{"id":1096,"date":"2021-08-30T09:38:12","date_gmt":"2021-08-30T07:38:12","guid":{"rendered":"http:\/\/katedrabiologie.sk\/?page_id=1096"},"modified":"2023-10-26T14:21:21","modified_gmt":"2023-10-26T12:21:21","slug":"doc-ing-stefan-janecek-drsc","status":"publish","type":"page","link":"https:\/\/oddeleniebiologie.sk\/en\/doc-ing-stefan-janecek-drsc\/","title":{"rendered":"prof. Ing. \u0160tefan Jane\u010dek, DrSc."},"content":{"rendered":"<div class=\"wp-block-columns is-layout-flex wp-container-core-columns-is-layout-8f761849 wp-block-columns-is-layout-flex\">\n<div class=\"wp-block-column is-layout-flow wp-block-column-is-layout-flow\" style=\"flex-basis:33.33%\">\n<figure class=\"wp-block-image size-full\"><img loading=\"lazy\" decoding=\"async\" width=\"700\" height=\"948\" src=\"http:\/\/oddeleniebiologie.sk\/wp-content\/uploads\/2021\/08\/Stefan_Janecek-1.jpg\" alt=\"\" class=\"wp-image-943\" srcset=\"https:\/\/oddeleniebiologie.sk\/wp-content\/uploads\/2021\/08\/Stefan_Janecek-1.jpg 700w, https:\/\/oddeleniebiologie.sk\/wp-content\/uploads\/2021\/08\/Stefan_Janecek-1-222x300.jpg 222w, https:\/\/oddeleniebiologie.sk\/wp-content\/uploads\/2021\/08\/Stefan_Janecek-1-9x12.jpg 9w\" sizes=\"auto, (max-width: 700px) 100vw, 700px\" \/><\/figure>\n<\/div>\n\n\n\n<div class=\"wp-block-column is-layout-flow wp-block-column-is-layout-flow\" style=\"flex-basis:66.66%\">\n<p class=\"wp-block-paragraph\"><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">vysoko\u0161kolsk\u00fd u\u010dite\u013e<\/span><\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Vedecko-pedagogick\u00e1 charakteristika<\/strong> &#8211;\u00a0<a href=\"http:\/\/oddeleniebiologie.sk\/wp-content\/uploads\/2021\/08\/Janecek.pdf\">stiahni PDF<\/a><\/span><\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><span class=\"has-inline-color has-black-color\">Tituly, hodnosti:<\/span><\/strong><\/p>\n\n\n\n<ul class=\"has-black-color has-text-color wp-block-list\">\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">1989 \u2013 Ing. Katedra biochemickej technol\u00f3gie, Chemicko-technologick\u00e1 fakulta STU v Bratislave<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">1993 \u2013 CSc.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">2002 \u2013 DrSc.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">2015 \u2013 doc.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">2021 \u2013 prof. <\/span><\/li>\n<\/ul>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><span class=\"has-inline-color has-black-color\">Pracovisko:<\/span><\/strong><\/p>\n\n\n\n<ul class=\"has-black-color has-text-color wp-block-list\">\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">1993 &#8211; doteraz \u00dastav molekul\u00e1rnej biol\u00f3gie SAV, Bratislava &#8211; ved\u00faci vedeck\u00fd pracovn\u00edk, Laborat\u00f3rium evol\u00facie prote\u00ednov &#8211; na \u00dastave molekul\u00e1rnej biol\u00f3gie SAV v Bratislave https:\/\/imb.savba.sk\/~janecek<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">2001 \u2013 doteraz Odborn\u00fd asistent, Katedra biol\u00f3gie, Univerzita sv. Cyrila a Metoda, Fakulta pr\u00edrodn\u00fdch vied, Trnava, &#8211; hlavn\u00e9 vyu\u010dovan\u00e9 predmety: Molekulovo-biologick\u00e9 datab\u00e1zy, Bioinformatika a Prote\u00ednov\u00fd dizajn v bakal\u00e1rskom a magisterskom stupni.