Biochémia a štruktúra proteínov
Ing. Eva Kutejová, DrSc. (vedúca pracovnej skupiny)
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.
Evolúcia proteínov
prof. Ing. Štefan Janeček, DrSc. (vedúci pracovnej skupiny)
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.
Molekulárna imunológia
Mgr. Vladimír Leksa, PhD. (vedúci pracovnej skupiny)
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.
Neurobiológia
RNDr. František Jurský, CSc. (vedúci pracovnej skupiny)
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.
Proteínová kryštalografia a molekulová dynamika
Dr. Jacob Bauer, PhD. (vedúci pracovnej skupiny)
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
Vedeckí a odborní pracovníci: prof. Ing. Štefan Janeček, DrSc. Ing. Eva Kutejová, DrSc. Dr. Jacob Bauer, PhD. prof. RNDr. Tetiana Moskalets, PhD.
Dr. Magda Suchánková, PhD.
Mgr. Vladena Bauerová, PhD. Mgr. Nina Kunová, PhD. RNDr. Vladimír Pevala, PhD. RNDr. František Jurský, CSc. RNDr. Ľubica Urbániková, CSc. Ing. Gabriela Ondrovičová, PhD. Mgr. Vladimír Leksa, PhD. Mgr. Martina Baliová, PhD. RNDr. Marian Farkašovský, CSc. Mgr. Henrieta Havalová, PhD. Mgr. Marek Gabriško, PhD. Mgr. Filip Mareček, PhD. Mgr. Barbora Stojkovičová, PhD. Mgr. Michaela Schorschová Mgr. Lucia MartinákováDoktorandi: Mgr. Iveta Jahodová Mgr. Adam Poláček Mgr. Martin Labuda Mgr. Terézia HromádkováDiplomanti: Bc. Michaela Gernátová
Bc. Matej Šmelko
Medzinárodná vedecká spolupráca
- BioChemoInformatics Unit, Institute of Organic Synthesis and Photoreactivity, National Research Council , Bologna, Taliansko
- Biofyzikální chemie a molekulární onkologie
Biofyzikální ústav Akademie věd České republiky, v.v.i.
, Brno, Česká republika
- Cardiff University School of Dentistry, Cardiff, Spojené kráľovstvo
- Chemistry & Biochemistry Department at University of California, Los Angeles, Los Angeles, USA
- Department for Structural and Computational Biology, Max Perutz Labs, Vienna, Rakúsko
- Department of Chemistry, University of York, York, Spojené kráľovstvo
- Department of Dermatology, Medical University of Vienna, Vienna, Rakúsko
- Dr. Dessy Natalia, Biochemistry Research Division, Faculty of Mathematics and Natural Sciences, Institut Teknologi Bandung, Bandung, Indonézia
- Dr. Jean-Luc Da Lage, Laboratoire Evolution, Génomes Comportement, Ecologie, CNRS, Université Paris Sud, Gif sur Yvette, Francúzko
- Dr. Kian Mau Goh, Department of Biosciences and Health Sciences, Universiti Teknologi Malaysia, Johor Bahru, Malajzia
- Dr. Natasa Bozic, Institute of Chemistry, Technology and Metallurgy, University of Belgrade, Belgrade, Srbsko
- Dr. Paweł Filipkowski, Department of Food Chemistry, Technology and Biotechnology, Faculty of Chemistry, Gdansk University of Technology, Gdansk, Poľsko
- Institute of Cellular Biology and Pathology, 1st Faculty of Medicine, Charles University in Prague, Prague, Česká republika
- Laboratory of Molecular Immunology, Institute of Molecular Genetics, AS CR, Praha, Česká republika
- Microbiological Institute, Academy of Sciences of Czech Republic, Prague, Česká republika
- Molecular Immunology Unit, Institute for Hygiene and Applied Immunology,
Center for Pathophysiology, Infectiology and Immunology, Medical University of Vienna, Vienna, Rakúsko
- National Centre for Biomolecular Research, Masaryk University, Brno, Česká republika
- Prof. Birte Svensson, Enzyme and Protein Chemistry, Department of Systems Biology, Technical University of Denmark, Kgs. Lyngby - Copenhagen, Dánsko
- 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
- Účinok patologických mutácií a posttranslačných modifikácií na funkcie mitochondriálnej procesujúcej peptidázy nevyhnutnej pre transport do mitochondrií.
(APVV-23-0407, Jul 2024 - Jun 2028)
Zodpovedný riešiteľ: Eva Kutejová
- Úloha ľudskej mitochondriálnej LON proteázy v prejavoch syndrómu CODAS.
