منابع مشابه
Molecular modeling of the rabbit colonic ( HK a 2 a ) H + , K + ATPase
A model of the HKa2a subunit of the rabbit colonic H+, K+ ATPase has been generated using the crystal structure of the Ca+2 ATPase as a template. A pairwise sequence alignment of the deduced primary sequences of the two proteins demonstrated that they share 29% amino acid sequence identity and 47% similarity. Using O (version 7) the model of HKa2a was constructed by interactively mutating, dele...
متن کاملDevelopment of p97 AAA ATPase inhibitors.
Specific p97 inhibitors are valuable research tools to carry out mechanistic and cellular investigations of p97 biology. p97 is an abundant, ubiquitin-selective chaperone that has multiple functions and is essential for life. Therefore, genetic methods that require long incubations like siRNA or expression of dominant-negative p97 mutants are likely to generate complicated outcomes due to secon...
متن کاملDirected HK propagator.
We offer a more formal justification for the successes of our recently communicated "directed Heller-Herman-Kluk-Kay" (DHK) time propagator by examining its performance in one-dimensional bound systems which exhibit at least quasi-periodic motion. DHK is distinguished by its single one-dimensional integral--a vast simplification over the usual 2N-dimensional integral in full Heller-Herman-Kluk-...
متن کاملNovel Inhibitors of E. coli RecA ATPase Activity
The bacterial RecA protein has been implicated as a bacterial drug target not as an antimicrobial target, but as an adjuvant target with the potential to suppress the mechanism by which bacteria gain drug resistance. In order to identify small molecules that inhibit RecA/ssDNA nucleoprotein filament formation, we have adapted the phosphomolybdate-blue ATPase assay for high throughput screening ...
متن کاملBinding assays of inhibitors towards selected V-ATPase domains.
The macrolide antibiotic bafilomycin and the related synthetic compound SB 242784 are potent inhibitors of the vacuolar H+ -ATPases (V-ATPase). It is currently believed that the site of action of these inhibitors is located on the membrane bound c-subunits of V-ATPases. To address the identification of the critical inhibitors binding domain, their specific binding to a synthetic peptide corresp...
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ژورنال
عنوان ژورنال: Journal of Synthetic Organic Chemistry, Japan
سال: 1993
ISSN: 0037-9980,1883-6526
DOI: 10.5059/yukigoseikyokaishi.51.86