Ing. Eva Kutejová, DrSc.

vedúca oddelenia

ATP-závislé proteázy a šaperóny v mitochondriách

Mitochondrie zohrávajú dôležitú úlohu vo viacerých bunkových funkciách, vrátane bunkovej diferenciácie a procesoch bunkovej smrti. Nesprávna funkcia mitochondrií preto môže prispievať k starnutiu a patogenéze neurodegeneratívnych ochorení a rakoviny. Mitochondriálne proteázy a šaperóny riadia kľúčové kroky mitochondriálnej biogenézy skladaním a proteolytickým spracovaním viacerých regulačných proteínov. Náš výskum sa zameriava na biochemickú, molekulárnu a štrukturálnu analýzu vlastností mitochondriálnych šaperónov a ATP-závislých AAA proteáz, kontrolu zostavovania komplexu nukleoidu, proteolytické procesy regulujúce mitochondriálnu dynamiku a štúdium vplyvu post-translačných modifikácií proteínov (sukcinylácia, fosforylácia) na homeostázu mitochondrií pomocou kvasinky Saccharomyces cerevisiae a ľudských buniek ako modelových organizmov.

Septíny - bunkové delenie

Naša práca sa tiež zameriava na mechanizmy regulácie bunkového delenia v kvasinke S. cerevisiae. Septíny sú konzervované guanozín fosfát viažuce proteíny, zapojené do cytokinézy a procesov remodulujúcich membrány. Cieľom projektu je vysvetliť ako špecifické proteín-proteínové interakcie a posttranslačné modifikácie indukujú zmeny v polymerizácii septínových filamentov, alebo v skladaní štruktúr vyššieho poriadku in vivo.

Štúdium mitofágie a apoptózy

V našej práci využívame kvasinku S. cerevisiae ako modelový eukaryotický organizmus pri hľadaní odpovede na otázku ako Mmi1/TCTP proteíny interagujú s mitochondriami a regulujú mitofágiu daných organel a apoptózu.

Laboratórium evolúcie proteínov sa venuje základnému výskumu v oblasti bioinformatiky proteínov. Zamerané je na teoretické štúdium proteínov na molekulárnej úrovni, t.j. porovnávať primárne a terciárne štruktúry proteínov a vyvodzovať vzájomné vzťahy medzi sekvenciou, štruktúrou a evolúciou na jednej strane, a funkciou, špecificitou a stabilitou na strane druhej. Cieľom je - v rámci spolupráce s experimentálnymi prístupmi - proteínové inžinierstvo a dizajn. V centre pozornosti sú enzýmy hydrolyzujúce škrob a príbuzné oligo- a polysacharidy, najmä z alfa-amylázových rodín (približne 30 rôznych enzýmových špecificít), ktoré sú v súčasnosti klasifikované v systéme CAZy (Carbohydrate-Active Enzymes) do rodín glykozidových hydroláz GH13, GH57, GH119 a prípadne aj GH126. Záujem je aj o funkčne a evolučne príbuzné enzýmy z rodín GH70, GH77 a GH31, ako aj o škrob-viažuce domény z tzv. CAZy CBM rodín.

Štefan Janeček patrí k priekopníkom bioinformatického, t.j. in silico, prístupu k štúdiu proteínov na Slovensku. Tomuto vedeckému smeru sa venuje nepretržite už 30 rokov, pričom 20 rokov odovzdáva svoje skúsenosti aj študentom ako vysokoškolský pedagóg na Fakulte prírodných vied UCM v Trnave. Publikoval ~100 WoS/Scopus publikácií, ktoré dosiahli viac než 3000 WOS-SCI citácií. Vychoval 7 úspešne obhájených PhD-študentov. Je zakladateľom a hlavným organizátorom série medzinárodných sympózií o enzýmoch z alfa-amylázovej rodiny - ALAMYs, konaných od roku 2001 tradične na Smolenickom zámku na Slovensku. V roku 2016 založil medzinárodný "open-access" vedecký časopis Amylase. Je aj jedným z kurátorov a spoluautorov internetovej encyklopédie pre enzýmy aktívne voči sacharidom CAZypedia.