(09I03-03-V04-00580, Sep 2024 - Aug 2026)
Zodpovedný riešiteľ: Nina Kunová
- Úloha mitochondriálnej proteázy Lon a fosforylácie proteínov mitochondriálneho nukleoidu v homeostáze a udržiavaní mtDNA.
(2/0069/23, Jan 2023 - Dec 2026)
Zodpovedný riešiteľ: Eva Kutejová
Vybrané publikácie
- Babulic, P., Cehlar, O., Ondrovicova, G., Moskalets, T., Skrabana, R., Leksa, V.
Lactoferrin Binds Through its N-terminus to the Receptor-binding Domain of the SARS-CoV-2 Spike Protein.
(2024) Pharmaceuticals 17(8): 1021-1033.
- Baliova, M., Jursky, F.
Manganese- and zinc-coordinated interaction of Schistosoma japonicum glutathione S-transferase with neurotransmitter transporters GlyT1 and GAT3 in vitro.
(2024) Exp. Parasitol. 259: 108721-.
- Baliova, M., Jursky, F.
Correlation of calpain sensitivity, Bradford assay instability, and electrophoretic mobility in phosphomimetic mutants of GlyT2 N-terminus.
(2024) Biochem. Biophys. Rep. 38: 101734-.
- Baliova, M., Jursky, F.
Common structural features in some of the sequentially distant neurotransmitter transporters N-termini .
(2024) J. Struct. Biol. 216: 108137-.
- Hodorova, M., Janecek, S.
The family GH126 - its relatedness to and differentiation from GH8 and GH48 including the intermediary sequences.
(2024) Food Biosci. 62: 105064-.
- 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 14: 9923-.
- Leksa, V.
Piccadilly full of people and otherfoul things: On heroism and perversion in the post-pandemic era.
(2024) EMBO Rep. 25(6): 2520-2524.
- Leksa, V.
And the stars look down: science beyond the finite: From prehistorical science to postscience.
(2024) EMBO Rep. 25(8): 3177-3181.
- Marecek, F., Terrapon, N., Janecek, S.
Two newly established and mutually related subfamilies GH13_48 and GH13_49 of the alpha-amylase family GH13.
(2024) Appl. Microbiol. Biotechnol. 108(1): 415-.
- Papayova, K., Bocanova, L., Bauerova-Hlinkova, V., Bauer, J., Halgasova, N., Kajsikova, M., Bukovska, G.
From sequence to function: Exploring biophysical properties of bacteriophage BFK20 lytic transglycosylase domain from the minor tail protein gp15 .
(2024) BBA-Proteins Proteomics 1873(1): 141044-.
- 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.
- Urbanikova, L., Janecek, S.
Trehalose synthases from the subfamily GH13_16 involved in alpha-glucan biosynthesis - a focus on their maltokinase domain.
(2024) Int. J. Biol. Macromol. 268(2): 131680-.
- Vojtova, J., Capek, M., Willeit, S., Grousl, T., Chvalova, V., Kutejova, E., Pevala, V., Valasek, L., Rinnethaler, M.
A fully automated morphological analysis of yeast mitochondria from wide-field fluorescence images.
(2024) Sci Rep 14: 30144-.
- 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.
- 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-.
- Janecek, S., Brumer, H., Henrissat, B.
News, trends, and challenges in Carbohydrate-Active enZymes.
(2023) Biologia 78(7): 1739-1740.
- Janecek, S.
Advances in amylases - what's going on?.
(2023) Molecules 28: 7268-.
- 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.
- 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-.
- 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-.
- 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.
- 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.
- 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-.
- 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-.
- Janecek, S., Svensson, B.
How many alpha-amylase GH families are there in the CAZy database?.
(2022) Amylase 6: 1-10.
- 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: 1297-.
- 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-.
- 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 13: 958581-.
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Interpretation of Single-Molecule Force Experiments on Proteins Using Normal Mode Analysis.
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The yeast mitochondrial succinylome: Implications for regulation of mitochondrial nucleoids.
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Mitochondrial HSP70 Chaperone System - The Influence of Post-Translational Modifications and Involvement in Human Diseases.
(2021) Int J Mol Sci 22(15): 8077-.
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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-.
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Mitochondrial Kinases and the Role of Mitochondrial Protein Phosphorylation in Health and Disease.
(2021) LIFE-BASEL 11: 82-.
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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.
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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-.
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The Role of CX3CL1 and ADAM17 in Pathogenesis of Diffuse Parenchymal Lung Diseases.
(2021) Diagnostics 11(6): 1074-.
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CE16 acetylesterases: in silico analysis, catalytic machinery prediction and comparison with related SGNH hydrolases.
(2021) 3 Biotech 11: 84-.
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Comparison of SynCAM1/CADM1 PDZ interactions with MUPP1 using mammalian and bacterial pull-down systems.
