Zobrazeno 1 - 6 of 6 pro vyhledávání: '"M E, Wales"'
1
Liposomal oxytetracycline and doxycycline: studies on enhancement of encapsulation efficiency
Autor: M, Budai, P, Chapela, L, Budai, M E, Wales, I, Petrikovics, A, Zimmer, P, Gróf, I, Klebovich
Publikováno v: Drug discoveriestherapeutics. 3(1)
Liposomal encapsulations of oxytetracycline (OTC) and doxycycline (DC) with various lipid compositions and hydrating solutions have been studied in order to develop a new liposomal formulation to treat bacterial infections. Encapsulation efficiencies
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bcaeac9a91c6242162e0cf3cbacc6e5f
https://pubmed.ncbi.nlm.nih.gov/22495463
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3
Site-directed alterations to the geometry of the aspartate transcarbamoylase zinc domain: selective alteration to regulation by heterotropic ligands, isoelectric point, and stability in urea
Autor: M. E. Wales, D. M. Brown, J. R. Wild, C. J. Strang
Publikováno v: Biochemistry. 32(16)
Structural aspects requisite for allosteric function in the regulatory chain of aspartate transcarbamoylase were explored by site-specific amino acid insertion or substitution within the zinc domain in the region of contact between the catalytic and
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12f13b29dab557191eb4860b8ef40733
https://pubmed.ncbi.nlm.nih.gov/8476846
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5
Site-specific substitutions of the Tyr-165 residue in the catalytic chain of aspartate transcarbamoylase promotes a T-state preference in the holoenzyme
Autor: M E Wales, T A Hoover, James R. Wild
Publikováno v: Journal of Biological Chemistry. 263:6109-6114
The amino acid residue Tyr-165C of aspartate transcarbamoylase (EC 2.1.3.2) of Escherichia coli has been proposed to be involved in the transition from the T-state to the R-state upon binding of the bisubstrate analogue N-(phosphonacetyl)-L-aspartate
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c4b4306e7c7935e23d5b319cf6764ece
https://doi.org/10.1016/s0021-9258(18)68756-3
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