Zobrazeno 1 - 10
of 105
pro vyhledávání: '"Veronika Harmat"'
Autor:
Zoé S. Tóth, Ibolya Leveles, Kinga Nyíri, Gergely N. Nagy, Veronika Harmat, Thapakorn Jaroentomeechai, Oliver Ozohanics, Rebecca L. Miller, Marina Ballesteros Álvarez, Beáta G. Vértessy, András Benedek
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-16 (2024)
Abstract The dUTPase is a key DNA repair enzyme in Mycobacterium tuberculosis, and it may serve as a novel promising anti-tuberculosis target. Stl repressor from Staphylococcus aureus was shown to bind to and inhibit dUTPases from various sources, an
Externí odkaz:
https://doaj.org/article/60538a93259949f983f23e69b5fb0f06
Autor:
Ho-Jin Lee, Shi-Wei Liu, Máté Sulyok-Eiler, Veronika Harmat, Viktor Farkas, Zoltán Bánóczi, Mouna El Khabchi, Hua-Jun Shawn Fan, Kimihiko Hirao, Jong-Won Song
Publikováno v:
Heliyon, Vol 10, Iss 12, Pp e33159- (2024)
The conformational properties of Alanine (Ala) residue have been investigated to understand protein folding and develop force fields. In this work, we examined the neighbor effect on the conformational spaces of Ala residue using model azapeptides, A
Externí odkaz:
https://doaj.org/article/8e15da5995494e1b9144799f408f3421
Publikováno v:
FASEB BioAdvances, Vol 2, Iss 8, Pp 489-505 (2020)
Abstract Calmodulin (CaM), the key calcium sensor of eukaryotic cells regulating a great number of target proteins, belongs to the most conserved proteins. We compared function and properties of CaMs from two evolutionarily distant species, the human
Externí odkaz:
https://doaj.org/article/48abeea2e2eb4ddfbc1b212af3bf775a
Autor:
Kinga Judit Fodor, Dániel Hutai, Tamás Jernei, Angéla Takács, Zsófia Szász, Máté Sulyok-Eiler, Veronika Harmat, Rita Oláh Szabó, Gitta Schlosser, Ferenc Hudecz, László Kőhidai, Antal Csámpai
Publikováno v:
Molecules, Vol 25, Iss 7, p 1599 (2020)
Use of a Pictet-Spengler reaction of tryptamine and l-tryptophan methyl ester and subsequent reduction of the nitro group followed by further cyclocondensation with aryl aldehydes and formyl–substituted carboxylic acids, including ferrocene-based c
Externí odkaz:
https://doaj.org/article/8454f92b0c3a4370822b1582c22c1b2b
Autor:
Péter Rapali, László Radnai, Dániel Süveges, Veronika Harmat, Ferenc Tölgyesi, Weixiao Y Wahlgren, Gergely Katona, László Nyitray, Gábor Pál
Publikováno v:
PLoS ONE, Vol 6, Iss 4, p e18818 (2011)
LC8 dynein light chain (DYNLL) is a eukaryotic hub protein that is thought to function as a dimerization engine. Its interacting partners are involved in a wide range of cellular functions. In its dozens of hitherto identified binding partners DYNLL
Externí odkaz:
https://doaj.org/article/b7cb1bc7ab3c47f7b216f39213f9e340
Autor:
Kende Attila Béres, Zoltán Homonnay, Libor Kvitek, Zsolt Dürvanger, Martina Kubikova, Veronika Harmat, Fanni Szilágyi, Zsuzsanna Czégény, Péter Németh, Laura Bereczki, Vladimir M. Petruševski, Mátyás Pápai, Attila Farkas, László Kótai
Publikováno v:
Inorganic Chemistry. 61:14403-14418
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b246a9abd19cc384e31449c6dd293fd9
https://doi.org/10.1021/acs.inorgchem.2c02265
https://doi.org/10.1021/acs.inorgchem.2c02265
Autor:
Zsolt Dürvanger, Eszter Boros, Zoltán Attila Nagy, Rózsa Hegedüs, Márton Megyeri, József Dobó, Péter Gál, Gitta Schlosser, Annamária F. Ángyán, Zoltán Gáspári, András Perczel, Veronika Harmat, Gábor Mező, Dóra K. Menyhárd, Gábor Pál
Publikováno v:
ACS Chemical Biology. 17:969-986
MASP-1 and MASP-2 are key activator proteases of the complement lectin pathway. The first specific mannose-binding lectin-associated serine protease (MASP) inhibitors had been developed from the 14-amino-acid sunflower trypsin inhibitor (SFTI) peptid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f3b092faa4cf89aef96103b48ea5111
https://doi.org/10.1021/acschembio.2c00114
https://doi.org/10.1021/acschembio.2c00114
Autor:
Anna J. Kiss-Szemán, Pál Stráner, Imre Jákli, Naoki Hosogi, Veronika Harmat, Dóra K. Menyhárd, András Perczel
Publikováno v:
Chemical Science. 13:7132-7142
The structure of tetrameric mammalian acylaminoacyl peptidase – a key upstream regulator of the proteasome – was determined by cryo-EM (and elucidated by MD), showing a “shutters-and-channels” substrate selection apparatus created by oligomer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dac992208edf00280908bbdb5d1582ca
https://doi.org/10.1039/d2sc02276a
https://doi.org/10.1039/d2sc02276a
Autor:
Zoltán Attila Nagy, Dávid Héja, Dániel Bencze, Bence Kiss, Eszter Boros, Dávid Szakács, Krisztián Fodor, Matthias Wilmanns, Andrea Kocsis, József Dobó, Péter Gál, Veronika Harmat, Gábor Pál
Publikováno v:
J Biol Chem
Ecotin is a homodimeric serine protease inhibitor produced by many commensal and pathogenic microbes. It functions as a virulence factor, enabling survival of various pathogens in the blood. The ecotin dimer binds two protease molecules, and each eco
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7761d6ddd3bf8b8fad27c9d367ca5b54
https://europepmc.org/articles/PMC9800290/
https://europepmc.org/articles/PMC9800290/
Autor:
Anna J. Kiss-Szemán, Luca Takács, Zoltán Orgován, Pál Stráner, Imre Jákli, Gitta Schlosser, Simonas Masiulis, Veronika Harmat, Dóra K. Menyhárd, András Perczel
Publikováno v:
Chemical science. 13(48)
The structure of porcine AAP (pAAP) in a covalently bound complex with meropenem was determined by cryo-EM to 2.1 Å resolution, showing the mammalian serine-protease inhibited by a carbapenem antibiotic. AAP is a modulator of the ubiquitin-proteasom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34265e8d4d92fea8d3bb3dbe3dee4bcc
https://pubmed.ncbi.nlm.nih.gov/36545146
https://pubmed.ncbi.nlm.nih.gov/36545146