Fragment o Svetozaru Stojanovicu
نویسندگان
چکیده
منابع مشابه
Recombinant Production of a Novel Fusion Protein: Listeriolysin O Fragment Fused to S1 Subunit Of Pertussis Toxin
Background: Some resources have suggested that genetically inactivated pertussis toxoid (PTs) bear a more protective effect than chemically inactivated products. This study aimed to produce new version of PT, by cloning an inactive pertussis toxin S1 subunit (PTS1) in a fusion form with N-terminal half of the listeriolysin O (LLO) pore-forming toxin. Methods: Deposited pdb structure file of the...
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A fragment-based development of 3C-triazol-1-yl-O-galactopyranosyl aldoximes led to the discovery of highly selective and high affinity (K(d) down to 11 microm) small monosaccharide based inhibitors of galectin-3. Galectin-7, 8 N-terminal CRD, and 9 N-terminal CRD bound the inhibitors only weakly. The galectin-3 selectivity was hypothesized to stem from interaction of the aldoxime moiety with a...
متن کاملFour-body reaction dynamics: complete correlated fragment measurement of the dissociative photodetachment dynamics of O(-)(8).
The four-body dissociative photodetachment (DPD) dynamics of O-8 were studied using photoelectron photofragment coincidence (PPC) spectroscopy. All four neutral photofragments were measured in coincidence with the photodetached electron, yielding a five-body kinematically complete experiment. Velocity and angular correlations for DPD of O(-)(8) are presented and compared to those for O(-)(6). T...
متن کاملO - Glycosylation Mimics N - Glycosylation in the 16 - kDa Fragment of Bovine
The NHz-terminal domain of pro-opiomelanocortin, designated as the 16-kDa fragment, is highly conserved throughout the vertebrate family and is likely therefore to have an important functional role. Bovine 16-kDa fragment is a 77residue glycopeptide, which has been found to be glycosylated at threonine 45 and asparagine 65. Available evidence suggests that glycoforms lacking glycans at the O-li...
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ژورنال
عنوان ژورنال: Filozofija i drustvo
سال: 2010
ISSN: 0353-5738,2334-8577
DOI: 10.2298/fid1003003i