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1-naphthylphenylamine and gramicidin a

1-naphthylphenylamine has been researched along with gramicidin a in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	1 (50.00)	18.2507
2000's	1 (50.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Farmer, SW; Hancock, RE; Hodges, RS; Kondejewski, LH; Wishart, DS	1
Hancock, RE; Hodges, RS; Lee, DL; Pflegerl, K; Powers, JP; Vasil, ML	1

Other Studies

2 other study(ies) available for 1-naphthylphenylamine and gramicidin a

Article	Year
Gramicidin S is active against both gram-positive and gram-negative bacteria. International journal of peptide and protein research, 1996, Volume: 47, Issue:6 Topics: 1-Naphthylamine; Anti-Bacterial Agents; Erythrocytes; Fluorescent Dyes; Gram-Negative Bacteria; Gram-Positive Bacteria; Gramicidin; Hemolysis; Peptides; Peptides, Cyclic; Permeability	1996
Effects of single D-amino acid substitutions on disruption of beta-sheet structure and hydrophobicity in cyclic 14-residue antimicrobial peptide analogs related to gramicidin S. The journal of peptide research : official journal of the American Peptide Society, 2004, Volume: 63, Issue:2 Topics: 1-Naphthylamine; Amino Acid Substitution; Anti-Infective Agents; Benzothiazoles; Candida albicans; Carbocyanines; Cell Membrane Permeability; Circular Dichroism; Glycine; Gram-Negative Bacteria; Gram-Positive Bacteria; Gramicidin; Hemolysis; Humans; Hydrophobic and Hydrophilic Interactions; Membrane Potentials; Microbial Sensitivity Tests; Peptides, Cyclic; Protein Structure, Secondary; Structure-Activity Relationship; Yeasts	2004

Article

Year

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

International journal of peptide and protein research, 1996, Volume: 47, Issue:6

Topics: 1-Naphthylamine; Anti-Bacterial Agents; Erythrocytes; Fluorescent Dyes; Gram-Negative Bacteria; Gram-Positive Bacteria; Gramicidin; Hemolysis; Peptides; Peptides, Cyclic; Permeability

1996

Effects of single D-amino acid substitutions on disruption of beta-sheet structure and hydrophobicity in cyclic 14-residue antimicrobial peptide analogs related to gramicidin S.

The journal of peptide research : official journal of the American Peptide Society, 2004, Volume: 63, Issue:2

Topics: 1-Naphthylamine; Amino Acid Substitution; Anti-Infective Agents; Benzothiazoles; Candida albicans; Carbocyanines; Cell Membrane Permeability; Circular Dichroism; Glycine; Gram-Negative Bacteria; Gram-Positive Bacteria; Gramicidin; Hemolysis; Humans; Hydrophobic and Hydrophilic Interactions; Membrane Potentials; Microbial Sensitivity Tests; Peptides, Cyclic; Protein Structure, Secondary; Structure-Activity Relationship; Yeasts

2004