<\/span><\/li>\n<\/ul>\n\n\n\n<p class=\"wp-block-paragraph\"><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Hlavn\u00e9 oblasti vedeck\u00e9ho z\u00e1ujmu:<\/strong> \u0165a\u017eisko pr\u00e1ce je teoretick\u00e9 <em>in silico<\/em> \u0161t\u00fadium prote\u00ednov &#8211; ich \u0161trukt\u00far vo vz\u0165ahu k ich funkcii, vlastnostiam a evol\u00facii. Hlavn\u00fd z\u00e1ujem je o enz\u00fdmy z alfa-amyl\u00e1zovej rodiny &#8211; v s\u00fa\u010dasnosti v r\u00e1mci klasifik\u00e1cie CAZy (Carbohydrate Active enZymes) ide o rodiny glykozidov\u00fdch hydrol\u00e1z GH13 (tvor\u00ed klan GH-H s rodinami GH70 a GH77), GH57 a GH119 (pr\u00edpadne GH31 a GH126). Rovnak\u00e1 pozornos\u0165 je venovan\u00e1 aj bioinformatick\u00fdm pr\u00edstupom k \u0161t\u00fadiu \u0161krob-via\u017eucich dom\u00e9n amylolytick\u00fdch enz\u00fdmov a ich anal\u00f3gov v neamylolytick\u00fdch enz\u00fdmoch a prote\u00ednoch, klasifikovan\u00fdch do tzv. rod\u00edn CBM (carbohydrate-binding module families).<\/span><\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><span class=\"has-inline-color has-black-color\">Vedenie pr\u00e1c&nbsp;(obh\u00e1jen\u00e9):<\/span><\/strong><\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Bakal\u00e1rske ; Diplomov\u00e9 ; Rigor\u00f3zne ; Doktorandsk\u00e9<\/span><\/p>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><span class=\"has-inline-color has-black-color\">\u010clenstvo v&nbsp;sk\u00fa\u0161obn\u00fdch komisi\u00e1ch, vo vedeck\u00fdch rad\u00e1ch, v&nbsp;odborn\u00fdch, habilita\u010dn\u00fdch a&nbsp;inaugura\u010dn\u00fdch komisi\u00e1ch<\/span><\/strong>:<\/p>\n\n\n\n<ul class=\"has-black-color has-text-color wp-block-list\">\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">\u010dlen komisie pre \u0161t\u00e1tne sk\u00fa\u0161ky v \u0161tudijnom programe Aplikovan\u00e1 biol\u00f3gia na FPV UCM v Trnave (bakal\u00e1rske, magistersk\u00e9, rigor\u00f3zne \u0161t\u00fadium)<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">\u010dlen komisie pre \u0161t\u00e1tne sk\u00fa\u0161ky v \u0161tudijnom programe Molekul\u00e1rna biol\u00f3gia na FPV UCM v Trnave (doktorandsk\u00e9 \u0161t\u00fadium)<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">\u010dlen vedeckej rady Fakulty pr\u00edrodn\u00fdch vied UCM Trnava<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">\u010dlen komisie pre obhajoby doktorsk\u00fdch dizert\u00e1ci\u00ed pre molekul\u00e1rnu biol\u00f3giu, \u010dlen<\/span><\/li>\n<\/ul>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><span class=\"has-inline-color has-black-color\">\u00da\u010das\u0165 na rie\u0161en\u00ed vedecko-v\u00fdskumn\u00fdch projektov za posledn\u00e9 roky:<\/span><\/strong><\/p>\n\n\n\n<ul class=\"has-black-color has-text-color wp-block-list\">\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">VEGA (od roku 1996)<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">APVV (LPP 2009)<\/span><\/li>\n<\/ul>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><span class=\"has-inline-color has-black-color\">Organiz\u00e1torsk\u00e1 a&nbsp;editorsk\u00e1 \u010dinnos\u0165:<\/span><\/strong><\/p>\n\n\n\n<ul class=\"has-black-color has-text-color wp-block-list\">\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">zakladate\u013e a hlavn\u00fd organiz\u00e1tor s\u00e9rie medzin\u00e1rodn\u00fdch konferenci\u00ed o enz\u00fdmoch z alfa-amyl\u00e1zovej rodiny &#8211; ALAMY &#8211; od roku 2001 https:\/\/www.degruyter.com\/view\/j\/amylase konaj\u00fa ka\u017ed\u00e9 tri roky (2001, 2004, 2007, 2010, 2013, 2016, 2019) na Slovensku v Kongresovom centre SAV na Smolenickom z\u00e1mku: https:\/\/imb.savba.sk\/~janecek\/Alamys\/<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">zakladate\u013e a hlavn\u00fd editor \u010dasopisu &#8220;Amylase&#8221;;\u00a0 \u010dasopis &#8220;Amylase&#8221;: zakladate\u013e a Editor-in-Chief;<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">\u010dasopis &#8220;3Biotech&#8221;: Associate Editor;<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">\u010dasopis &#8220;Biologia&#8221;, section Cellular and Molecular Biology: Managing Editor.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">\u010dasopis &#8220;Enzyme and Microbial Technology&#8221;: Editorial Board Member.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Ad hoc recenzent pre \u010dasopisy v odbore Life Sciences.<\/span><\/li>\n<\/ul>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><span class=\"has-inline-color has-black-color\">Spolupr\u00e1ca v&nbsp;zahrani\u010d\u00ed:<\/span><\/strong><\/p>\n\n\n\n<ul class=\"has-black-color has-text-color wp-block-list\">\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Prof. Birte Svensson, Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Kgs. Lyngby &#8211; Copenhagen, D\u00e1nsko<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Prof. Marc J.E.C. van der Maarel, Department Aquatic Biotechnology and Bioproduct Engineering, University of Groningen, Groningen, Holandsko<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Dr. Dessy Natalia, Biochemistry Research Division, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Bandung, Indon\u00e9zia<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Dr. Kian Mau Goh, Department of Biosciences and Health Sciences, Universiti Teknologi Malaysia, Johor Bahru, Malajzia<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Dr. Jean-Luc Da Lage, Laboratoire Evolution, G\u00e9nomes Comportement, Ecologie, CNRS, Universit\u00e9 Paris Sud, Gif sur Yvette, Franc\u00fazko<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Dr. Natasa Bozic, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Belgrade, Srbsko<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Dr. Pawe\u0142 Filipkowski, Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdansk, Po\u013esko<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Dr. Matthew S. Gentry, Department of Molecular and Cellular Biochemistry, Epilepsy and Brain Metabolism Alliance, and Epilepsy Research Center, University of Kentucky College of Medicine, Lexington, KY, USA<\/span><\/li>\n<\/ul>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><span class=\"has-inline-color has-black-color\">Ocenenia:<\/span><\/strong><\/p>\n\n\n\n<ul class=\"has-black-color has-text-color wp-block-list\">\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Cena SAV &#8211; 1997 a 2013<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Cena rektora UCM v Trnave \u2013 2015<\/span><\/li>\n<\/ul>\n\n\n\n<p class=\"wp-block-paragraph\"><strong><span class=\"has-inline-color has-black-color\">Vybran\u00e9 publik\u00e1cie:<\/span><\/strong><\/p>\n\n\n\n<ol type=\"1\" class=\"has-black-color has-text-color wp-block-list\">\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Janecek, S.