The Experts below are selected from a list of 294 Experts worldwide ranked by ideXlab platform

Yannis D. Clonis - One of the best experts on this subject based on the ideXlab platform.

  • isoenzyme and Allozyme specific inhibitors 2 2 dihydroxybenzophenones and their carbonyl n analogues that discriminate between human glutathione transferase a1 1 and p1 1 Allozymes
    Chemical Biology & Drug Design, 2015
    Co-Authors: Foteini M Pouliou, Trias Thireou, Elias Eliopoulos, Petros G. Tsoungas, Nikolaos E. Labrou, Yannis D. Clonis
    Abstract:

    The selectivity of certain benzophenones and their carbonyl N-analogues was investigated towards the human GSTP1-1 Allozymes A, B and C involved in MDR. The Allozymes were purified from extracts derived from E. coli harbouring the plasmids pEXP5-CT/TOPO-TA-hGSTP1*A, pOXO4-hGSTP1*B or pOXO4-hGSTP1*C. Compound screening with each Allozyme activity indicated three compounds with appreciable inhibitory potencies, 12 and 13 with P1-1A 62% and 67%, 11 and 12 with P1-1C 51% and 70%, whereas that of 15 fell behind with P1-1B (41%). These findings were confirmed by IC50 values (74-125 μm). Enzyme inhibition kinetics, aided by molecular modelling and docking, revealed that there is competition with the substrate CDNB for the same binding site on the Allozyme (Ki(13/A)  = 63.6 ± 3.0 μm, Ki(15/B)  = 198.6 ± 14.3 μm, and Ki(11/C)  = 16.5 ± 2.7 μm). These data were brought into context by an in silico structural comparative analysis of the targeted proteins. Although the screened compounds showed moderate inhibitory potency against hGSTP1-1, remarkably, some of them demonstrated absolute isoenzyme and/or Allozyme selectivity.

  • Isoenzyme‐ and Allozyme‐Specific Inhibitors: 2,2′‐Dihydroxybenzophenones and Their Carbonyl N‐Analogues that Discriminate between Human Glutathione Transferase A1‐1 and P1‐1 Allozymes
    Chemical biology & drug design, 2015
    Co-Authors: Foteini M Pouliou, Trias Thireou, Elias Eliopoulos, Petros G. Tsoungas, Nikolaos E. Labrou, Yannis D. Clonis
    Abstract:

    The selectivity of certain benzophenones and their carbonyl N-analogues was investigated towards the human GSTP1-1 Allozymes A, B and C involved in MDR. The Allozymes were purified from extracts derived from E. coli harbouring the plasmids pEXP5-CT/TOPO-TA-hGSTP1*A, pOXO4-hGSTP1*B or pOXO4-hGSTP1*C. Compound screening with each Allozyme activity indicated three compounds with appreciable inhibitory potencies, 12 and 13 with P1-1A 62% and 67%, 11 and 12 with P1-1C 51% and 70%, whereas that of 15 fell behind with P1-1B (41%). These findings were confirmed by IC50 values (74-125 μm). Enzyme inhibition kinetics, aided by molecular modelling and docking, revealed that there is competition with the substrate CDNB for the same binding site on the Allozyme (Ki(13/A)  = 63.6 ± 3.0 μm, Ki(15/B)  = 198.6 ± 14.3 μm, and Ki(11/C)  = 16.5 ± 2.7 μm). These data were brought into context by an in silico structural comparative analysis of the targeted proteins. Although the screened compounds showed moderate inhibitory potency against hGSTP1-1, remarkably, some of them demonstrated absolute isoenzyme and/or Allozyme selectivity.

Patrick Berrebi - One of the best experts on this subject based on the ideXlab platform.

Laura A. Katz - One of the best experts on this subject based on the ideXlab platform.

  • Systematics of dusky salamanders, Desmognathus (Caudata: Plethodontidae), in the mountain and Piedmont regions of Virginia and North Carolina, USA
    Zoological Journal of the Linnean Society, 2008
    Co-Authors: Stephen G. Tilley, Renée L. Eriksen, Laura A. Katz
    Abstract:

    We analysed mitochondrial (cytochrome b) nucleotide sequences, nuclear Allozyme markers, and morphometric characters to investigate species boundaries and phylogenetic relationships among dusky salamanders (Desmognathus) in the southern Blue Ridge and adjacent Piedmont Physiographic Provinces of Virginia and North Carolina. Our results revealed four distinct mitochondrial DNA clades that are also characterized by distinct Allozyme markers. One clade consists of sequences derived from populations distributed from New England to south-western Virginia that are referable to Desmognathus fuscus Rafinesque, 1820, although there is considerable sequence and Allozyme divergence within this clade. A second clade consists of sequences derived from populations referable to Desmognathus planiceps Newman, 1955, a form that we resurrect from its long synonymy under D. fuscus. Desmognathus planiceps and D. fuscus also differ in mandibular tooth shape. Two other cytochrome b sequences recovered from populations along the Blue Ridge escarpment in southern Virginia are quite divergent from those of the previous two clades, and these populations may represent yet another distinct species. Sequences from a population in the Brushy Mountains in the Piedmont of northern North Carolina are similar to those of Desmognathus carolinensis. Population groupings indicated by Allozyme data generally correspond to the cytochrome b clades. Cryptic diversity in Appalachian desmognathan salamanders clearly requires further study. © 2008 The Linnean Society of London, Zoological Journal of the Linnean Society, 2008, 152, 115‐130. ADDITIONAL KEYWORDS: Allozymes ‐ cytochrome b ‐ Desmognathus planiceps ‐ mitochondrial DNA ‐ morphometrics ‐ phylogeography ‐ taxonomy.

