| http://purl.uniprot.org/citations/18361504 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18361504 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18361504 | http://www.w3.org/2000/01/rdf-schema#comment | "The virulence factor CBP is the most abundant protein secreted by Histoplasma capsulatum, a pathogenic fungus that causes histoplasmosis. Although the biochemical function and pathogenic mechanism of CBP are unknown, quantitative Ca (2+) binding measurements indicate that CBP has a strong affinity for calcium ( K D = 6.45 +/-0.4 nM). However, no change in structure was observed upon binding of calcium, prompting a more thorough investigation of the molecular properties of CBP with respect to self-association, secondary structure, and stability. Over a wide range of pH values and salt concentrations, CBP exists predominantly as a stable, noncovalent homodimer in both its calcium-free and -bound states. Solution-state NMR and circular dichroism (CD) measurements indicated that the protein is largely alpha-helical, and its secondary structure content changes little over the range of pH values encountered physiologically. ESI-MS revealed that the six cysteine residues of CBP are involved in three intramolecular disulfide bonds that help maintain a highly protease resistant structure. Thermally and chemically induced denaturation studies indicated that unfolding of disulfide-intact CBP is reversible and provided quantitative measurements of protein stability. This disulfide-linked, protease resistant, homodimeric alpha-helical structure of CBP is likely to be advantageous for a virulence factor that must survive the harsh environment within the phagolysosomes of host macrophages."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi701495v"xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi701495v"xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "Gross M.L."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "Gross M.L."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "Goldman W.E."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "Goldman W.E."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "Beck M.R."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "Beck M.R."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "Cistola D.P."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "Cistola D.P."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "DeKoster G.T."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "DeKoster G.T."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "Hambly D.M."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/author | "Hambly D.M."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/pages | "4427-4438"xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/pages | "4427-4438"xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/title | "Structural features responsible for the biological stability of Histoplasma's virulence factor CBP."xsd:string |
| http://purl.uniprot.org/citations/18361504 | http://purl.uniprot.org/core/title | "Structural features responsible for the biological stability of Histoplasma's virulence factor CBP."xsd:string |