D
Dalia Shallom-Shezifi
Researcher at Technion – Israel Institute of Technology
Publications - 7
Citations - 365
Dalia Shallom-Shezifi is an academic researcher from Technion – Israel Institute of Technology. The author has contributed to research in topics: Aminoglycoside & Mutation (genetic algorithm). The author has an hindex of 6, co-authored 7 publications receiving 342 citations.
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Journal ArticleDOI
The Structure of an Inverting GH43 beta-Xylosidase from Geobacillus stearothermophilus with its Substrate Reveals the Role of the Three Catalytic Residues.
Christian Brüx,Alon Ben-David,Dalia Shallom-Shezifi,Maya Leon,Karsten Niefind,Gil Shoham,Yuval Shoham,Dietmar Schomburg +7 more
TL;DR: Structures of the enzyme-substrate (xylobiose) complex provide insights into the role of the three catalytic residues of the inverting family 43 beta-xylosidase, and why Asp128 is an invariant among all five-bladed beta-propeller glycoside hydrolases.
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Redesign of aminoglycosides for treatment of human genetic diseases caused by premature stop mutations.
Igor Nudelman,Annie Rebibo-Sabbah,Dalia Shallom-Shezifi,Mariana Hainrichson,Ido Stahl,Tamar Ben-Yosef,Timor Baasov +6 more
TL;DR: A series of new derivatives of the clinically used aminoglycoside antibiotic paromomycin were designed, synthesized, and their ability to read-through premature stop codon mutations was examined in both in vitro translation system and ex vivo mammalian cultured cells.
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Differential Selectivity of Natural and Synthetic Aminoglycosides towards the Eukaryotic and Prokaryotic Decoding A Sites.
Jiro Kondo,Mariana Hainrichson,Igor Nudelman,Dalia Shallom-Shezifi,Christopher M. Barbieri,Daniel S. Pilch,Eric Westhof,Timor Baasov +7 more
TL;DR: This work has used a combination of biochemical and structural analysis to compare and contrast the molecular mechanisms of action and the structure–activity relationships of a new synthetic aminoglycoside, NB33, and a structurally similar natural aminglycoside apramycin, and demonstrates the general molecular principles that determine the decreased selectivity of apramYcin for the prokaryotic decoding site, and the increased selectivity for NB33.
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Branched aminoglycosides: Biochemical studies and antibacterial activity of neomycin B derivatives
Mariana Hainrichson,Varvara Pokrovskaya,Dalia Shallom-Shezifi,Micha Fridman,Valery Belakhov,Dina Shachar,Sima Yaron,Timor Baasov +7 more
TL;DR: The designed structures show antibacterial activity superior to that of neomycin B against pathogenic and resistant strains, while in parallel they demonstrate poor substrate activity with APH(3')-IIIa.
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Overexpression and initial characterization of the chromosomal aminoglycoside 3'-O-phosphotransferase APH(3')-IIb from Pseudomonas aeruginosa.
Mariana Hainrichson,Orit Yaniv,Marina Cherniavsky,Igor Nudelman,Dalia Shallom-Shezifi,Sima Yaron,Timor Baasov +6 more
TL;DR: The chromosomal gene aph(3′)-IIb, encoding an aminoglycoside 3′-phosphotransferase in Pseudomonas aeruginosa, was cloned and overexpressed in Escherichia coli and was shown to phosphorylate its substrates at the C-3′-OH position.