The Experts below are selected from a list of 291 Experts worldwide ranked by ideXlab platform
Gary L. Sloan - One of the best experts on this subject based on the ideXlab platform.
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Characteristics of Extracellular Protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus.
FEMS microbiology letters, 1991Co-Authors: J D Nitterauer, Harry E. Heath, L S Heath, P A Leblanc, Gary L. SloanAbstract:A derivative of Staphylococcus simulans biovar staphylolyticus cured of all five plasmids present in the wild-type organism was developed, and the characteristics of Extracellular Protein production by this plasmidless strain were compared to those of the wild type. Although staphylolytic endopeptidase (lysostaphin) and beta-lactamase are known to be plasmid encoded, analysis of this cured strain revealed that most other Extracellular Proteins are chromosomally encoded.
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Characteristics of Extracellular Protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus.
FEMS Microbiology Letters, 1991Co-Authors: J D Nitterauer, Harry E. Heath, L S Heath, P A Leblanc, Gary L. SloanAbstract:A derivative of Staphylococcus simulans biovar staphylolyticus cured of all five plasmids present in the wild-type organism was developed, and the characteristics of Extracellular Protein production by this plasmidless strains were compared to those of the wild type. Although staphylolytic endopeptidase (lysostaphin) and β-lactamase are known to be plasmid encoded, analysis of this cured strain revealed that most other Extracellular Proteins are chromosomally encoded.
J D Nitterauer - One of the best experts on this subject based on the ideXlab platform.
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Characteristics of Extracellular Protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus.
FEMS microbiology letters, 1991Co-Authors: J D Nitterauer, Harry E. Heath, L S Heath, P A Leblanc, Gary L. SloanAbstract:A derivative of Staphylococcus simulans biovar staphylolyticus cured of all five plasmids present in the wild-type organism was developed, and the characteristics of Extracellular Protein production by this plasmidless strain were compared to those of the wild type. Although staphylolytic endopeptidase (lysostaphin) and beta-lactamase are known to be plasmid encoded, analysis of this cured strain revealed that most other Extracellular Proteins are chromosomally encoded.
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Characteristics of Extracellular Protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus.
FEMS Microbiology Letters, 1991Co-Authors: J D Nitterauer, Harry E. Heath, L S Heath, P A Leblanc, Gary L. SloanAbstract:A derivative of Staphylococcus simulans biovar staphylolyticus cured of all five plasmids present in the wild-type organism was developed, and the characteristics of Extracellular Protein production by this plasmidless strains were compared to those of the wild type. Although staphylolytic endopeptidase (lysostaphin) and β-lactamase are known to be plasmid encoded, analysis of this cured strain revealed that most other Extracellular Proteins are chromosomally encoded.
Alan C Rapraeger - One of the best experts on this subject based on the ideXlab platform.
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characterization of the high affinity cell binding domain in the cell surface proteoglycan syndecan 4
Journal of Biological Chemistry, 1998Co-Authors: Aidan J Mcfall, Alan C RapraegerAbstract:Abstract The syndecan family of cell surface proteoglycans regulates cell adhesion via their glycosaminoglycan chains and discrete domains of their core Proteins. Core Protein domains that are variable between syndecan family members may regulate syndecan-specific associations, thereby endowing individual syndecans with unique functions. A syndecan-4-specific domain has been identified in the Extracellular syndecan-4 Protein. This region mediates cell adhesion when provided as an artificial substratum and is localized within amino acids 56–109 of the recombinant Extracellular Protein domain of mouse syndecan-4 (mS4ED) (McFall, A. J., and Rapraeger, A. C. (1997) J. Biol. Chem. 272, 12901–12904). To characterize its interaction with the cell surface, radiolabeled ligand binding studies were performed. A single high affinity interaction, with a dissociation constant of 2 × 10−9 m, was observed between mS4ED and both human and mouse cells. Both chicken S4ED and mS4ED compete for this interaction, although they are only 34% identical within the cell-binding domain sequence. The Extracellular Protein domains of syndecan-1, -2, and -3, however, fail to compete. The interaction is also observed with native syndecan-4 shed from cell surfaces. Interestingly, the Extracellular Protein domain of syndecan-1 also mediates cell adhesion, suggesting a similar but discrete interaction for this family member.
