| dbo:abstract
|
- The antifungal protein family is a protein family, with members sharing a structure consisting of five antiparallel beta strands which are highly twisted creating a beta barrel stabilised by four internal disulphide bridges. A cationic site adjacent to a hydrophobic stretch on the protein surface may constitute a phospholipid binding site. Human epithelium produce antifungal proteins. The proteins kill fungi by inducing apoptosis and/or forming pores on the cell membrane. (en)
|
| dbo:symbol
| |
| dbo:thumbnail
| |
| dbo:wikiPageID
| |
| dbo:wikiPageLength
|
- 2175 (xsd:nonNegativeInteger)
|
| dbo:wikiPageRevisionID
| |
| dbo:wikiPageWikiLink
| |
| dbp:caption
|
- solution structure of the antifungal protein from aspergillus giganteus. evidence for disulphide configurational isomerism (en)
|
| dbp:interpro
| |
| dbp:name
| |
| dbp:pfam
| |
| dbp:symbol
| |
| dbp:wikiPageUsesTemplate
| |
| dcterms:subject
| |
| rdf:type
| |
| rdfs:comment
|
- The antifungal protein family is a protein family, with members sharing a structure consisting of five antiparallel beta strands which are highly twisted creating a beta barrel stabilised by four internal disulphide bridges. A cationic site adjacent to a hydrophobic stretch on the protein surface may constitute a phospholipid binding site. Human epithelium produce antifungal proteins. The proteins kill fungi by inducing apoptosis and/or forming pores on the cell membrane. (en)
|
| rdfs:label
|
- Antifungal protein family (en)
|
| owl:sameAs
| |
| prov:wasDerivedFrom
| |
| foaf:depiction
| |
| foaf:isPrimaryTopicOf
| |
| is dbo:wikiPageRedirects
of | |
| is dbo:wikiPageWikiLink
of | |
| is foaf:primaryTopic
of | |