(2020) Brain Behav. 10: e01587-.
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Phosphomimetic Mutation of Glycine Transporter GlyT1 C-Terminal PDZ Binding Motif Inhibits its Interactions with PSD95.
(2020) J. Mol. Neurosci. 70: 488-493.
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Phosphorylation of Serine 157 Protects the Rat Glycine Transporter GlyT2 from Calpain Cleavage.
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Disease-Associated Mutations Alter the Dynamic Motion of the N-terminal Domain of the Human Cardiac Ryanodine Receptor.
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Structure and function of the human ryanodine receptors and their association with myopathies-present state, challenges, and perspectives.
(2020) Molecules 25: 4040-.
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Septin architecture and function in budding yeast.
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The in silico characterization of neutral alpha-glucosidase C (GANC) and its evolution from GANAB.
(2020) Gene 726: 144192-.
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Characterization and diversity of the complete set of GH family 3 enzymes from Rhodothermus marinus DSM 4253.
(2020) Sci Rep 10: 1329-.
- Janecek, S., Zamocka, B.
A new GH13 subfamily represented by the alpha-amylase from the halophilic archaeon Haloarcula hispanica.
(2020) Extremophiles 24: 207-217.
- Janecek, S., Martinovicova, M.
New groups of protein homologues in the alpha-amylase family
GH57 closely related to alpha-glucan branching enzymes
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(2020) Genetica 148: 77-86.
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Fungal alpha-amylases from three GH13 subfamilies: their sequence-structural features and evolutionary relationships.
(2020) Int. J. Biol. Macromol. 159: 763-772.
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A detailed in silico analysis of the amylolytic family GH126 and its possible relatedness to family GH76.
(2020) Carbohydr. Res. 494: 108082-.
- Kerenyiova, L., Janecek, S.
Extension of the taxonomic coverage of the family GH126 outside Firmicutes and in silico characterization of its non-catalytic terminal domains.
(2020) 3 Biotech 10: 420-.
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Mitochondrial HMG-Box Containing Proteins: From Biochemical Properties to the Roles in Human Diseases.
(2020) Biomolecules 10: 1193-.
- Baliova, M., Jursky, F.
Similarity of Coomassie Dye Spectral Absorbance Dynamic
of Sequentially Distant Polymeric N-Terminal Segments of
Glycine and GABA Transporters.
(2019) ChemistrySelect 4: 6304 -6308.
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Normal Mode Analysis as a Routine Part of a Structural Investigation.
(2019) Molecules 24: 3293-.
- Janecek, S., Marecek, F., MacGregor, E.A., Svensson, B.
Starch-binding domains as CBM families - history, occurrence, structure, function and evolution.
(2019) Biotechnol. Adv. 37: 107451-.
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Biocleaning of historical documents: The use and characterization of bacterial enzymatic resources.
(2019) Int. Biodeterior. Biodegrad. 140: 106-112.
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The mannose 6-phosphate/insulin-like growth factor 2 receptor mediates plasminogen-induced efferocytosis .
(2019) J. Leukoc. Biol. 105(3): 519-530.
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Yeast phosphatidylinositol transfer protein Pdr17 does not require high affinity phosphatidylinositol binding for its cellular function.
(2019) Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1864: 1412-1421.
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Residue Mutations in Murine Herpesvirus 68 Immunomodulatory Protein M3 Reveal Specific Modulation of Chemokine Binding.
(2019) Front. Cell. Infect. Microbiol. 9:210: 1-14.
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Identification of Thermotoga maritima MSB8 GH57 alpha-amylase AmyC as a glycogen-branching enzyme with high hydrolytic activity.
(2019) Appl. Microbiol. Biotechnol. 103: 6141-6151.
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Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes.
(2018) Glycobiology 28: 3-8.
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Specific glycine to alanine mutation eliminates dynamic interaction of polymeric GlyT1a N-terminus with Coomassie Brilliant Blue G-250.
(2018) Electrophoresis 39: 1357-1360.
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Biochemical and proteomic characterization of the extracellular enzymatic preparate of Exiguobacterium undae, suitable for efficient animal glue removal.
(2018) Appl. Microbiol. Biotechnol. 102: 6525-6536.
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Modulation of septin higher-order structure by the Cdc28 protein kinase.
(2018) Biologia 73: 1025-1033.
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The unique evolution of the carbohydrate-binding module CBM20 in laforin.
(2018) FEBS Lett. 592: 586-598.
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Mitochondrial Lon protease-unique structure and essential
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(2018) Integr Cancer Sci Therap 5: 1-2.
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Biotin-Chasing Assay to Evaluate uPAR Stability and Cleavage on the Surface of Cells.
(2018) Methods Mol Biol. 1731: 39-47.
