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Monomeric Cu,Zn-superoxide Dismutase Is a Common Misfolding Intermediate in the Oxidation Models of Sporadic and Familial Amyotrophic Lateral Sclerosis[boxs]

The Journal of biological chemistry, 2004-04, Vol.279 (15), p.15499-15504

2004

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Oxidation-induced Misfolding and Aggregation of Superoxide Dismutase and Its Implications for Amyotrophic Lateral Sclerosis

The Journal of biological chemistry, 2002-12, Vol.277 (49), p.47551-47556

2002

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Effect of Ring Size on Conformation and Biological Activity of Cyclic Cationic Antimicrobial Peptides

Journal of medicinal chemistry, 2009-04, Vol.52 (7), p.2090-2097

2009

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Optimization of Microbial Specificity in Cyclic Peptides by Modulation of Hydrophobicity within a Defined Structural Framework

The Journal of biological chemistry, 2002-01, Vol.277 (1), p.67-74

2002

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A prion protein epitope selective for the pathologically misfolded conformation

Nature medicine, 2003-07, Vol.9 (7), p.893-899

2003

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Dissociation of Antimicrobial and Hemolytic Activities in Cyclic Peptide Diastereomers by Systematic Alterations in Amphipathicity

The Journal of biological chemistry, 1999-05, Vol.274 (19), p.13181-13192

1999

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New ice-binding face for type I antifreeze protein

FEBS letters, 1999-12, Vol.463 (1), p.87-91

1999

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Modulation of Structure and Antibacterial and Hemolytic Activity by Ring Size in Cyclic Gramicidin S Analogs

The Journal of biological chemistry, 1996-10, Vol.271 (41), p.25261-25268

1996

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Development of the Structural Basis for Antimicrobial and Hemolytic Activities of Peptides Based on Gramicidin S and Design of Novel Analogs Using NMR Spectroscopy

The Journal of biological chemistry, 2000-05, Vol.275 (19), p.14287-14294

2000

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Antifreeze protein from shorthorn sculpin: Identification of the ice‐binding surface

Protein science, 2001-12, Vol.10 (12), p.2566-2576

2001

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Nonlamellar Phases Induced by the Interaction of Gramicidin S with Lipid Bilayers. A Possible Relationship to Membrane-Disrupting Activity

Biochemistry (Easton), 1997-06, Vol.36 (25), p.7906-7916

1997

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Fourier Transform Infrared Spectroscopic Studies of the Interaction of the Antimicrobial Peptide Gramicidin S with Lipid Micelles and with Lipid Monolayer and Bilayer Membranes

Biochemistry (Easton), 1999-11, Vol.38 (46), p.15193-15203

1999

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[19] Analysis of synthetic peptides by high-performance liquid chromatography

Methods in Enzymology, 1997, Vol.289, p.426-469

1997

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Unusual β-sheet periodicity in small cyclic peptides

Nature structural biology, 1998-04, Vol.5 (4), p.284-288

1998

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Differential scanning calorimetric study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol lipid bilayer membranes

Biochimica et biophysica acta, 1999-03, Vol.1417 (2), p.211-223

1999

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Diastereoisomeric analogues of gramicidin S: structure, biological activity and interaction with lipid bilayers

Biochemical journal, 2000-08, Vol.349 (3), p.747-755

2000

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Preferential Heterodimeric Parallel Coiled-coil Formation by Synthetic Max and c-Myc Leucine Zippers: A Description of Putative Electrostatic Interactions Responsible for the Specificity of Heterodimerization

Journal of molecular biology, 1995-12, Vol.254 (3), p.505-520

1995

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Gramicidin S is active against both gram-positive and gram-negative bacteria

International Journal of Peptide and Protein Research, 1996-06, Vol.47 (6), p.460-466

1996

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Reply to "Properties of a disease-specific prion probe"

Nature medicine, 2004-01, Vol.10 (1), p.11-12

2004

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Properties of a disease-specific prion probe

Nature medicine, 2004-01, Vol.10 (1), p.11-11

2004

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Membrane-bound structure and alignment of the antimicrobial [beta]-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19F-NMR

Journal of biomolecular NMR, 2001-11, Vol.21 (3), p.191

2001

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A method for the facile solid-phase synthesis of gramicidin S and its analogs

Letters in peptide science : LIPS, 1996-03, Vol.3 (1), p.53-60

1996

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Monomeric Cu,Zn-superoxide Dismutase Is a Common Misfolding Intermediate in the Oxidation Models of Sporadic and Familial Amyotrophic Lateral Sclerosis[boxs]

Oxidation-induced Misfolding and Aggregation of Superoxide Dismutase and Its Implications for Amyotrophic Lateral Sclerosis

Effect of Ring Size on Conformation and Biological Activity of Cyclic Cationic Antimicrobial Peptides

Optimization of Microbial Specificity in Cyclic Peptides by Modulation of Hydrophobicity within a Defined Structural Framework

A prion protein epitope selective for the pathologically misfolded conformation

Dissociation of Antimicrobial and Hemolytic Activities in Cyclic Peptide Diastereomers by Systematic Alterations in Amphipathicity

New ice-binding face for type I antifreeze protein

Modulation of Structure and Antibacterial and Hemolytic Activity by Ring Size in Cyclic Gramicidin S Analogs

Development of the Structural Basis for Antimicrobial and Hemolytic Activities of Peptides Based on Gramicidin S and Design of Novel Analogs Using NMR Spectroscopy

Antifreeze protein from shorthorn sculpin: Identification of the ice‐binding surface

Nonlamellar Phases Induced by the Interaction of Gramicidin S with Lipid Bilayers. A Possible Relationship to Membrane-Disrupting Activity

Fourier Transform Infrared Spectroscopic Studies of the Interaction of the Antimicrobial Peptide Gramicidin S with Lipid Micelles and with Lipid Monolayer and Bilayer Membranes

[19] Analysis of synthetic peptides by high-performance liquid chromatography

Unusual β-sheet periodicity in small cyclic peptides

Differential scanning calorimetric study of the effect of the antimicrobial peptide gramicidin S on the thermotropic phase behavior of phosphatidylcholine, phosphatidylethanolamine and phosphatidylglycerol lipid bilayer membranes

Diastereoisomeric analogues of gramicidin S: structure, biological activity and interaction with lipid bilayers

Preferential Heterodimeric Parallel Coiled-coil Formation by Synthetic Max and c-Myc Leucine Zippers: A Description of Putative Electrostatic Interactions Responsible for the Specificity of Heterodimerization

Gramicidin S is active against both gram-positive and gram-negative bacteria

Reply to "Properties of a disease-specific prion probe"

Properties of a disease-specific prion probe

Membrane-bound structure and alignment of the antimicrobial [beta]-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19F-NMR

A method for the facile solid-phase synthesis of gramicidin S and its analogs

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