Správne fungovanie fyziologických procesov si vyžaduje dobre nastavenie citlivosti bunkových odpovedí. Tie zahŕňajú vzájomné interakcie mimobunkových rozpustných ligandov s receptormi na povrchu buniek a ich presné naviazanie na vnútrobunkové signalizačné kaskády. Strata kontroly nad týmito molekulovými vzťahmi vedie k rozličným ochoreniam. Napríklad k nádorovej transformácii či poruchám imunity.

Imunitné bunky vrodenej aj adaptívnej línie imunitného systému, ako sú T bunky, B bunky, makrofágy či dendritické bunky, sú neustále vystavované množstvu stimulov a musia sa v okamihu rozhodnúť medzi vlastným a cudzím, neškodným a nebezpečným, a teda medzi voľbou tolerovať či odpovedať. Mnoho molekulových mechanizmov v tom zohráva dôležitú úlohu .

V našom laboratóriu študujeme vzťahy bunkových receptorov a ich zodpovedajúcich ligandov a signalizačných molekúl a ich funkcie pre správne nastavenie imunity. Sústredíme sa najmä na molekuly nevyhnutné pre transport proteínov, tzv. prenášače. Naše doterajšie výsledky výrazne poukazujú na úlohu pre Manóza 6-fosfátový receptor (CD222) v regulácii rozličných bunkových odpovedí, a to nielen imunitných buniek, napríklad proteolýzy, migrácie, prenosu signálu cez membránu, či endocytóze. Naším cieľom je odhaliť, akú špecifickú úlohu zohráva tento endozómový prenášač proteínov, a transport proteínov vôbec, pri imunitných odpovediach v zdraví, ale aj v rôznych chorobách. Naším dlhodobým cieľom je ponúknuť farmakologické nástroje na úpravu týchto odpovedí, ak je ich rovnováha porušená. Naše laboratórium úzko spolupracuje s Oddelením molekulárnej imunológie na Inštitúte hygieny a aplikovanej imunológie na Medickej Univerzite vo Viedni. Viac informácií o našich spoločných projektoch je možné nájsť tiež tu.

Transportéry neurotransmiterov sú membránové proteíny, príbuzensky zoskupené do rodiny: sodium/chloride dependent transporters solute carrier 6 (SLC6). Udržiavajú správnu koncentráciu viacerých neurotransmiterov a ich poruchy možu mať za následok vážne ochorenia. Zatiaľ čo značne štruktúrne konzervované jadro molekúl transportérov sa počas fylogenézy veľmi nezmenilo, málo sa vie o štruktúre a funkcii cytoplazmatických úsekov transportérov. Tieto úseky sa priamo nezúčastňujú transportu, obsahujú však viaceré regulačné signály ovplyvňujúce výslednú výkonnosť transportéra.

Naše laboratórium v predchádzajúcej práci zistilo že viaceré transportéry sú substráty vápnikovo závislej proteázy kalpain. Či toto proteolytické skrátenie transportérov predstavuje nový spôsob ich regulácie naďalej skúmame. Naše posledné experimenty ukázali, že N-terminálne konce glycínových transportérov vykazujú atypickú dynamickú interakciu s Coomassie Brilliant Blue, čo naznačuje ich vysokú flexibilitu a neštrukturovaný character, ktorý sme nezávisle potvrdili cirkulárnym dichroizmom týchto proteínov.

Glycínový transporter GlyT1  je v mozgu často kolokalizovaný s NMDA receptorom a pretože NMDA receptor používa glycín ako koagonist, GlyT1 zohráva dôležitú úlohu v jeho regulácii. V našom laboratóriu sme zistili že benzofenantridínove alkaloidy inhibujú GlyT1 v mikromolárnej koncentrácii a identifikovali sme tiež ich potenciálne väzbové vrecko. Aj keď tieto alkaloidy vykazujú široké spectrum aktivít a výsledok má predovšetkým toxikologický význam, optimalizácia famakoforu može viesť k inhibítorom s väčšou špecificitou pre GlyT1.  NMDA receptor sa zúčastňuje regulácie vyššej nervovej činnosti, pamäti a prenosu signálu bolesti, preto inhibítory GlyT1 možu predstavovať potenciálne významné liečivá ovplyvňujúce tieto procesy.