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In silico analysis of the alpha-amylase family GH57: eventual subfamilies reflecting enzyme specificities.
(2018) 3 Biotech 8: 307-.
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Extracellular Purine Metabolism Is the Switchboard of Immunosuppressive Macrophages and a Novel Target to Treat Diseases With Macrophage Imbalances.
(2018) Front Immunol 9: 852-.
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Extracellular vesicles ? biogenesis, composition, function, uptake and therapeutic applications.
(2018) Biologia 73: 437-448.
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Serum and urinary levels of CD222 in cancer: origin and diagnostic value..
(2018) Neoplasma 65: 762-768.
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Lactoferrin is a natural inhibitor of plasminogen activation.
(2018) J. Biol. Chem. 293: 8600-8613.
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The N-Terminal Region of the Ryanodine Receptor Affects Channel Activation..
(2017) Front. Physiol. 8: 443-.
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The starch-binding domain family CBM41 - an in silico analysis of evolutionary relationships.
(2017) Proteins 85: 1480-1492.
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The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes.
(2017) Sci Rep 7: 631-.
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Unravelling novel functions of the endosomal transporter mannose 6-phosphate/insulin-like growth factor receptor (CD222) in health and disease: An emerging regulator of the immune system..
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- Mieog, J.C., Janecek, S., Ral, J.P.
New insight in cereal starch degradation: identification and structural characterization of four alpha-amylases in bread wheat.
(2017) Amylase 1: 35-49.
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A new group of glycoside hydrolase family 13 alpha-amylases with an aberrant catalytic triad.
(2017) Sci Rep 7: 44230-.
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Fungal Hybrid B heme peroxidases - unique fusions of a heme peroxidase domain with a carbohydrate-binding domain .
(2017) Sci Rep 7 (9393): 1-12-.
- Janecek, S., Gabrisko, M.
Remarkable evolutionary relatedness among the enzymes
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(2016) Cell. Mol. Life Sci. 73(14): 2707-2725.
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Amylolytic glycoside hydrolases.
(2016) Cell. Mol. Life Sci. 73: 2601-2602.
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A Dynamic Interaction of Coomassie Dye with the Glycine Transporters N-termini.
(2016) Protein J. 35: 371-378.
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The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease..
(2016) Sci Rep 6(33631): 1-10.
- Kuchtova, A., Janecek, S.
Domain evolution in enzymes of the neopullulanase subfamily.
(2016) Microbiology-(UK) 162(12): 2099-2115.
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Folate Receptor ? Regulates Integrin CD11b/CD18 Adhesion of a Macrophage Subset to Collagen.
(2016) J. Immunol. 197(&): 2229-2238.
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The structure and DNA-binding properties of Mgm101 from a yeast with a linear mitochondrial genome.
(2016) Nucleic Acids Res. 44(5): 2227-2239.
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Association of CD147 and Calcium Exporter PMCA4 Uncouples IL-2 Expression from Early TCR Signaling.
(2016) J. Immunol. 196(3): 1387-1399.
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The elution of certain protein affinity tags with millimolar concentrations of diclofenac.
(2015) J. Chromatogr. B 1006: 187-193.
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A RepA-like protein from bacteriophage BFK20 is a multifunctional protein with primase, polymerase, NTPase and helicase activities.
(2015) Virus Res. 210: 178-187.
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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.
(2015) Biologia 70(10): 1284-1294.
- Jursky, F., Baliova, M., Juhasova, A.
Structural insights into the benzophenanthridines binding to human glycine transporter GlyT1.
(2015) Eur. J. Pharmacol. 765: 1-6.
- Kuchtova, A., Janecek, S.
In silico analysis of family GH77 with focus on amylomaltases from borreliae and disproportionating enzymes DPE2 from plants and bacteria.
(2015) BBA-Proteins Proteomics 1854: 1260-1268.
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The mannose-6-phosphate analogue, PXS64, inhibits fibrosis via TGF-beta1 pathway in human lung fibroblasts.
(2015) Immunol. Lett. 2(165): 90-101.
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Mutations to a glycine loop in the catalytic site of human
Lon changes its protease, peptidase and ATPase activities.
(2014) FEBS J. 281: 1784-1797.
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Using a collection of MUPP1 domains to investigate similarities of neurotransmitter transporters C-terminal PDZ motifs.
(2014) Biochem. Biophys. Res. Commun. 454(1): 25-29.
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Structure and possible mechanism of the CcbJ methyltransferase from Streptomyces caelestis.
(2014) Acta Crystallogr. D 70(4): 943-957.
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Structural insights into the human RyR2 N-terminal region involved in cardiac arrhythmias.
(2014) Acta Crystallogr. D D70(11): 2897-2912.