<\/strong> (<strong>1992<\/strong>). New conserved amino acid region of \u03b1-amylases in the third loop of their (\u03b2\/\u03b1) 8-barrel domains.\u00a0<em>Biochemical Journal<\/em>,\u00a0<em>288<\/em>(3), 1069-1070.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160. <\/strong>(<strong>1994<\/strong>). Sequence similarities and evolutionary relationships of microbial, plant and animal \u03b1\u2010amylases.\u00a0<em>European journal of biochemistry<\/em>,\u00a0<em>224<\/em>(2), 519-524.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Janecek, S.<\/strong>, MacGregor, E. A., &amp; Svensson, B. (<strong>1995<\/strong>). Characteristic differences in the primary structure allow discrimination of cyclodextrin glucanotransferases from alpha-amylases.\u00a0<em>Biochemical Journal<\/em>,\u00a0<em>305<\/em>(Pt 2), 685.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Janec\u0306ek, S. <\/strong>(<strong>1997<\/strong>). \u03b1-Amylase family: molecular biology and evolution.\u00a0<em>Progress in biophysics and molecular biology<\/em>,\u00a0<em>67<\/em>(1), 67-97.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Janecek, S.<\/strong>, Svensson, B., &amp; Henrissat, B. (<strong>1997<\/strong>). Domain evolution in the \u03b1-amylase family.\u00a0<em>Journal of molecular evolution<\/em>,\u00a0<em>45<\/em>(3), 322-331.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160.<\/strong>, L\u00e9v\u00eaque, E., Belarbi, A., &amp; Haye, B. (<strong>1999<\/strong>). Close evolutionary relatedness of \u03b1-amylases from archaea and plants.\u00a0<em>Journal of molecular evolution<\/em>,\u00a0<em>48<\/em>(4), 421-426.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160.<\/strong>, &amp; \u0160ev\u010d\u0131\u0301k, J. (<strong>1999<\/strong>). The evolution of starch-binding domain.\u00a0<em>FEBS letters<\/em>,\u00a0<em>456<\/em>(1), 119-125.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">L\u00e9v\u00eaque, E., <strong>Jane\u010dek, \u0160<\/strong>., Haye, B., &amp; Belarbi, A. (<strong>2000<\/strong>). Thermophilic archaeal amylolytic enzymes.\u00a0<em>Enzyme and microbial technology<\/em>,\u00a0<em>26<\/em>(1), 3-14.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">MacGregor, E. A., <strong>Jane\u010dek, \u0160.<\/strong>, &amp; Svensson, B. (<strong>2001<\/strong>). Relationship of sequence and structure to specificity in the \u03b1-amylase family of enzymes.\u00a0<em>Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology<\/em>,\u00a0<em>1546<\/em>(1), 1-20.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Oslancova, A., &amp; <strong>Jane\u010dek, \u0160. <\/strong>(<strong>2002<\/strong>). Oligo-1, 6-glucosidase and neopullulanase enzyme subfamilies from the \u03b1-amylase family defined by the fifth conserved sequence region.\u00a0<em>Cellular and Molecular Life Sciences CMLS<\/em>,\u00a0<em>59<\/em>(11), 1945-1959.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160. <\/strong>(<strong>2002<\/strong>). How many conserved sequence regions are there in the \u03b1-amylase family.\u00a0<em>Biologia<\/em>,\u00a0<em>57<\/em>(Suppl 11), 29-41.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160.<\/strong>, Svensson, B., &amp; MacGregor, E. A. (<strong>2003<\/strong>). Relation between domain evolution, specificity, and taxonomy of the \u03b1\u2010amylase family members containing a C\u2010terminal starch\u2010binding domain.