  • genetic structure of the blue ridge dusky salamander desmognathus orestes inferences from Allozymes mitochondrial dna and behavior
    Evolution, 2001
    Co-Authors: Louise S Mead, Stephen G. Tilley, Laura A. Katz
    Abstract:

    Abstract The plethodontid salamander Desmognathus orestes, a member of the D. ochrophaeus species complex, is distributed in southwestern Virginia, eastern Tennessee, and western North Carolina. Previous Allozyme analyses indicate that D. orestes consists of two distinct groups of populations (D. orestes ‘B’ and D. orestes ‘C’) with extensive intergradation and probable gene flow between these two groups. Spatially varying allele frequencies can reflect historical associations, current gene flow, or a combination of population-level processes. To differentiate among these processes, we use multiple markers to further characterize divergence among populations of D. orestes and assess the degree of intergradation between D. orestes ‘B’ and D. orestes ‘C’, specifically investigating variation in Allozymes, mitochondrial DNA (mtDNA), and reproductive behavior among populations. On a broad scale, the mtDNA genealogies reconstruct haplotype clades that correspond to the species identified from previous Allozyme...

Foteini M Pouliou - One of the best experts on this subject based on the ideXlab platform.

  • isoenzyme and Allozyme specific inhibitors 2 2 dihydroxybenzophenones and their carbonyl n analogues that discriminate between human glutathione transferase a1 1 and p1 1 Allozymes
    Chemical Biology & Drug Design, 2015
    Co-Authors: Foteini M Pouliou, Trias Thireou, Elias Eliopoulos, Petros G. Tsoungas, Nikolaos E. Labrou, Yannis D. Clonis
    Abstract:

    The selectivity of certain benzophenones and their carbonyl N-analogues was investigated towards the human GSTP1-1 Allozymes A, B and C involved in MDR. The Allozymes were purified from extracts derived from E. coli harbouring the plasmids pEXP5-CT/TOPO-TA-hGSTP1*A, pOXO4-hGSTP1*B or pOXO4-hGSTP1*C. Compound screening with each Allozyme activity indicated three compounds with appreciable inhibitory potencies, 12 and 13 with P1-1A 62% and 67%, 11 and 12 with P1-1C 51% and 70%, whereas that of 15 fell behind with P1-1B (41%). These findings were confirmed by IC50 values (74-125 μm). Enzyme inhibition kinetics, aided by molecular modelling and docking, revealed that there is competition with the substrate CDNB for the same binding site on the Allozyme (Ki(13/A)  = 63.6 ± 3.0 μm, Ki(15/B)  = 198.6 ± 14.3 μm, and Ki(11/C)  = 16.5 ± 2.7 μm). These data were brought into context by an in silico structural comparative analysis of the targeted proteins. Although the screened compounds showed moderate inhibitory potency against hGSTP1-1, remarkably, some of them demonstrated absolute isoenzyme and/or Allozyme selectivity.

  • Isoenzyme‐ and Allozyme‐Specific Inhibitors: 2,2′‐Dihydroxybenzophenones and Their Carbonyl N‐Analogues that Discriminate between Human Glutathione Transferase A1‐1 and P1‐1 Allozymes
    Chemical biology & drug design, 2015
    Co-Authors: Foteini M Pouliou, Trias Thireou, Elias Eliopoulos, Petros G. Tsoungas, Nikolaos E. Labrou, Yannis D. Clonis
    Abstract:

    The selectivity of certain benzophenones and their carbonyl N-analogues was investigated towards the human GSTP1-1 Allozymes A, B and C involved in MDR. The Allozymes were purified from extracts derived from E. coli harbouring the plasmids pEXP5-CT/TOPO-TA-hGSTP1*A, pOXO4-hGSTP1*B or pOXO4-hGSTP1*C. Compound screening with each Allozyme activity indicated three compounds with appreciable inhibitory potencies, 12 and 13 with P1-1A 62% and 67%, 11 and 12 with P1-1C 51% and 70%, whereas that of 15 fell behind with P1-1B (41%). These findings were confirmed by IC50 values (74-125 μm). Enzyme inhibition kinetics, aided by molecular modelling and docking, revealed that there is competition with the substrate CDNB for the same binding site on the Allozyme (Ki(13/A)  = 63.6 ± 3.0 μm, Ki(15/B)  = 198.6 ± 14.3 μm, and Ki(11/C)  = 16.5 ± 2.7 μm). These data were brought into context by an in silico structural comparative analysis of the targeted proteins. Although the screened compounds showed moderate inhibitory potency against hGSTP1-1, remarkably, some of them demonstrated absolute isoenzyme and/or Allozyme selectivity.

Costas S Tsigenopoulos - One of the best experts on this subject based on the ideXlab platform.