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Träfflista för sökning "WFRF:(Kay L.) srt2:(1995-1999)"

Sökning: WFRF:(Kay L.) > (1995-1999)

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  • Skeppstedt, O, et al. (författare)
  • The EUROBALL neutron wall - design and performance tests of neutron detectors
  • 1999
  • Ingår i: NUCLEAR INSTRUMENTS & METHODS IN PHYSICS RESEARCH SECTION A-ACCELERATORS SPECTROMETERS DETECTORS AND ASSOCIATED EQUIPMENT. - : ELSEVIER SCIENCE BV. ; 421:3, s. 531-541
  • Tidskriftsartikel (övrigt vetenskapligt/konstnärligt)abstract
    • The mechanical design of the EUROBALL neutron wall and neutron detectors, and their performance measured with a Cm-246,Cm-248 fission source are described. The array consists of 15 pseudohexaconical detector units subdivided into three, 149 mm high, herme
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  • Wilson, Sara I, et al. (författare)
  • Escape mutants of HIV-1 proteinase : enzymic efficiency and susceptibility to inhibition
  • 1997
  • Ingår i: Biochimica et Biophysica Acta. - 0006-3002 .- 1878-2434. ; 1339:1, s. 113-125
  • Tidskriftsartikel (refereegranskat)abstract
    • Genes encoding a number of mutants of HIV-1 proteinase were sub-cloned and expressed in E. coli. The proteinases containing mutations of single residues (e.g., G48V, V82F, I84V and L90M) were purified and their catalytic efficiencies relative to that of wild-type proteinase were examined using a polyprotein (recombinant HIV-1 gag) substrate and several series of synthetic peptides based on the -Hydrophobic * Hydrophobic-, -Aromatic * Pro- and pseudo-symmetrical types of cleavage junction. The L90M proteinase showed only small changes, whereas the activity of the other mutant enzymes was compromised more severely, particularly towards substrates of the -Aromatic * Pro- and pseudo-symmetrical types. The susceptibility of the mutants and the wild-type proteinase to inhibition by eleven different compounds was compared. The L90M proteinase again showed only marginal changes in its susceptibility to all except one of the inhibitors examined. The K(i) values determined for one inhibitor (Ro31-8959) showed that its potency towards the V82F, L90M, I84V and G48V mutant proteinases respectively was 2-, 3-, 17- and 27-fold less than against the wild-type proteinase. Several of the other inhibitors examined form a systematic series with Ro31-8959. The inhibition constants derived with these and a number of other inhibitors, including ABT-538 and L-735,524, are used in conjunction with the data on enzymic efficiency to assess whether each mutation in the proteinase confers an advantage for viral replication in the presence of any given inhibitor.
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