\u00a0<em>European Journal of Biochemistry<\/em>,\u00a0<em>270<\/em>(4), 635-645.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Da Lage, J. L., Feller, G., &amp; <strong>Jane\u010dek, \u0160. <\/strong>(<strong>2004<\/strong>). Horizontal gene transfer from Eukarya to Bacteria and domain shuffling: the \u03b1-amylase model.\u00a0<em>Cellular and Molecular Life Sciences CMLS<\/em>,\u00a0<em>61<\/em>(1), 97-109.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Zona, R., Chang\u2010Pi\u2010Hin, F., O&#8217;Donohue, M. J., &amp; <strong>Jane\u010dek, \u0160. <\/strong>(<strong>2004<\/strong>). Bioinformatics of the glycoside hydrolase family 57 and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis.\u00a0<em>European journal of biochemistry<\/em>,\u00a0<em>271<\/em>(14), 2863-2872.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Machovi\u010d, M., Svensson, B., Ann MacGregor, E., &amp; <strong>Jane\u010dek, \u0160. <\/strong>(<strong>2005<\/strong>). A new clan of CBM families based on bioinformatics of starch\u2010binding domains from families CBM20 and CBM21.\u00a0<em>The FEBS journal<\/em>,\u00a0<em>272<\/em>(21), 5497-5513.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Machovi\u010d, M., &amp; <strong>Jane\u010dek, \u0160. <\/strong>(<strong>2006<\/strong>). Starch-binding domains in the post-genome era.\u00a0<em>Cellular and Molecular Life Sciences CMLS<\/em>,\u00a0<em>63<\/em>(23), 2710-2724.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Machovi\u010d, M., &amp; <strong>Jane\u010dek, \u0160. <\/strong>(2006). The evolution of putative starch-binding domains.\u00a0<em>FEBS letters<\/em>,\u00a0<em>580<\/em>(27), 6349-6356.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Van der Kaaij, R. M., <strong>Jane\u010dek, \u0160.<\/strong>, van der Maarel, M. J. E. C., &amp; Dijkhuizen, L. (<strong>2007<\/strong>). Phylogenetic and biochemical characterization of a novel cluster of intracellular fungal \u03b1-amylase enzymes.\u00a0<em>Microbiology<\/em>,\u00a0<em>153<\/em>(12), 4003-4015.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">God\u00e1ny, A., Vidov\u00e1, B., &amp; <strong>Jane\u010dek, \u0160. <\/strong>(<strong>2008<\/strong>). The unique glycoside hydrolase family 77 amylomaltase from Borrelia burgdorferi with only catalytic triad conserved.\u00a0<em>FEMS microbiology letters<\/em>,\u00a0<em>284<\/em>(1), 84-91.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Christiansen, C., Abou Hachem, M., <strong>Jane\u010dek, \u0160.<\/strong>, Viks\u00f8\u2010Nielsen, A., Blennow, A., &amp; Svensson, B. (<strong>2009<\/strong>). The carbohydrate\u2010binding module family 20\u2013diversity, structure, and function.\u00a0<em>The FEBS journal<\/em>,\u00a0<em>276<\/em>(18), 5006-5029.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Gabri\u0161ko, M., &amp; <strong>Jane\u010dek, \u0160.<\/strong> (<strong>2009<\/strong>). Looking for the ancestry of the heavy\u2010chain subunits of heteromeric amino acid transporters rBAT and 4F2hc within the GH13 \u03b1\u2010amylase family.\u00a0<em>The FEBS journal<\/em>,\u00a0<em>276<\/em>(24), 7265-7278.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160.<\/strong>, &amp; Bles\u00e1k, K. (<strong>2011<\/strong>). Sequence-structural features and evolutionary relationships of family GH57 \u03b1-amylases and their putative \u03b1-amylase-like homologues.