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identification of an adhesion site within the syndecan 4 Extracellular Protein domain
Journal of Biological Chemistry, 1997Co-Authors: Aidan J Mcfall, Alan C RapraegerAbstract:Abstract The syndecan family of cell surface proteoglycans regulates cell adhesion and growth factor signaling by binding components of the Extracellular matrix and growth factors. To date, all known ligand interactions are via the covalently attached glycosaminoglycan chains. To assay for potential Extracellular interactions via the core Proteins directly, the recombinant Extracellular domain of syndecan-4 (S4ED), one of the four syndecan family members, was tested as a substratum for the attachment of mammalian cells. Human foreskin fibroblasts bind to mouse S4ED, and both mouse and chicken S4ED can block this binding, with 50% inhibition observed between 0.1 and 1 × 10−7 m. The Extracellular domain of another syndecan family member, syndecan-1, fails to compete for cell binding to mouse S4ED. Amino acids 56–109 of the 120-amino acid mouse S4ED compete fully, suggesting that the cell binding domain is within this region. The ability of syndecan-4 to interact with molecules at the cell surface via its core Protein as well as its glycosaminoglycan chains may uniquely regulate the formation of cell surface signaling complexes following engagement of this proteoglycan with its Extracellular ligands.
P A Leblanc - One of the best experts on this subject based on the ideXlab platform.
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Characteristics of Extracellular Protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus.
FEMS microbiology letters, 1991Co-Authors: J D Nitterauer, Harry E. Heath, L S Heath, P A Leblanc, Gary L. SloanAbstract:A derivative of Staphylococcus simulans biovar staphylolyticus cured of all five plasmids present in the wild-type organism was developed, and the characteristics of Extracellular Protein production by this plasmidless strain were compared to those of the wild type. Although staphylolytic endopeptidase (lysostaphin) and beta-lactamase are known to be plasmid encoded, analysis of this cured strain revealed that most other Extracellular Proteins are chromosomally encoded.
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Characteristics of Extracellular Protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus.
FEMS Microbiology Letters, 1991Co-Authors: J D Nitterauer, Harry E. Heath, L S Heath, P A Leblanc, Gary L. SloanAbstract:A derivative of Staphylococcus simulans biovar staphylolyticus cured of all five plasmids present in the wild-type organism was developed, and the characteristics of Extracellular Protein production by this plasmidless strains were compared to those of the wild type. Although staphylolytic endopeptidase (lysostaphin) and β-lactamase are known to be plasmid encoded, analysis of this cured strain revealed that most other Extracellular Proteins are chromosomally encoded.
Harry E. Heath - One of the best experts on this subject based on the ideXlab platform.
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Characteristics of Extracellular Protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus.
FEMS microbiology letters, 1991Co-Authors: J D Nitterauer, Harry E. Heath, L S Heath, P A Leblanc, Gary L. SloanAbstract:A derivative of Staphylococcus simulans biovar staphylolyticus cured of all five plasmids present in the wild-type organism was developed, and the characteristics of Extracellular Protein production by this plasmidless strain were compared to those of the wild type. Although staphylolytic endopeptidase (lysostaphin) and beta-lactamase are known to be plasmid encoded, analysis of this cured strain revealed that most other Extracellular Proteins are chromosomally encoded.
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Characteristics of Extracellular Protein production by a plasmidless derivative of Staphylococcus simulans biovar staphylolyticus.
FEMS Microbiology Letters, 1991Co-Authors: J D Nitterauer, Harry E. Heath, L S Heath, P A Leblanc, Gary L. SloanAbstract:A derivative of Staphylococcus simulans biovar staphylolyticus cured of all five plasmids present in the wild-type organism was developed, and the characteristics of Extracellular Protein production by this plasmidless strains were compared to those of the wild type. Although staphylolytic endopeptidase (lysostaphin) and β-lactamase are known to be plasmid encoded, analysis of this cured strain revealed that most other Extracellular Proteins are chromosomally encoded.