Transportéry neurotransmiterov nesú na svojom C-terminálnom konci tzv. PDZ viažúci motív. V našej nedávno publikovanej práci sme zistili, že motívy viacerých transportérov interagujú in vitro s PDZ doménami multi-PDZ signálneho proteínu MUPP1. Tieto interakcie odhalili viaceré 3D podobnosti PDZ motívov transportérov, ktoré by nebolo možné získať z ich primárnych aminokyselinových sekvencií. 

Pracovná skupina proteínovej kryštalografie a molekulovej dynamiky sa venuje dvom zásadným projektom:

• Štúdium štruktúry a funkcie ľudského ryanodínového receptora 2
• Štúdium štruktúry a funkcie priemyselne zaujímavých enzýmov využívaných v biosenzoroch

Obidva projekty sú riešené multidisciplinárnym prístupom, ktorý spája spája predovšetkým in vitro laboratórne experimenty s in silico prístupom s cieľom získania komplexného pohľadu na danú problematiku.

Štúdium štruktúry a funkcie ľudského ryanodínového receptora 2

 Pravidelná srdcová činnosť je jednou zo základných fyziologických funkcií nevyhnutných pre život človeka. Bielkovina, ktorá zohráva v tomto procese kľúčovú úlohu je ryanodínový receptor 2 (hRyR2), ktorý je exprimovaný predovšetkým v myokarde. Je to doteraz najväčší známy vápnikový kanál, ktorý sprostredkováva uvoľnenie vápnika zo sarkoplazmatického retikula do cytoplazmy. Zvýšenie koncentrácie Ca²⁺ v cytoplzme myocytov spôsovuje kaskádu reakcií, ktoré podmienňujú pravidelnú srdcovú činnosť. Nesprávna funkcia RyR2 kanála u človeka spôsobuje závažné srdcové ochorenia - arytmie (CPVT1, ARVC/D2, SIDS, SUO). Nedávno bola zistená dysfunkcia hRyR2 aj v súvislosti s rakovinou hrubého čreva.

 V našom laboratóriu sa venujeme štúdiu štruktúry a funkcie hRyR2 využitím bioinformatiky, proteomiky, molekulárnej a štruktúrnej biológie a biofyziky. Dôležitým míľnikom na tejto ceste bolo určenie štruktúry N-terminálnej domény hRyR2 pomocou RTG-štruktúrnej a SAXS a analýzy. Okrem toho sme pripravili a charakterizovali viaceré mutanty v tejto domény, ktoré sú asociované s vyššie uvedenými ochoreniami. Taktiež sa zaoberáme vplyvom dantrolénu - svalového relaxantu štandartne využívaného pri liečbe malígnej hypertermie, a jeho väzbou na hRyR2.

Štúdium štruktúry a funkcie priemyselne zaujímavých enzýmov využívaných v biosenzoroch

Tento projekt sa zaoberá predovšetkým enzýmom glukózooxidáza (GOx), ktorý štiepi glukózu na glukónolaktón a peroxid vodíka. Pre výnimočnú rýchlosť štiepenia bola GOx označená aj ako Ferari oxidáčno-redukčných enzýmov. V našom laboratóriu sme určili terciárnu štruktúru GOx v natívnej aj mutovanej forme a zaoberáme sa vplyvom rôznych modulátorov na jej stabilitu a aktivitu.