\u00a0<em>The protein journal<\/em>,\u00a0<em>30<\/em>(6), 429-435.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160.<\/strong>, Svensson, B., &amp; MacGregor, E. A. (<strong>2011<\/strong>). Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals.\u00a0<em>Enzyme and microbial technology<\/em>,\u00a0<em>49<\/em>(5), 429-440.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Bles\u00e1k, K., &amp; <strong>Jane\u010dek, \u0160.<\/strong> (<strong>2012<\/strong>). Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57.\u00a0<em>Extremophiles<\/em>,\u00a0<em>16<\/em>(3), 497-506.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160.<\/strong>, &amp; Kuchtov\u00e1, A. (<strong>2012<\/strong>). In silico identification of catalytic residues and domain fold of the family GH119 sharing the catalytic machinery with the \u03b1-amylase family GH57.\u00a0<em>FEBS letters<\/em>,\u00a0<em>586<\/em>(19), 3360-3366.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Puspasari, F., Radjasa, O. K., Noer, A. S., Nurachman, Z., Syah, Y. M., van der Maarel, M. J. E. C., <strong>Jane\u010dek, \u0160.<\/strong> &amp; Natalia, D. (<strong>2013<\/strong>). Raw starch\u2013degrading \u03b1\u2010amylase from B acillus aquimaris MKSC 6.2: isolation and expression of the gene, bioinformatics and biochemical characterization of the recombinant enzyme.\u00a0<em>Journal of applied microbiology<\/em>,\u00a0<em>114<\/em>(1), 108-120.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Majzlova, K., Pukajova, Z., &amp; <strong>Jane\u010dek, \u0160. <\/strong>(<strong>2013<\/strong>). Tracing the evolution of the \u03b1-amylase subfamily GH13_36 covering the amylolytic enzymes intermediate between oligo-1, 6-glucosidases and neopullulanases.\u00a0<em>Carbohydrate research<\/em>,\u00a0<em>367<\/em>, 48-57.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Da Lage, J. L., Binder, M., Hua-Van, A., <strong>Jane\u010dek, \u0160.<\/strong>, &amp; Casane, D. (<strong>2013<\/strong>). Gene make-up: rapid and massive intron gains after horizontal transfer of a bacterial \u03b1-amylase gene to Basidiomycetes.\u00a0<em>BMC evolutionary biology<\/em>,\u00a0<em>13<\/em>(1), 1-13.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Blesak, K., &amp; <strong>Jane\u010dek, \u0160. <\/strong>(<strong>2013<\/strong>). Two potentially novel amylolytic enzyme specificities in the prokaryotic glycoside hydrolase \u03b1-amylase family GH57.\u00a0<em>Microbiology<\/em>,\u00a0<em>159<\/em>(Pt_12), 2584-2593.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160.<\/strong>, Svensson, B., &amp; MacGregor, E. A. (<strong>2014<\/strong>). \u03b1-Amylase: an enzyme specificity found in various families of glycoside hydrolases.\u00a0<em>Cellular and molecular life sciences<\/em>,\u00a0<em>71<\/em>(7), 1149-1170.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Ranjani, V., <strong>Jane\u010dek, \u0160.<\/strong>, Chai, K. P., Shahir, S., Rahman, R. N. Z. R. A., Chan, K. G., &amp; Goh, K. M. (<strong>2014<\/strong>). Protein engineering of selected residues from conserved sequence regions of a novel Anoxybacillus \u03b1-amylase.\u00a0<em>Scientific reports<\/em>,\u00a0<em>4<\/em>(1), 1-8.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Kuchtova, A., &amp; <strong>Jane\u010dek, \u0160.