Search results
- 1.0583248 - BTÚ 2024 RIV US eng J - Journal Article
Husťáková, Blanka - Trundová, Mária - Adámková, Kristýna - Koval, Tomáš - Dušková, Jarmila - Dohnálek, Jan
A highly active S1-P1 nuclease from the opportunistic pathogen iStenotrophomonas maltophilia/i cleaves c-di-GMP.
FEBS Letters. Roč. 597, č. 16 (2023), s. 2103-2118. ISSN 0014-5793. E-ISSN 1873-3468
R&D Projects: GA ČR(CZ) GA20-12109S; GA MŠMT EF15_003/0000447
Research Infrastructure: CIISB III - 90242
Institutional support: RVO:86652036
Keywords : n-glycosylation * phosphodiesterase * mechanism * enzyme * S1-P1 nuclease
OECD category: Biophysics
Impact factor: 3.5, year: 2022
Method of publishing: Open access
https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14683
Permanent Link: https://hdl.handle.net/11104/0351252 - 2.0574533 - BTÚ 2024 RIV US eng J - Journal Article
Malý, Martin - Kolenko, Petr - Stránský, Jan - Švecová, Leona - Dušková, Jarmila - Koval, Tomáš - Skálová, Tereza - Trundová, Mária - Adámková, Kristýna - Černý, Jiří - Božíková, Paulina - Dohnálek, Jan
Tetracycline-modifying enzyme SmTetX from Stenotrophomonas maltophilia.
Acta Crystallographica Section F-Structural Biology and Crystallization Communications. Roč. 79, JUL 2023 (2023), s. 180-192. ISSN 1744-3091. E-ISSN 2053-230X
R&D Projects: GA MŠMT EF16_019/0000778; GA MŠMT EF15_003/0000447; GA MŠMT(CZ) ED1.1.00/02.0109; GA MŠMT(CZ) EF18_046/0015974
Research Infrastructure: CIISB III - 90242
Institutional support: RVO:86652036
Keywords : FAD-dependent monooxygenases * tetracycline * antibiotic resistance
OECD category: Biochemistry and molecular biology
Impact factor: 0.9, year: 2022
Method of publishing: Open access
https://scripts.iucr.org/cgi-bin/paper?S2053230X23005381
Permanent Link: https://hdl.handle.net/11104/0346203 - 3.0562970 - BTÚ 2023 RIV DK eng J - Journal Article
Adámková, Kristýna - Koval, Tomáš - Ostergaard, L. H. - Dušková, Jarmila - Malý, Martin - Švecová, Leona - Skálová, Tereza - Kolenko, Petr - Dohnálek, Jan
Atomic resolution studies of S1 nuclease complexes reveal details of RNA interaction with the enzyme despite multiple lattice-translocation defects.
Acta Crystallographica Section D-Biological Crystallography. Roč. 78, OCT 1 2022 (2022), s. 1194-1209. ISSN 1399-0047. E-ISSN 2059-7983
R&D Projects: GA MŠMT(CZ) LM2015043; GA MŠMT(CZ) LM2018127; GA ČR(CZ) GA20-12109S; GA MŠMT EF15_003/0000447
Institutional support: RVO:86652036
Keywords : S1 nuclease * Aspergillus oryzae * lattice-translocation defects * nucleotides * nucleosides * complexes
OECD category: Analytical chemistry
Impact factor: 2.2, year: 2022
Method of publishing: Limited access
https://scripts.iucr.org/cgi-bin/paper?S2059798322008397
Permanent Link: https://hdl.handle.net/11104/0340705