Matches in DBpedia 2016-04 for { ?s ?p "Liver-expressed antimicrobial peptides are a family of mammalian liver-expressed antimicrobial peptides (LEAP). LEAP-2 is a cysteine-rich, and cationic protein. LEAP2 contains a core structure with two disulphide bonds formed by cysteine residues in relative 1-3 and 2-4 positions. LEAP-2 is synthesised as a 77-residue precursor, which is predominantly expressed in the liver and highly conserved among mammals. The largest native LEAP-2 form of 40 amino acid residues is generated from the precursor at a putative cleavage site for a furin-like endoprotease. In contrast to smaller LEAP-2 variants, this peptide exhibits dose-dependent antimicrobial activity against selected microbial model organisms. The exact function of this family is unclear."@en }
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- Liver-expressed_antimicrobial_peptide abstract "Liver-expressed antimicrobial peptides are a family of mammalian liver-expressed antimicrobial peptides (LEAP). LEAP-2 is a cysteine-rich, and cationic protein. LEAP2 contains a core structure with two disulphide bonds formed by cysteine residues in relative 1-3 and 2-4 positions. LEAP-2 is synthesised as a 77-residue precursor, which is predominantly expressed in the liver and highly conserved among mammals. The largest native LEAP-2 form of 40 amino acid residues is generated from the precursor at a putative cleavage site for a furin-like endoprotease. In contrast to smaller LEAP-2 variants, this peptide exhibits dose-dependent antimicrobial activity against selected microbial model organisms. The exact function of this family is unclear.".
- Q6658198 abstract "Liver-expressed antimicrobial peptides are a family of mammalian liver-expressed antimicrobial peptides (LEAP). LEAP-2 is a cysteine-rich, and cationic protein. LEAP2 contains a core structure with two disulphide bonds formed by cysteine residues in relative 1-3 and 2-4 positions. LEAP-2 is synthesised as a 77-residue precursor, which is predominantly expressed in the liver and highly conserved among mammals. The largest native LEAP-2 form of 40 amino acid residues is generated from the precursor at a putative cleavage site for a furin-like endoprotease. In contrast to smaller LEAP-2 variants, this peptide exhibits dose-dependent antimicrobial activity against selected microbial model organisms. The exact function of this family is unclear.".