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Phosphatidylinositol binding of Saccharomyces cerevisiae Pdr16p represents an essential feature of this lipid transfer protein to provide protection against azole antifungals.
(2014) Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1841(10): 1483-1490.
- Janecek, S., Svensson, B., MacGregor, E.A.
Alpha-amylase: an enzyme specificity found in various families of glycoside hydrolases.
(2014) Cell. Mol. Life Sci. 71: 1149-1170.
- Kereiche, S., Kovacik, L., Pevala, V., Ambro, L., Bellova, J., Kutejova, E., Raska, I.
Three-Dimensional Reconstruction of the S885A Mutant of Human Mitochondrial Lon Protease.
(2014) Folia Biol.-Prague 60(Suppl 1): 62-65.
- Majzlova, K., Janecek, S.
Two structurally related starch-binding domain families CBM25 and CBM26.
(2014) Biologia 69(9): 1087-1096.
- Mihalikova, A., Baliova, M., Jursky, F.
Effect of phosphomimetic mutations on the C-terminal sensitivity of glycine transporter GlyT1 to calpain.
(2014) Neurosci. Res. 81-82: 85-91.
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Calcium Dependent Interaction of Calmodulin with the GlyT1
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(2014) Neurochem. Res. 39(11): 2225-2233.
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Contribution of hydrogen bonds to protein stability.
(2014) Protein Sci. 23(5): 652-661.
- Pfisterer, K., Forster, F., Paster, W., Supper, V., Ohradanova-Repic, A., Eckerstorfer, P., Zwirzitz, A., Donner, C., Boulegue, C., Schiller, H.B., Ondrovicova, G., Acuto, O., Stockinger, H., Leksa, V.
The Late Endosomal Transporter CD222 Directs the Spatial Distribution and Activity of Lck..
(2014) J. Immunol. 193(6): 2718-2732.
- Ranjani, V., Janecek, S., Chai, K.P., Shahir, S., Raja Abd Rahman, R.N., Chan, K.G., Goh, K.M.
Protein engineering of selected residues from conserved sequence regions of a novel Anoxybacillus alpha-amylase.
(2014) Sci Rep 4: 5850-.
- Blesak, K., Janecek, S.
Two potentially novel amylolytic enzyme specificities in the prokaryotic glycoside hydrolase alpha-amylase family GH57.
(2013) Microbiology-(UK) 159: 2584-2593.
- Borko, L., Kostan, J., Zahradnikova, A., Pevala, V., Gasperik, J., Hostinova, E., Urbanikova, L., Djinović-Carugo, K., Bauerova-Hlinkova, V., Sevcik, J.
Human Cardiac Ryanodine Receptor: Preparation, Crystallization and Preliminary X-ray Analysis of the N-terminal Region.
(2013) Protein Pept. Lett. 20(11): 1211-1216.
- Faltinova, A., Zahradnikova, A.
Modification of cardiac RYR2 gating by a peptide from the central domain of the RYR2.
(2013) Cent. Eur. J. Biol. 8(12): 1164-1171.
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Expression and purification of recombinant calpain-derived N-terminal peptides from glycine transporter GlyT2
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(2013) Protein Expr. Purif. 88(1): 143-149.
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Adaptation of an L-Proline Adenylation Domain to Use 4- Propyl-L-Proline in the Evolution of Lincosamide Biosynthesis.
(2013) PLoS One 8: e84902-.
- Kucera, T., Otyepka, M., Matuskova, A., Samad, A., Kutejova, E., Janata, J.
A Computational Study of the Glycine-Rich Loop of
Mitochondrial Processing Peptidase.
(2013) PLoS One 8: e74518-.
- Majzlova, K., Pukajova, Z., Janecek, S.
Tracing the evolution of the alpha-amylase subfamily GH13_36 covering the amylolytic enzymes intermediate between oligo-1,6-glucosidases and neopullulanases.
(2013) Carbohydr. Res. 367: 48-57.
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Characterization of N-Demethyllincosamide
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(2013) ChemBioChem 14: 2259-2262.
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Lincomycin Biosynthesis Involves a Tyrosine
Hydroxylating Heme Protein of an Unusual Enzyme
Family.
(2013) PLoS One 8(12): e79974-.
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Purification of recombinant M3 proteins of murine gammaherpesviruses 68 and 72 expressed in Escherichia coli.
(2013) Acta Virol. 57: 59-68.
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Raw starch–degrading alpha-amylase from Bacillus aquimaris MKSC 6.2: isolation and expression of the gene, bioinformatics and biochemical characterization of the recombinant enzyme.
(2013) J. Appl. Microbiol. 114: 108-120.
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The influence of ATP-dependent proteases on a variety
of nucleoid-associated processes.
