spring Harbor Symp. Quant. Biol.<\/em>&nbsp;Vol. LXVI 175-183.<\/li><li>AhelI.,&nbsp;<strong>Stathopoulos<\/strong><strong>C<\/strong><strong>.,<\/strong>AmbrogellyA.,&nbsp;SauerwaldA.,&nbsp;ToogoodH.,&nbsp;HartschT.&nbsp;andS\u00f6llD.&nbsp;Cysteineactivationisaninherentpropertyprolyl-tRNAsynthetases.&nbsp;277: 34743-34748.<\/li><li>Ambrogelly A., Ahel I., Polycarpo C., Bunjun-Srihari S., Krett B., Jacquin-Becker C., Kohrer C.,&nbsp;<strong>Stathopoulos C.,<\/strong>&nbsp;RajBhandary U.L. and S\u00f6ll D.&nbsp;<em>Methanocaldococcus jannaschii<\/em>&nbsp;prolyl-tRNA synthetase charges tRNA<sup>Pro<\/sup>&nbsp;with cysteine.&nbsp;<em>J. Biol. Chem.<\/em>&nbsp;277: 34749-34754.<\/li><\/ol>\n\n\n\n<p><strong>2003<\/strong><\/p>\n\n\n\n<ol class=\"wp-block-list\"><li>KalavriziotiD.,&nbsp;VourekasA.,&nbsp;TekosA.,&nbsp;<strong>Stathopoulos<\/strong><strong>C<\/strong><strong>.<\/strong>andDrainasD.&nbsp;KineticsinhibitionribonucleaseP&nbsp;activity&nbsp;bypeptidyl-transferaseinhibitors<em>Mol<\/em><em>.&nbsp;<\/em>30: 9-15.&nbsp;(\u0399F: 2.506)<\/li><li>Kamtekar S., Kennedy D.W., Wang J.,&nbsp;<strong>Stathopoulos C.<\/strong>,&nbsp;S\u00f6llT.A. (2003) The structural basis of cysteine aminoacylation of tRNA<sup>Pro<\/sup>&nbsp;by prolyl-tRNA synthetases&nbsp;<em>Proc<\/em><em>.&nbsp;<\/em>.&nbsp;<em>USA<\/em><em>&nbsp;100<\/em>: 1673-1678.<\/li><\/ol>\n\n\n\n<p><strong>2004<\/strong><\/p>\n\n\n\n<ol class=\"wp-block-list\"><li>Korencic D., Ahel I., Schelert J., Sacher M., Ruan B.,&nbsp;<strong>Stathopoulos C.<\/strong>, Blum P., Ibba, M. and S\u00f6ll D. A freestanding proofreading domain isrequired for protein synthesis quality control in archaea.&nbsp;<em>.<\/em><em>USA<\/em><em>&nbsp;101<\/em>: 10260-10265.<\/li><li>Tekos A.&nbsp;<strong>(*)<\/strong>,&nbsp;<strong>Stathopoulos C. (*)<\/strong>, Tsambaos D. and Drainas D. (2004) RNase P: a screening system and molecular target for the development of new drugs.&nbsp;<em>Curr. Med. Chem<\/em>. 11: 2979-2989.&nbsp;<strong>(*)<\/strong>Equal contribution, first co-authors<\/li><\/ol>\n\n\n\n<p><strong>2005<\/strong><\/p>\n\n\n\n<ol class=\"wp-block-list\"><li>RuanB.,&nbsp;BoveeM.L.,&nbsp;SacherM.,&nbsp;<strong>Stathopoulos<\/strong><strong>C<\/strong><strong>.<\/strong>,&nbsp;PorallaK.,&nbsp;FrancklynC.S.&nbsp;andS\u00f6llD. (200A unique hydrophobic cluster near the active site contributes to differences of borrelidin inhibition among threonyl-tRNA&nbsp;synthetases.&nbsp;280: 571-577.<\/li><li>Ambrogelly A., Kamtekar S.,&nbsp;<strong>Stathopoulos C.,<\/strong>&nbsp;Kennedy D. and&nbsp;S\u00f6ll D. Asymmetrical behavior of archaeal proly-tRNA synthetase&nbsp;<em>FEBS<\/em><em>Letters<\/em>&nbsp;579: 6017-6022.<\/li><\/ol>\n","protected":false},"excerpt":{"rendered":"<p>2001 Stathopoulos C.,&nbsp;Jacquin-Becker C., Becker H.D., Li T., Ambrogelly A., Longman R. and S\u00f6ll D.&nbsp;Methanococcus jannaschii&nbsp;Prolyl-Cysteinyl-tRNA synthetase possesses overlapping amino acid binding sites.&nbsp;Biochemistry&nbsp;40: 46-52. Stathopoulos C.,&nbsp;Tekos A., Zarkadis, I. and Drainas D. (2001) Extensive deproteinization of&nbsp;Dictyostelium discoideum&nbsp;RNase \u03a1 reveals a new catalytic activity.&nbsp;Eur. J. Biochem.&nbsp;268: 2134-214 Ibba M.,&nbsp;Stathopoulos C.&nbsp;and S\u00f6ll D. . Protein Synthesis: 23 Amino&nbsp;acids and counting.&nbsp;Current Biology&nbsp;11: 563-565.&hellip;<\/p>\n","protected":false},"author":2,"featured_media":0,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[7],"tags":[],"class_list":["post-183","post","type-post","status-publish","format-standard","hentry","category-publications"],"_links":{"self":[{"href":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/wp-json\/wp\/v2\/posts\/183","targetHints":{"allow":["GET"]}}],"collection":[{"href":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/wp-json\/wp\/v2\/users\/2"}],"replies":[{"embeddable":true,"href":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/wp-json\/wp\/v2\/comments?post=183"}],"version-history":[{"count":1,"href":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/wp-json\/wp\/v2\/posts\/183\/revisions"}],"predecessor-version":[{"id":184,"href":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/wp-json\/wp\/v2\/posts\/183\/revisions\/184"}],"wp:attachment":[{"href":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/wp-json\/wp\/v2\/media?parent=183"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/wp-json\/wp\/v2\/categories?post=183"},{"taxonomy":"post_tag","embeddable":true,"href":"http:\/\/9.dynacomp2.eu\/rna\/wordpress\/wp-json\/wp\/v2\/tags?post=183"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}