Zoznam pracovníkov

Medzinárodná vedecká spolupráca

1. BioChemoInformatics Unit, Institute of Organic Synthesis and Photoreactivity, National Research Council , Bologna, Taliansko
2. Biofyzikální chemie a molekulární onkologie Biofyzikální ústav Akademie věd České republiky, v.v.i. , Brno, Česká republika
3. Cardiff University School of Dentistry, Cardiff, Spojené kráľovstvo
4. Chemistry & Biochemistry Department at University of California, Los Angeles, Los Angeles, USA
5. Department for Structural and Computational Biology, Max Perutz Labs, Vienna, Rakúsko
6. Department of Chemistry, University of York, York, Spojené kráľovstvo
7. Department of Dermatology, Medical University of Vienna, Vienna, Rakúsko
8. Dr. Dessy Natalia, Biochemistry Research Division, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Bandung, Indonézia
9. Dr. Jean-Luc Da Lage, Laboratoire Evolution, Génomes Comportement, Ecologie, CNRS, Université Paris Sud, Gif sur Yvette, Francúzko
10. Dr. Kian Mau Goh, Department of Biosciences and Health Sciences, Universiti Teknologi Malaysia, Johor Bahru, Malajzia
11. Dr. Natasa Bozic, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Belgrade, Srbsko
12. Dr. Paweł Filipkowski, Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdansk, Poľsko
13. Institute of Cellular Biology and Pathology, 1st Faculty of Medicine, Charles University in Prague, Prague, Česká republika
14. Laboratory of Molecular Immunology, Institute of Molecular Genetics, AS CR, Praha, Česká republika
15. Microbiological Institute, Academy of Sciences of Czech Republic, Prague, Česká republika
16. Molecular Immunology Unit, Institute for Hygiene and Applied Immunology, Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Rakúsko
17. National Centre for Biomolecular Research, Masaryk University, Brno, Česká republika
18. Prof. Birte Svensson, Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Kgs. Lyngby - Copenhagen, Dánsko
19. Prof. Marc J.E.C. van der Maarel, Department Aquatic Biotechnology and Bioproduct Engineering, University of Groningen, Groningen, Holandsko

Riešené projekty

• Covid-19 a dlhý covid na molekulárnej úrovni - biomarkery, nástroje a ciele pre diagnostiku a terapiu.
  (09I03-03-V02-00047, Sep 2023 - Aug 2027)
  Zodpovedný riešiteľ: Vladimír Leksa
• Dvojsečný meč plazminogénového systému: Od udržiavania homeostázy po COVID-19.
  (APVV-20-0513, Aug 2021 - Jun 2025)
  Zodpovedný riešiteľ: Vladimír Leksa
• Interakcia proteínu Mmi1/TCTP s mitochondriami.
  (SK-CZ-RD-21-0104, Jul 2022 - Jun 2025)
  Zodpovedný riešiteľ: Vladimír Pevala
• Laktoferín a laktofericín ako prirodzené inhibítory plazmínu: Od určenia štruktúry po terapeutické aplikácie.
  (2/0152/21, Jan 2021 - Dec 2024)
  Zodpovedný riešiteľ: Vladimír Leksa
• Regulácia interakčnej špecificity multi-PDZ proteínov..
  (2/0127/21, Jan 2021 - Dec 2024)
  Zodpovedný riešiteľ: Martina Baliová
• Štipendiá pre excelentných výskumníkov ohrozených vojnovým konfliktom na Ukrajine .
  (09I03-03-V01-00113, Jan 2023 - Dec 2025)
  Zodpovedný riešiteľ: Tetiana Moskalets
• Vzájomná inerakcia proteáz, šaperónov a kináz v mitochodriách pri strese spôsobenom patologickými stavmi.
  (APVV-19-0298, Jul 2000 - Jun 2024)
  Zodpovedný riešiteľ: Eva Kutejová