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Sequence fingerprints of enzyme specificities from the glycoside hydrolase family GH57.
(2012) Extremophiles 16(3): 497-506.
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In silico identification of catalytic residues and domain fold of the family GH119 sharing the catalytic machinery with the alpha-amylase family GH57.
(2012) FEBS Lett. 586(19): 3360-3366.
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Association of novel domain in active site of archaic hyperthermophilic maltogenic amylase from
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Molecular basis for differential glycine transporters sensitivity to sanguinarine
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Dissecting Mannose 6-Phosphate-Insulin-like Growth Factor 2 Receptor Complexes That Control Activation and Uptake of Plasminogen in Cells.
(2012) J. Biol. Chem. 287(27): 22450-22462.
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Recombinant fragment of an antibody tailored
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Crystallization and preliminary X-ray diffraction analysis of two peptides from Alzheimer PHF in complex with the MN423 antibody Fab fragment.
(2012) Acta Crystallographica Sect. F-Struct. Biol. Cryst. Commun. 68(10): 1186-1190.
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Sequence-structural features and evolutionary relationships of family GH57 alpha-amylases and their putative alpha-amylase-like homologues.
(2011) Protein J. 30(6): 429-435.
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Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals.
(2011) Enzyme Microb. Technol. 49(5): 429-440.
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Differential effect of the benzophenanthridine alkaloids sanguinarine and chelerythrine on glycine transporters.
(2011) Neurochem. Int. 58: 641-647.
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Soluble M6P/IGF2R released by TACE controls angiogenesis via blocking plasminogen activation.
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(2011) Circ.Res. 108(6): 676-685.
- Baliova, M., Jursky, F.
Calcium dependent modification of distal C-terminal sequences of glycine transporter GlyT1.
(2010) Neurochem. Int. 57: 254-261.
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Glycine-rich loop of mitochondrial processing peptidase alpha-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20..
(2010) J. Mol. Biol. 396(5): 1197-1210.
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Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity.
(2010) Protein Sci. 19(5): 987-999.
- Godany, A., Majzlova, K., Horvathova, V., Vidova, B., Janecek, S.
Tyrosine 39 of GH13 alpha-amylase from Thermococcus hydrothermalis contributes to its thermostability.
(2010) Biologia 65(3): 408-415.
- Hostinova, E., Janecek, S., Gasperik, J.
Gene sequence, bioinformatics and enzymatic characterization of alpha-amylase from Saccharomycopsis fibuligera KZ.
(2010) Protein J. 29(5): 355-364.
- Baliova, M., Knab, A., Franekova, V., Jursky, F.
Modification of the cytosolic regions of GABA transporter GAT1 by calpain.
(2009) Neurochem. Int. 55(5): 288-294.
- Christiansen, C., Abou Hachem, M., Janecek, S., Viksoe-Nielsen, A., Blennow, A., Svensson, B.
The carbohydrate-binding module family 20 – diversity, structure, and function.
(2009) FEBS J. 276(18): 5006-5029.
- Gabrisko, M., Janecek, S.
Looking for the ancestry of the heavy-chain subunits of heteromeric amino acid transporters rBAT and 4F2hc within the GH13 alpha-amylase family.
(2009) FEBS J. 276(24): 7265-7278.
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Sequential Cooperation of CD2 and CD48 in the Buildup of the Early TCR Signalosome.
(2009) J. Immunol. 182(12): 7672-7680.
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The mannose 6-phosphate/insulin-like growth factor II receptor restricts the tumourigenicity and invasiveness of squamous cell carcinoma cells..
(2009) Int. J. Cancer 124(11): 2559-2567.
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Mannose 6-phosphate/insulin-like growth factor 2 receptor limits cell invasion by controlling alphaVbeta3 integrin expression and proteolytic processing of urokinase-type plasminogen activator receptor..
(2009) Mol. Biol. Cell 20(3): 745-756.
- Franekova, V., Baliova, M., Jursky, F.
Truncation of human dopamine transporter by protease calpain.
(2008) Neurochem. Int. 52: 1436-1441.
- Godany, A., Vidova, B., Janecek, S.
The unique glycoside hydrolase family 77 amylomaltase from Borrelia burgdorferi with only catalytic triad conserved.
(2008) FEMS Microbiol. Lett. 284(1): 84-91.
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Structures of monomeric, dimeric and trimeric
PCNA: PCNA-ring assembly and opening.
(2008) Acta Crystallogr. D D64: 941-949.
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LFA-1-mediated leukocyte adhesion regulated by interaction of CD43 with LFA-1 and CD147.
(2008) Mol. Immunol. 45(6): 1703-1711.
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Reductive Evolution of the Mitochondrial Processing
Peptidases of the Unicellular Parasites Trichomonas
vaginalis and Giardia intestinalis.
