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Mechanism of antimicrobial action of indolicidin

FEMS microbiology letters, 1998-03, Vol.160 (1), p.91-96

1998

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Host-defense antimicrobial peptides: importance of structure for activity

Current pharmaceutical design, 2002-01, Vol.8 (9), p.727-742

2002

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Mechanism of antimicrobial action of indolicidin

FEMS microbiology letters, 1998-03, Vol.160 (1), p.91-96

1998

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Structure-Function Relationship Studies on the Frog Skin Antimicrobial Peptide Tigerinin 1: Design of Analogs with Improved Activity and Their Action on Clinical Bacterial Isolates

Antimicrobial Agents and Chemotherapy, 2002-07, Vol.46 (7), p.2279-2283

2002

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Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity

BBA - Biomembranes, 1999-12, Vol.1462 (1), p.29-54

1999

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Indolicidin, a 13-residue basic antimicrobial peptide rich in tryptophan and proline, interacts with Ca(2+)-calmodulin

Biochemical and biophysical research communications, 2003-10, Vol.309 (4), p.879-884

2003

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Tigerinins: Novel Antimicrobial Peptides from the Indian FrogRana tigerina

The Journal of biological chemistry, 2001-01, Vol.276 (4), p.2701-2707

2001

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Interaction of the 47-residue antibacterial peptide seminalplasmin and its 13-residue fragment which has antibacterial and hemolytic activities with model membranes

Biochemistry (Easton), 1993-03, Vol.32 (12), p.3124-3130

1993

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Indolicidin, a 13-residue basic antimicrobial peptide rich in tryptophan and proline, interacts with Ca2+-calmodulin

Biochemical and biophysical research communications, 2003-10, Vol.309 (4), p.879-884

2003

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Tigerinins: novel antimicrobial peptides from the Indian frog Rana tigerina

The Journal of biological chemistry, 2001-01, Vol.276 (4), p.2701-2707

2001

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Indolicidin, a 13-residue basic antimicrobial peptide rich in tryptophan and proline, interacts with Ca 2+-calmodulin

Biochemical and biophysical research communications, 2003, Vol.309 (4), p.879-884

2003

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Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin

FEBS letters, 1997-01, Vol.400 (3), p.289-292

1997

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Effect Of Introducing P-Fluorophenylalanine And Multiple Tryptophan Residues In A 13-Residue Antibacterial Peptide

Protein and peptide letters, 1999-04, Vol.6 (2), p.67-71

1999

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A synthetic 13-residue peptide corresponding to the hydrophobic region of bovine seminalplasmin has antibacterial activity and also causes lysis of red blood cells

The Journal of biological chemistry, 1990-06, Vol.265 (18), p.10438-10442

1990

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Structural and charge requirements for antimicrobial and hemolytic activity in the peptide PKLLETFLSKWIG, corresponding to the hydrophobic region of the antimicrobial protein bovine seminalplasmin

International Journal of Peptide and Protein Research, 1995-08, Vol.46 (2), p.166-173

1995

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Apparent specificity of bovine seminal ribonucleases can depend on the conditions used for the isolation of substrate

Biochemistry international, 1992-02, Vol.26 (1), p.125

1992

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Mechanism of antimicrobial action of indolicidin

Host-defense antimicrobial peptides: importance of structure for activity

Mechanism of antimicrobial action of indolicidin

Structure-Function Relationship Studies on the Frog Skin Antimicrobial Peptide Tigerinin 1: Design of Analogs with Improved Activity and Their Action on Clinical Bacterial Isolates

Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity

Indolicidin, a 13-residue basic antimicrobial peptide rich in tryptophan and proline, interacts with Ca(2+)-calmodulin

Tigerinins: Novel Antimicrobial Peptides from the Indian FrogRana tigerina

Interaction of the 47-residue antibacterial peptide seminalplasmin and its 13-residue fragment which has antibacterial and hemolytic activities with model membranes

Indolicidin, a 13-residue basic antimicrobial peptide rich in tryptophan and proline, interacts with Ca2+-calmodulin

Tigerinins: novel antimicrobial peptides from the Indian frog Rana tigerina

Indolicidin, a 13-residue basic antimicrobial peptide rich in tryptophan and proline, interacts with Ca 2+-calmodulin

Identification of the region that plays an important role in determining antibacterial activity of bovine seminalplasmin

Effect Of Introducing P-Fluorophenylalanine And Multiple Tryptophan Residues In A 13-Residue Antibacterial Peptide

A synthetic 13-residue peptide corresponding to the hydrophobic region of bovine seminalplasmin has antibacterial activity and also causes lysis of red blood cells

Structural and charge requirements for antimicrobial and hemolytic activity in the peptide PKLLETFLSKWIG, corresponding to the hydrophobic region of the antimicrobial protein bovine seminalplasmin

Apparent specificity of bovine seminal ribonucleases can depend on the conditions used for the isolation of substrate

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