Vybrané publikácie

1. Kunova, N., Ondrovicova, G., Bauer, J., Krajcovicova, V., Pinkas, M., Stojkovicova, B., Havalova, H., Lukacova, V., Kohutova, L., Kostan, J., Martinakova, L., Barath, P., Kereiche, S., Kutejova, E., Pevala, V.
   Polyphosphate and tyrosine phosphorylation in the N-terminal domain of the human mitochondrial Lon protease disrupts its functions.
   (2024) Sci Rep 1: 1-.
2. Photenhauer, A.L., Villafuerte-Vega, R.C., Cerqueira, F.M., Armbruster, K.M., Marecek, F., Chen, T., Wawrzak, Z., Hopkins, J.B., Vander Kooi, C.W., Janecek, S., Ruotolo, B.T., Koropatkin, N.M.
   The Ruminococcus bromii amylosome protein Sas6 binds single and double helical alpha-glucan structures in starch.
   (2024) Nat. Struct. Mol. Biol. 31(2): 255-265.
3. Baliova, M., Jahodová, I., Jursky, F.
   A Significant Difference in Core PDZ Interactivity of SARS-CoV, SARS-CoV2 and MERS-CoV Protein E Peptide PDZ Motifs In Vitro.
   (2023) Protein J. 42: 253-262.
4. Jahodová, I., Baliova, M., Jursky, F.
   PDZ interaction of the GABA transporter GAT1 with the syntenin-1 in Neuro-2a cells..
   (2023) Neurochem. Int. 165: 105522-.
5. Janecek, S., Brumer, H., Henrissat, B.
   News, trends, and challenges in Carbohydrate-Active enZymes.
   (2023) Biologia 78(7): 1739-1740.
6. Janecek, S.
   Advances in amylases - what's going on?.
   (2023) Molecules 28: 7268-.
7. Leksa, V.
   Milky way of immunity - galactic functions of lactoferrin in host defence (meeting abstract).
   (2023) Eur. J. Immunol. 53(SI): 48-48.
8. Magyar, Z.E., Bauer, J., Bauerova-Hlinkova, V., Jóna, I., Gaburjakova, J., Gaburjakova, M., Almássy, J.
   Eu3+ detects two functionally distinct luminal Ca2+ binding sites in ryanodine receptors.
   (2023) Biophys. J. 122(17): 3516-3531.
9. Meskova, K., Martonova, K., Hrasnova, P., Sinska, K., Skrabanova, M., Fialova, L., Njemoga, S., Cehlar, O., Parmar, O., Kolenko, P., Pevala, V., Skrabana, R.
   Cost-Effective Protein Production in CHO Cells Following Polyethylenimine-Mediated Gene Delivery Showcased by the Production and Crystallization of Antibody Fabs.
   (2023) Antibodies 12: 51-.
10. Ohradanova-Repic, A., Praženicová, R., Gebetsberger, L., Moskalets, T., Skrabana, R., Cehlar, O., Tajti, G., Stockinger, H., Leksa, V.
    Time to Kill and Time to Heal: The Multifaceted Role of Lactoferrin and Lactoferricin in Host Defense.
    (2023) Pharmaceutics 15(4): 1056-.
11. Polacek, A., Janecek, S.
    Sequence-structural features and evolution of the alpha-amylase family GH119 revealed by the in silico analysis of its relatedness to the family GH57.
    (2023) Biologia 78(7): 1847-1860.
12. Stastny, D., Petriskova, L., Tahotna, D., Bauer, J., Pokorna, L., Holic, R., Valachovic, M., Pevala, V., Cockroft, S., Griac, P.
    Yeast Sec14-like lipid transfer proteins Pdr16 and Pdr17 bind and transfer lanosterol in addition to phosphatidylinositol.
    (2023) FEBS Lett. 597(4): 504-514.
13. Wang, Y., Wu, Y., Christensen, S.J., Janecek, S., Bai, Y., Moeller, M.S., Svensson, B.
    Impact of starch binding domain fusion on activities and starch product structure of 4-alpha-glucanotransferase.
    (2023) Molecules 28: 1320-.
14. Bauer, J., Zamocka, M., Majtan, J., Bauerova-Hlinkova, V.
    Glucose Oxidase, an Enzyme "Ferrari": Its Structure, Function, Production and Properties in the Light of Various Industrial and Biotechnological Applications.
    (2022) Biomolecules 12: 472-.
15. Janecek, S., Svensson, B.
    How many alpha-amylase GH families are there in the CAZy database?.
    (2022) Amylase 6: 1-10.
16. Kunova, N., Havalova, H., Ondrovicova, G., Stojkovicova, B., Bauer, J., Bauerova-Hlinkova, V., Pevala, V., Kutejova, E.
    Mitochondrial processing peptidases - structure, function and the role in human diseases.
    (2022) Int J Mol Sci 23(3): 1-24.
17. Marecek, F., Janecek, S.
    A novel subfamily GH13_46 of the alpha-amylase family GH13 represented by the cyclomaltodextrinase from Flavobacterium sp. No. 92.