(2008) PLoS Pathog. 4(12): e1000243-.
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A remote but significant sequence homology between glycoside hydrolase clan GH-H and family GH31.
(2007) FEBS Lett. 581(7): 1261-1268.
- Jiang, Z., Li, B., Jursky, F., Shen, W.
Differential distribution of glycine transporters in Muller cells and neurons in amphibian retinas.
(2007) Visual Neurosci. 24(2): 157-168.
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Roles for the Human ATP-dependent Lon Protease in Mitochondrial DNA Maintenance.
(2007) J. Biol. Chem. 282(24): 17363-17374.
- van der Kaaij, R.M., Janecek, S., van der Maarel, M.J., Dijkhuizen, L.
Phylogenetic and biochemical characterization of a novel cluster of intracellular fungal alpha-amylase enzymes.
(2007) Microbiology-(UK) 153(12): 4003-4015.
- Csokova, N., Skrabana, R., Urbanikova, L., Kovacech, B., Popov, A., Sevcik, J., Novak, M.
Preparation, crystallization and preliminary X-ray analysis of the Fab fragment of monoclonal antibody MN423, revealing the structural aspects of Alzheimer’s paired helical filaments.
(2006) Protein Pept. Lett. 13(9): 941-944.
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Starch-binding domains in the post-genome era.
(2006) Cell. Mol. Life Sci. 63(23): 2710-2721.
- Machovic, M., Janecek, S.
The evolution of putative starch-binding domains.
(2006) FEBS Lett. 580(27): 6349-6356.
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Calpain Sensitive Regions in the N-terminal Cytoplasmic Domains of Glycine Transporters GlyT1A and GlyT1B.
(2005) Neurochem. Res. 30: 1093-1100.
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TGF-beta-induced apoptosis in endothelial cells
mediated by M6P/IGFII-R and mini-plasminogen.
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A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21.
(2005) FEBS J. 272(21): 5497-5513.
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Cleavage site selection within a folded substrate by the mitochondrial ATPdependent Lon protease.
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Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa.
(2004) Biophys. J. 87: 4036-4047.
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Calpain-mediated proteolytic cleavage of the neuronal glycine transporter, GlyT2.
(2004) J. Neurochem. 88: 227-232.
- Baliova, M., Jursky, F.
Use of calpain for native GlyT2 N-terminal region separation and its potential use in transporter N-terminus interaction studies.
(2004) Biologia 59(6): 839-842.
- Baliova, M., Jursky, F.
Phosphatase inhibitors influence proteolytic cleavage pattern of Glycine transporter GlyT2 N-terminus.
(2004) Biologia 59(6): 843-845.
- Janata, J., Hola, K., Kubala, M., Gakh, O., Parkhomenko, N., Matuskova, A., Kutejova, E., Amler, E.
Substrate evokes translocation of both domains in the mitochondrial processing peptidase alpha-subunit during which the C-terminus acts as a stabilizing element.
(2004) Biochem. Biophys. Res. Commun. 316(1): 211-217.
- Liu, T., Lu, B., Lee, I., Ondrovicova, G., Kutejova, E., Suzuki, C.K.
DNA and RNA binding by the mitochondrial Lon protease is regulated by nucleotide and protein substrate.
(2004) J. Biol. Chem. 279: 13902-13910.
- Sevcik, J., Urbanikova, L., Kostan, J., Janda, L., Wiche, G.
Actin-binding domain of mouse plectin: crystal structure and binding to vimentin.
(2004) Eur. J. Biochem. 271: 1873-1884.
- Stahlberg, H., Kutejova, E., Muchova, K., Gregorini, M., Lustig, A., Muller, S.A., Olivieri, V., Engel, A., Wilkinson, A.J., Barak, I.
Oligomeric structure of the Bacillus subtilis cell division protein DivIVA determined by transmission electron microscopy.
(2004) Mol. Microbiol. 52: 1281-1290.
- Zona, R., Chang-Pi-Hin, F., O'Donohue, M.J., Janecek, S.
Bioinformatics of the family 57 glycoside hydrolases and identification of catalytic residues in amylopullulanase from Thermococcus hydrothermalis.
(2004) Eur. J. Biochem. 271(14): 2863-2872.
- Horecka, T., Perecko, D., Kutejova, E., Mikulasova, D., Kollarova, M.
The activities of the two thioredoxins from Streptomyces aureofaciens are not interchangeable.
(2003) J. Basic Microbiol. 43(1): 62-67.
- Janecek, S., Svensson, B., MacGregor, E.A.
Relation between domain evolution, specificity, and taxonomy of the a-amylase family members containing a C-terminal starch-binding domain.
