| Year |
Citation |
Score |
| 2010 |
Thennarasu S, Huang R, Lee DK, Yang P, Maloy L, Chen Z, Ramamoorthy A. Limiting an antimicrobial peptide to the lipid-water interface enhances its bacterial membrane selectivity: a case study of MSI-367. Biochemistry. 49: 10595-605. PMID 21062093 DOI: 10.1021/Bi101394R |
0.767 |
|
| 2010 |
Thennarasu S, Tan A, Penumatchu R, Shelburne CE, Heyl DL, Ramamoorthy A. Antimicrobial and membrane disrupting activities of a peptide derived from the human cathelicidin antimicrobial peptide LL37. Biophysical Journal. 98: 248-57. PMID 20338846 DOI: 10.1016/J.Bpj.2009.09.060 |
0.856 |
|
| 2006 |
Ramamoorthy A, Thennarasu S, Tan A, Gottipati K, Sreekumar S, Heyl DL, An FY, Shelburne CE. Deletion of all cysteines in tachyplesin I abolishes hemolytic activity and retains antimicrobial activity and lipopolysaccharide selective binding. Biochemistry. 45: 6529-40. PMID 16700563 DOI: 10.1021/Bi052629Q |
0.845 |
|
| 2006 |
Porcelli F, Buck-Koehntop BA, Thennarasu S, Ramamoorthy A, Veglia G. Structures of the dimeric and monomeric variants of magainin antimicrobial peptides (MSI-78 and MSI-594) in micelles and bilayers, determined by NMR spectroscopy. Biochemistry. 45: 5793-9. PMID 16669623 DOI: 10.1021/Bi0601813 |
0.803 |
|
| 2006 |
Ramamoorthy A, Thennarasu S, Lee DK, Tan A, Maloy L. Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin. Biophysical Journal. 91: 206-16. PMID 16603496 DOI: 10.1529/Biophysj.105.073890 |
0.788 |
|
| 2006 |
Ramamoorthy A, Thennarasu S, Tan A, Lee DK, Clayberger C, Krensky AM. Cell selectivity correlates with membrane-specific interactions: a case study on the antimicrobial peptide G15 derived from granulysin. Biochimica Et Biophysica Acta. 1758: 154-63. PMID 16579960 DOI: 10.1016/J.Bbamem.2006.02.014 |
0.759 |
|
| 2005 |
Thennarasu S, Lee DK, Poon A, Kawulka KE, Vederas JC, Ramamoorthy A. Membrane permeabilization, orientation, and antimicrobial mechanism of subtilosin A. Chemistry and Physics of Lipids. 137: 38-51. PMID 16095584 DOI: 10.1016/J.Chemphyslip.2005.06.003 |
0.771 |
|
| 2005 |
Thennarasu S, Lee DK, Tan A, Prasad Kari U, Ramamoorthy A. Antimicrobial activity and membrane selective interactions of a synthetic lipopeptide MSI-843. Biochimica Et Biophysica Acta. 1711: 49-58. PMID 15904663 DOI: 10.1016/J.Bbamem.2005.02.010 |
0.793 |
|
| 2001 |
Thennarasu S, Nagaraj R. Effects of salt and denaturant on structure of the amino terminal alpha-helical segment of an antibacterial peptide dermaseptin and its binding to model membranes. Indian Journal of Biochemistry & Biophysics. 38: 142-8. PMID 11693375 |
0.765 |
|
| 1999 |
Thennarasu S, Nagaraj R. Synthetic peptides corresponding to the beta-hairpin loop of rabbit defensin NP-2 show antimicrobial activity. Biochemical and Biophysical Research Communications. 254: 281-3. PMID 9918829 DOI: 10.1006/bbrc.1998.9933 |
0.42 |
|
| 1997 |
Thennarasu S, Nagaraj R. Solution conformations of peptides representing the sequence of the toxin pardaxin and analogues in trifluoroethanol-water mixtures: analysis of CD spectra. Biopolymers. 41: 635-45. PMID 9108731 DOI: 10.1002/(SICI)1097-0282(199705)41:6<635::AID-BIP4>3.0.CO;2-R |
0.64 |
|
| 1996 |
Thennarasu S, Nagaraj R. Specific antimicrobial and hemolytic activities of 18-residue peptides derived from the amino terminal region of the toxin pardaxin. Protein Engineering. 9: 1219-24. PMID 9010936 |
0.615 |
|
| 1995 |
Thennarasu S, Nagaraj R. Design of 16-residue peptides possessing antimicrobial and hemolytic activities or only antimicrobial activity from an inactive peptide. International Journal of Peptide and Protein Research. 46: 480-6. PMID 8748708 |
0.607 |
|
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