    (2022) Molecules 27: 8735-.
18. Ohradanova-Repic, A., Skrabana, R., Gebetsberger, L., Tajti, G., Barath, P., Ondrovicova, G., Praženicová, R., Jantova, N., Hrasnova, P., Stockinger, H., Leksa, V.
    Blockade of TMPRSS2-mediated priming of SARS-CoV-2 by lactoferricin.
    (2022) Front Immunol Aug 23;13(958581): online-.
19. Bauer, J., Žoldák, G.
    Interpretation of Single-Molecule Force Experiments on Proteins Using Normal Mode Analysis.
    (2021) Nanomaterials 11: 2795-.
20. Frankovsky, J., Keresztesova, B., Bellova, J., Kunova, N., Canigova, N., Hanakova, K., Bauer, J., Ondrovicova, G., Lukacova, V., Sivakova, B., Zdrahal, Z., Pevala, V., Prochazkova, K., Nosek, J., Kutejova, E.
    The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids.
    (2021) J. Biol. Chem. 297 (4): 1-16.
21. Havalova, H., Ondrovicova, G., Keresztesova, B., Bauer, J., Pevala, V., Kutejova, E., Kunova, N.
    Mitochondrial HSP70 Chaperone System - The Influence of Post-Translational Modifications and Involvement in Human Diseases.
    (2021) Int J Mol Sci 22(15): 8077-.
22. Janickova, Z., Janecek, S.
    In silico analysis of fungal and chloride-dependent alpha-amylases within the family GH13 with identification of possible secondary surface-binding sites.
    (2021) Molecules 26: 5704-.
23. Kotrasova, V., Keresztesova, B., Ondrovicova, G., Bauer, J., Havalova, H., Pevala, V., Kutejova, E., Kunova, N.
    Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease.
    (2021) LIFE-BASEL 11: 82-.
24. Leitner, J., Mahasongkram, K., Schatzlmaier, P., Pfisterer, K., Leksa, V., Pata, S., Kasinrerk, W., Stockinger, H., Steinberger, P.
    Differentiation and activation of human CD4 T cells is associated with a gradual loss of myelin and lymphocyte protein.
    (2021) Eur. J. Immunol. 51 (4): 848-863.
25. Marecek, F., Moeller, M.S., Svensson, B., Janecek, S.
    A putative novel starch-binding domain revealed by in silico analysis of the N-terminal domain in bacterial amylomaltases from the family GH77.
    (2021) 3 Biotech 11: 229-.
26. Urban, J., Suchankova, M., Ganovska, M., Leksa, V., Sandor, F., Tedlova, E., Konig, B., Bucova, M.
    The Role of CX3CL1 and ADAM17 in Pathogenesis of Diffuse Parenchymal Lung Diseases.
    (2021) Diagnostics 11(6): 1074-.
27. Urbanikova, L.
    CE16 acetylesterases: in silico analysis, catalytic machinery prediction and comparison with related SGNH hydrolases.
    (2021) 3 Biotech 11: 84-.
28. Baliova, M., Jursky, F.
    Comparison of SynCAM1/CADM1 PDZ interactions with MUPP1 using mammalian and bacterial pull-down systems.
    (2020) Brain Behav. 10: e01587-.
29. Baliova, M., Jursky, F.
    Phosphomimetic Mutation of Glycine Transporter GlyT1 C-Terminal PDZ Binding Motif Inhibits its Interactions with PSD95.
    (2020) J. Mol. Neurosci. 70: 488-493.
30. Baliova, M., Jursky, F.
    Phosphorylation of Serine 157 Protects the Rat Glycine Transporter GlyT2 from Calpain Cleavage.
    (2020) J. Mol. Neurosci. 70: 1216-1224.
31. Bauer, J., Borko, L., Pavlovič, J., Kutejova, E., Bauerova-Hlinkova, V.
    Disease-Associated Mutations Alter the Dynamic Motion of the N-terminal Domain of the Human Cardiac Ryanodine Receptor.
    (2020) J. Biomol. Struct. Dyn. 38: 1054-1070.
32. Bauerova-Hlinkova, V., Hajdúchová, D., Bauer, J.
    Structure and Function of the Human RyanodineReceptors and Their Association withMyopathies?Present State, Challenges,and Perspectives.
    (2020) Molecules 25: 4040-.
33. Farkasovsky, M.
    Septin architecture and function in budding yeast.
    (2020) Biol. Chem. 401: 903-919.
34. Gabrisko, M.
    The in silico characterization of neutral alpha-glucosidase C (GANC) and its evolution from GANAB.
    (2020) Gene 726: 144192-.
35. Gulshan Ara, K.Z., Manberger, A., Gabrisko, M., Linares-Pasten, J.A., Jasilionis, A., Fridjonsson, O.H., Hreggvidsson, G.O., Janecek, S., Nordberg Karlsson, E.