<\/strong> (<strong>2015<\/strong>). In silico analysis of family GH77 with focus on amylomaltases from borreliae and disproportionating enzymes DPE2 from plants and bacteria.\u00a0<em>Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics<\/em>,\u00a0<em>1854<\/em>(10), 1260-1268.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160.<\/strong>, &amp; Gabri\u0161ko, M. (<strong>2016<\/strong>). Remarkable evolutionary relatedness among the enzymes and proteins from the \u03b1-amylase family.\u00a0<em>Cellular and Molecular Life Sciences<\/em>,\u00a0<em>73<\/em>(14), 2707-2725.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Kuchtova, A., &amp; <strong>Jane\u010dek, \u0160.<\/strong> (<strong>2016<\/strong>). Domain evolution in enzymes of the neopullulanase subfamily.\u00a0<em>Microbiology<\/em>,\u00a0<em>162<\/em>(12), 2099-2115.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160.<\/strong>, Majzlov\u00e1, K., Svensson, B., &amp; MacGregor, E. A. (<strong>2017<\/strong>). The starch\u2010binding domain family CBM41\u2014An in silico analysis of evolutionary relationships.\u00a0<em>Proteins: Structure, Function, and Bioinformatics<\/em>,\u00a0<em>85<\/em>(8), 1480-1492.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Sarian, F. D., <strong>Jane\u010dek, \u0160.<\/strong>, Pijning, T., Nurachman, Z., Radjasa, O. K., Dijkhuizen, L., &#8230; &amp; van der Maarel, M. J. (<strong>2017<\/strong>). A new group of glycoside hydrolase family 13 \u03b1-amylases with an aberrant catalytic triad.\u00a0<em>Scientific reports<\/em>,\u00a0<em>7<\/em>(1), 1-10.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Kuchtov\u00e1, A., Gentry, M. S., &amp; <strong>Jane\u010dek, \u0160.<\/strong> (<strong>2018<\/strong>). The unique evolution of the carbohydrate\u2010binding module CBM 20 in laforin.\u00a0<em>FEBS letters<\/em>,\u00a0<em>592<\/em>(4), 586-598.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Martinovi\u010dov\u00e1, M., &amp; <strong>Jane\u010dek, \u0160.<\/strong> (<strong>2018<\/strong>). In silico analysis of the \u03b1-amylase family GH57: eventual subfamilies reflecting enzyme specificities.\u00a0<em>3 Biotech<\/em>,\u00a0<em>8<\/em>(7), 1-11.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\">Zhang, X., Leemhuis, H., <strong>Jane\u010dek, \u0160.<\/strong>, Martinovi\u010dov\u00e1, M., Pijning, T., &amp; van der Maarel, M. J. (<strong>2019<\/strong>). Identification of Thermotoga maritima MSB8 GH57 \u03b1-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity.\u00a0<em>Applied microbiology and biotechnology<\/em>,\u00a0<em>103<\/em>(15), 6141-6151.<\/span><\/li>\n\n\n\n<li><span style=\"background-color:rgba(0, 0, 0, 0)\" class=\"has-inline-color has-black-color\"><strong>Jane\u010dek, \u0160.<\/strong>, Mare\u010dek, F., MacGregor, E. A., &amp; Svensson, B. (<strong>2019<\/strong>). Starch-binding domains as CBM families\u2013history, occurrence, structure, function and evolution.\u00a0<em>Biotechnology advances<\/em>,\u00a0<em>37<\/em>(8), 107451.