Title : Antimicrobial action of histone H2B in Escherichia coli: evidence for membrane translocation and DNA-binding of a histone H2B fragment after proteolytic cleavage by outer membrane proteinase T.

Pub. Date : 2008 Nov-Dec

PMID : 18706965






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1 Antimicrobial action of histone H2B in Escherichia coli: evidence for membrane translocation and DNA-binding of a histone H2B fragment after proteolytic cleavage by outer membrane proteinase T. Previous studies have led to the isolation of histone H2B with antibacterial properties from an extract of the skin of the Schlegel"s green tree frog Rhacophorus schlegelii and it is now demonstrated that the intact peptide is released into norepinephrine-stimulated skin secretions. Norepinephrine H2B clustered histone 21 Homo sapiens
2 Antimicrobial action of histone H2B in Escherichia coli: evidence for membrane translocation and DNA-binding of a histone H2B fragment after proteolytic cleavage by outer membrane proteinase T. Previous studies have led to the isolation of histone H2B with antibacterial properties from an extract of the skin of the Schlegel"s green tree frog Rhacophorus schlegelii and it is now demonstrated that the intact peptide is released into norepinephrine-stimulated skin secretions. Norepinephrine H2B clustered histone 21 Homo sapiens
3 Antimicrobial action of histone H2B in Escherichia coli: evidence for membrane translocation and DNA-binding of a histone H2B fragment after proteolytic cleavage by outer membrane proteinase T. Previous studies have led to the isolation of histone H2B with antibacterial properties from an extract of the skin of the Schlegel"s green tree frog Rhacophorus schlegelii and it is now demonstrated that the intact peptide is released into norepinephrine-stimulated skin secretions. Norepinephrine H2B clustered histone 21 Homo sapiens