Structure of the Cathelicidin Motif of Protegrin-3 Precursor: Structural Insights into the Activation Mechanism of an Antimicrobial Protein

This publication has 35 references indexed in Scilit:

• 3D domain swapping: As domains continue to swap
  Protein Science, 2002
• Cathelicidins: microbicidal activity, mechanisms of action, and roles in innate immunity
  Microbes and Infection, 2002
• Protein folding and three-dimensional domain swapping: astrained relationship?
  Current Opinion in Structural Biology, 2002
• Antimicrobial peptides of multicellular organisms
  Nature, 2002
• Cathelicidins: a family of endogenous antimicrobial peptides
  Current Opinion in Hematology, 2002
• Innate antimicrobial peptide protects the skin from invasive bacterial infection
  Nature, 2001
• Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
  The EMBO Journal, 2001
• Human cystatin C, an amyloidogenic protein, dimerizes through three-dimensional domain swapping.
  Nature Structural & Molecular Biology, 2001
• Structural features and biological activities of the cathelicidin-derived antimicrobial peptides
  Biopolymers, 2000
• The Formation of Diselenide Bridges in Proteins by Incorporation of Selenocysteine Residues: Biosynthesis and Characterization of (Se)2-Thioredoxin
  Biochemistry, 1994