<\/span><\/li>\n<\/ol>\n<\/div>\n<\/div>","protected":false},"excerpt":{"rendered":"<p>vysoko\u0161kolsk\u00fd u\u010dite\u013e Vedecko-pedagogick\u00e1 charakteristika &#8211;\u00a0stiahni PDF Tituly, hodnosti: Pracovisko: Hlavn\u00e9 oblasti vedeck\u00e9ho z\u00e1ujmu: \u0165a\u017eisko pr\u00e1ce je teoretick\u00e9 in silico \u0161t\u00fadium prote\u00ednov &#8211; ich \u0161trukt\u00far vo vz\u0165ahu k ich funkcii, vlastnostiam a evol\u00facii. Hlavn\u00fd z\u00e1ujem je o enz\u00fdmy z alfa-amyl\u00e1zovej rodiny &#8211; v s\u00fa\u010dasnosti v r\u00e1mci klasifik\u00e1cie CAZy (Carbohydrate Active enZymes) ide o rodiny glykozidov\u00fdch hydrol\u00e1z&hellip; <br \/> <a class=\"read-more\" href=\"https:\/\/oddeleniebiologie.sk\/en\/doc-ing-stefan-janecek-drsc\/\">Read more<\/a><\/p>","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"_monsterinsights_skip_tracking":false,"ngg_post_thumbnail":0,"footnotes":""},"class_list":["post-1096","page","type-page","status-publish","hentry"],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v28.5 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>prof. Ing. \u0160tefan Jane\u010dek, DrSc. - oddeleniebiologie.sk<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/oddeleniebiologie.sk\/en\/doc-ing-stefan-janecek-drsc\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"prof. Ing. \u0160tefan Jane\u010dek, DrSc. - oddeleniebiologie.sk\" \/>\n<meta property=\"og:description\" content=\"vysoko\u0161kolsk\u00fd u\u010dite\u013e Vedecko-pedagogick\u00e1 charakteristika &#8211;\u00a0stiahni PDF Tituly, hodnosti: Pracovisko: Hlavn\u00e9 oblasti vedeck\u00e9ho z\u00e1ujmu: \u0165a\u017eisko pr\u00e1ce je teoretick\u00e9 in silico \u0161t\u00fadium prote\u00ednov &#8211; ich \u0161trukt\u00far vo vz\u0165ahu k ich funkcii, vlastnostiam a evol\u00facii. Hlavn\u00fd z\u00e1ujem je o enz\u00fdmy z alfa-amyl\u00e1zovej rodiny &#8211; v s\u00fa\u010dasnosti v r\u00e1mci klasifik\u00e1cie CAZy (Carbohydrate Active enZymes) ide o rodiny glykozidov\u00fdch hydrol\u00e1z&hellip; Read more\" \/>\n<meta property=\"og:url\" content=\"https:\/\/oddeleniebiologie.sk\/en\/doc-ing-stefan-janecek-drsc\/\" \/>\n<meta property=\"og:site_name\" content=\"oddeleniebiologie.sk\" \/>\n<meta property=\"article:modified_time\" content=\"2023-10-26T12:21:21+00:00\" \/>\n<meta property=\"og:image\" content=\"http:\/\/oddeleniebiologie.sk\/wp-content\/uploads\/2021\/08\/Stefan_Janecek-1.jpg\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:label1\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data1\" content=\"10 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\\\/\\\/schema.org\",\"@graph\":[{\"@type\":\"WebPage\",\"@id\":\"https:\\\/\\\/oddeleniebiologie.sk\\\/doc-ing-stefan-janecek-drsc\\\/\",\"url\":\"https:\\\/\\\/oddeleniebiologie.sk\\\/doc-ing-stefan-janecek-drsc\\\/\",\"name\":\"prof. 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Hlavn\u00fd z\u00e1ujem je o enz\u00fdmy z alfa-amyl\u00e1zovej rodiny &#8211; v s\u00fa\u010dasnosti v r\u00e1mci klasifik\u00e1cie CAZy (Carbohydrate Active enZymes) ide o rodiny glykozidov\u00fdch hydrol\u00e1z&hellip; Read more","og_url":"https:\/\/oddeleniebiologie.sk\/en\/doc-ing-stefan-janecek-drsc\/","og_site_name":"oddeleniebiologie.sk","article_modified_time":"2023-10-26T12:21:21+00:00","og_image":[{"url":"http:\/\/oddeleniebiologie.sk\/wp-content\/uploads\/2021\/08\/Stefan_Janecek-1.jpg","type":"","width":"","height":""}],"twitter_card":"summary_large_image","twitter_misc":{"Est. reading time":"10 minutes"},"schema":{"@context":"https:\/\/schema.org","@graph":[{"@type":"WebPage","@id":"https:\/\/oddeleniebiologie.sk\/doc-ing-stefan-janecek-drsc\/","url":"https:\/\/oddeleniebiologie.sk\/doc-ing-stefan-janecek-drsc\/","name":"prof. 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