(2003) Eur. J. Biochem. 270(4): 635-345.
- Janecek, S.
A motif of a microbial starch-binding domain found in human genethonin.
(2002) Bioinformatics 18(11): 1534-1537.
- Janecek, S.
How many conserved sequence regions are there in the alpha-amylase family?.
(2002) Biologia 57(Suppl. 11): 29-41.
- Mertova, J., Almasiova, M., Perecko, D., Bilka, F., Benesova, M., Bezakova, L., Psenak, M., Kutejova, E.
ATP-dependent Lon protease from maize mitochondria - comparison with the other Lon proteases.
(2002) Biologia 57(6): 739-745.
- Oslancova, A., Janecek, S.
Oligo-1,6-glucosidase and neopullulanase enzyme subfamilies from the a-amylase family defined by the fifth conserved sequence region.
(2002) Cell. Mol. Life Sci. 59(11): 1945-1959.
- Sevcik, J., Urbanikova, L., Leland, P.A., Raines, R.T.
X-ray structure of two crystalline forms of a Streptomycete ribonuclease with cytotoxic activity.
(2002) J. Biol. Chem. 277: 47325-47330.
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Purification, crystallization and preliminary X-ray analysis of the plectin actin binding domain.
(2002) Acta Crystallogr. D 58: 1368-1370.
- MacGregor, E.A., Janecek, S., Svensson, B.
Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
(2001) Biochim. Biophys. Acta 1546(1): 1-20.
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Tyrosine Hydrogen Bonds Make a Large Contribution to Protein Stability.
(2001) J. Mol. Biol. 312: 393-404.
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Location of repeat elements in glucansucrases of Leuconostoc and Streptococcus species.
(2000) FEMS Microbiol. Lett. 192(1): 53-57.
- Janecek, S., Sevcik, J.
The evolution of starch-binding domain.
(1999) FEBS Lett. 456(1): 119-125.
- Janecek, S., Leveque, E., Belarbi, A., Haye, B.
Close evolutionary relatedness of alpha-amylases from Archaea and plants.
(1999) J. Mol. Evol. 48(4): 421-426.
- Stahlberg, H., Kutejova, E., Suda, K., Wolpensinger, B., Lustig, A., Schatz, G., Engel, A., Suzuki, C.K.
Mitochondrial Lon of Saccharomyces cerevisiae is a ring-shaped protease with seven flexible subunits.
(1999) Proc. Natl. Acad. Sci. U. S. A. 96: 6787-6790.
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Recognition of RNase Sa by the inhibitor barstar: Crystal structure of the complex at 1.7 A resolution.
(1998) Acta Crystallogr. D 54: 954-963.
- Urbanikova, L., Sevcik, J.
Crystallization and preliminary X-ray investigation of the complex of RNase Sa with wild-type barstar.
(1998) Acta Crystallogr. D 54: 403-404.
- Urbanikova, L., Sevcik, J.
Crystal structure of the complex RNase Sa - barstar at 1.7 A resolution.
(1998) Gen. Physiol. Biophys. 17: 12-15.
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The ATPase and protease domains of yeast mitochondrial Lon: roles in proteolysis and respiration-dependent growth.
(1998) Proc. Natl. Acad. Sci. U. S. A. 95: 10584-10589.
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Domain evolution in the alpha-amylase family.
(1997) J. Mol. Evol. 45(3): 322-331.
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Alpha-amylase family: molecular biology and evolution.
(1997) Prog. Biophys. Mol. Biol. 67(1): 67-97.
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Spinach chloroplast ATP-dependent endopeptidase Ti-like protease .
(1996) Phytochemistry 41: 65-69.
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Characteristic differences in the primary structure allow discrimination of cyclodextrin glucanotransferases from alpha-amylases.
(1995) Biochem J. 305(2): 685-686.
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Analysis and purification of ATP-dependent mitochondrial lon protease of Saccharomyces cerevisiae.
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Purification and some characteristics of the acetylxylan esterase from Schizophyllum commune.
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Sequence similarities and evolutionary relationships of microbial, plant and animal alpha-amylases.
(1994) Eur. J. Biochem. 224(2): 519-524.
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Parallel beta/alpha-barrels of alpha-amylase, cyclodextrin glycosyltransferase and oligo-1,6-glucosidase versus the barrel of beta-amylase: evolutionary distance is a reflection of unrelated sequences.
(1994) FEBS Lett. 353(2): 119-123.
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Yeast mitochondrial ATP-dependent protease: purification and comparison with the homologous rat enzyme and the bacterial ATP-dependent protease La.
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SbvI restriction endonuclease from Streptococcus bovis.
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New conserved amino acid region of alpha-amylases in the third loop of their (beta/alpha)8-barrel domains.
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