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54. Kuchtova, A., Gentry, M.S., Janecek, S.
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55. Kutejova, E.
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57. Martinovicova, M., Janecek, S.
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60. Vicikova, K., Petrovcikova, E., Manka, P., Drach, J., Stockinger, H., Leksa, V.
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61. Zwirzitz, A., Reiter, M., Skrabana, R., Ohradanova-Repic, A., Majdic, O., Gutekova, M., Cehlar, O., Petrovcikova, E., Kutejova, E., Stanek, G., Stockinger, H., Leksa, V.
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65. Leksa, V., Ilkova, A., Vicikova, K., Stockinger, H.
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66. Mieog, J.C., Janecek, S., Ral, J.P.
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67. Sarian, F.D., Janecek, S., Pijning, T., Ihsanawati, -., Nurachman, Z., Radjasa, O.K., Dijkhuizen, L., Natalia, D., van der Maarel, M.J.
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68. Zamocky, M., Janecek, S., Obinger, C.
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69. Janecek, S., Gabrisko, M.
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70. Janecek, S., Svensson, B.
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71. Juhasova, A., Baliova, M., Jursky, F.
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72. Kereiche, S., Kovacik, L., Bednar, J., Pevala, V., Kunova, N., Ondrovicova, G., Bauer, J., Ambro, L., Bellova, J., Kutejova, E., Raska, I.
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73. Kuchtova, A., Janecek, S.
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74. Machacek, C., Supper, V., Leksa, V., Mitulovic, G., Spittler, A., Drbal, K., Suchanek, M., Ohradanova-Repic, A., Stockinger, H.
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75. Pevala, V., Truban, D., Bauer, J., Kostan, J., Kunova, N., Bellova, J., Brandstetter, M., Marini, V., Krejci, L., Tomaska, L., Nosek, J., Kutejova, E.
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76. Supper, V., Schiller, H.B., Paster, W., Forster, F., Boulegue, C., Mitulovic, G., Leksa, V., Ohradanova-Repic, A., Machacek, C., Schatzlmaier, P., Zlabinger, G.J., Stockinger, H.
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77. Baliova, M., Juhasova, A., Jursky, F.
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78. Halgasova, N., Solteszova, B., Pevala, V., Kostan, J., Kutejova, E., Bukovska, G.
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79. Janecek, S., Kuchtova, A., Petrovicova, S.
    A novel GH13 subfamily of alpha-amylases with a pair of tryptophans in the helix alpha3 of the catalytic TIM-barrel, the LPDlx signature in the conserved sequence region V and a conserved aromatic motif at the C-terminus.
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80. Jursky, F., Baliova, M., Juhasova, A.
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81. Kuchtova, A., Janecek, S.
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82. Schilter, H., Cantemir-Stone, C.Z., Leksa, V., Ohradanova-Repic, A., Findlay, A.D., Deodhar, M., Stockinger, H., Song, X., Molloy, M., Marsh, C.B., Jarolimek, W.
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85. Bauer, J., Ondrovicova, G., Najmanova, L., Pevala, V., Kamenik, Z., Kostan, J., Janata, J., Kutejova, E.
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90. Majzlova, K., Janecek, S.
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91. Mihalikova, A., Baliova, M., Jursky, F.
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102. Majzlova, K., Pukajova, Z., Janecek, S.
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110. Jung, T.Y., Li, D., Park, J.T., Yoon, S.M., Tran, P.L., Oh, B.H., Janecek, S., Park, S.G., Woo, E.J., Park, K.H.
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