Zobrazeno 1 - 10
of 76
pro vyhledávání: '"Anna Bujacz"'
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 2, p 1534 (2023)
Free drug concentration in the blood sera is crucial for its appropriate activity. Serum albumin, the universal blood carrier protein, is responsible for transporting drugs and releasing them into the bloodstream. Therefore, a drug’s binding to SA
Externí odkaz:
https://doaj.org/article/22d763574112401f8bac47189ca436c8
Autor:
Anna Bujacz, Jedrzej Rum, Maria Rutkiewicz, Agnieszka J. Pietrzyk-Brzezinska, Grzegorz Bujacz
Publikováno v:
Materials, Vol 14, Iss 12, p 3351 (2021)
Aromatic amino acid aminotransferases present a special potential in the production of drugs and synthons, thanks to their ability to accommodate a wider range of substrates in their active site, in contrast to aliphatic amino acid aminotransferases.
Externí odkaz:
https://doaj.org/article/b38fa1bd7e3742ff8aae08fa86491392
Publikováno v:
Acta Crystallographica Section E: Crystallographic Communications, Vol 72, Iss 1, Pp 102-105 (2016)
In the title compound, [FeII(C44H24Cl4N4)(C6H5CH2NH2)2]·C6H14 or [FeII(TPP-Cl)(BzNH2)2]·n-hexane [where TPP-Cl and BzNH2 are 5,10,15,20-tetrakis(4-chlorophenyl)porphyrinate and benzylamine ligands, respectively], the FeII cation lies on an inversio
Externí odkaz:
https://doaj.org/article/cefa1294080944c2879d8a85342945f0
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 15, p 5354 (2020)
β-Galactosidase from Arthrobacter sp. 32cB (ArthβDG) is a cold-adapted enzyme able to catalyze hydrolysis of β-d-galactosides and transglycosylation reaction, where galactosyl moiety is being transferred onto an acceptor larger than a water molecu
Externí odkaz:
https://doaj.org/article/57f0fcb2bd394e70be29fad82875539b
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 17, p 4301 (2019)
ArthβDG is a dimeric, cold-adapted β-d-galactosidase that exhibits high hydrolytic and transglycosylation activity. A series of crystal structures of its wild form, as well as its ArthβDG_E441Q mutein complexes with ligands were obtained in order
Externí odkaz:
https://doaj.org/article/8b1379d5a8dc441eb0b4d25e42a15a07
Publikováno v:
PLoS ONE, Vol 9, Iss 11, p e108761 (2014)
The 30-kDa lipoprotein (LP) family of mulberry silkworm comprises major hemolymph proteins specific to the fifth instar larvae. The family consists of 46 members, 24 of which are referred to as typical 30-kDa LPs. To date, two crystal structures of 3
Externí odkaz:
https://doaj.org/article/ba87a1679b5344d8a10b5df681fa1474
Autor:
Agnieszka J Pietrzyk, Anna Bujacz, Jochen Mueller-Dieckmann, Malgorzata Lochynska, Mariusz Jaskolski, Grzegorz Bujacz
Publikováno v:
PLoS ONE, Vol 8, Iss 4, p e61303 (2013)
The 30-kDa family of lipoproteins from insect hemolymph has been the focus of a number of studies over the last few years. Recently, four crystal structures of Bombyx mori lipoprotein 7 have been determined. Here we report two crystal structures of a
Externí odkaz:
https://doaj.org/article/ebb9b9ced3d64368848b1d5d66d43f1b
Publikováno v:
PLoS ONE, Vol 8, Iss 1, p e55697 (2013)
The presented study examines the phenomenon of the fluorescence under UV light excitation (312 nm) of E. coli cells expressing a novel metagenomic-derived putative methylthioadenosine phosphorylase gene, called rsfp, grown on LB agar supplemented wit
Externí odkaz:
https://doaj.org/article/6266f4f82a024966b0b64f361936bd20
Publikováno v:
Chirality. 32:334-344
Serum albumin, the most abundant transport protein of mammalian blood, interacts with various nonsteroidal anti-inflammatory drugs (NSAIDs) affecting their disposition, metabolism, and excretion. A big group of chiral NSAIDs transported by albumin, p
Autor:
Grzegorz Bujacz, Maria Rutkiewicz, Anna Bujacz, Agnieszka J. Pietrzyk-Brzezinska, Jedrzej Rum
Publikováno v:
Materials, Vol 14, Iss 3351, p 3351 (2021)
Materials
Volume 14
Issue 12
Materials
Volume 14
Issue 12
Aromatic amino acid aminotransferases present a special potential in the production of drugs and synthons, thanks to their ability to accommodate a wider range of substrates in their active site, in contrast to aliphatic amino acid aminotransferases.