Year |
Citation |
Score |
2017 |
Hicks R. Preparation of Membrane Models of Gram-Negative Bacteria and Their Interaction with Antimicrobial Peptides Studied by CD and NMR. Methods in Molecular Biology (Clifton, N.J.). 1548: 231-245. PMID 28013508 DOI: 10.1007/978-1-4939-6737-7_16 |
0.438 |
|
2016 |
Hicks RP. Antibacterial and anticancer activity of a series of novel peptides incorporating cyclic tetra-substituted C(α) amino acids. Bioorganic & Medicinal Chemistry. PMID 27387357 DOI: 10.1016/J.Bmc.2016.06.048 |
0.408 |
|
2015 |
Abercrombie JJ, Leung KP, Chai H, Hicks RP. Spectral and biological evaluation of a synthetic antimicrobial peptide derived from 1-aminocyclohexane carboxylic acid. Bioorganic & Medicinal Chemistry. 23: 1341-7. PMID 25684423 DOI: 10.1016/J.Bmc.2015.01.027 |
0.479 |
|
2014 |
Chai H, Allen WE, Hicks RP. Spectroscopic investigations of the binding mechanisms between antimicrobial peptides and membrane models of Pseudomonas aeruginosa and Klebsiella pneumoniae. Bioorganic & Medicinal Chemistry. 22: 4210-22. PMID 24931276 DOI: 10.1016/J.Bmc.2014.05.040 |
0.472 |
|
2013 |
Bhonsle JB, Clark T, Bartolotti L, Hicks RP. A brief overview of antimicrobial peptides containing unnatural amino acids and ligand-based approaches for peptide ligands. Current Topics in Medicinal Chemistry. 13: 3205-24. PMID 24200355 DOI: 10.2174/15680266113136660226 |
0.471 |
|
2013 |
Clark TD, Bartolotti L, Hicks RP. The application of DOSY NMR and molecular dynamics simulations to explore the mechanism(s) of micelle binding of antimicrobial peptides containing unnatural amino acids. Biopolymers. 99: 548-61. PMID 23712491 DOI: 10.1002/Bip.22215 |
0.549 |
|
2013 |
Hicks RP, Abercrombie JJ, Wong RK, Leung KP. Antimicrobial peptides containing unnatural amino acid exhibit potent bactericidal activity against ESKAPE pathogens. Bioorganic & Medicinal Chemistry. 21: 205-14. PMID 23199484 DOI: 10.1016/J.Bmc.2012.10.039 |
0.489 |
|
2012 |
Russell AL, Williams BC, Spuches A, Klapper D, Srouji AH, Hicks RP. The effect of the length and flexibility of the side chain of basic amino acids on the binding of antimicrobial peptides to zwitterionic and anionic membrane model systems. Bioorganic & Medicinal Chemistry. 20: 1723-39. PMID 22304850 DOI: 10.1016/J.Bmc.2012.01.015 |
0.662 |
|
2012 |
Hicks RP, Russell AL. Application of unnatural amino acids to the de novo design of selective antibiotic peptides. Methods in Molecular Biology (Clifton, N.J.). 794: 135-67. PMID 21956561 DOI: 10.1007/978-1-61779-331-8_9 |
0.615 |
|
2011 |
Russell AL, Spuches AM, Williams BC, Venugopal D, Klapper D, Srouji AH, Hicks RP. The effect of the placement and total charge of the basic amino acid clusters on antibacterial organism selectivity and potency. Bioorganic & Medicinal Chemistry. 19: 7008-22. PMID 22047803 DOI: 10.1016/J.Bmc.2011.10.033 |
0.659 |
|
2011 |
Russell AL, Kennedy AM, Spuches AM, Gibson WS, Venugopal D, Klapper D, Srouji AH, Bhonsle JB, Hicks RP. Determining the effect of the incorporation of unnatural amino acids into antimicrobial peptides on the interactions with zwitterionic and anionic membrane model systems. Chemistry and Physics of Lipids. 164: 740-58. PMID 21945566 DOI: 10.1016/J.Chemphyslip.2011.09.003 |
0.671 |
|
2010 |
Venugopal D, Klapper D, Srouji AH, Bhonsle JB, Borschel R, Mueller A, Russell AL, Williams BC, Hicks RP. Novel antimicrobial peptides that exhibit activity against select agents and other drug resistant bacteria. Bioorganic & Medicinal Chemistry. 18: 5137-47. PMID 20558071 DOI: 10.1016/J.Bmc.2010.05.065 |
0.608 |
|
2010 |
Russell AL, Kennedy AM, Spuches AM, Venugopal D, Bhonsle JB, Hicks RP. Spectroscopic and thermodynamic evidence for antimicrobial peptide membrane selectivity. Chemistry and Physics of Lipids. 163: 488-97. PMID 20362562 DOI: 10.1016/J.Chemphyslip.2010.03.009 |
0.643 |
|
2007 |
Bhonsle JB, Venugopal D, Huddler DP, Magill AJ, Hicks RP. Application of 3D-QSAR for identification of descriptors defining bioactivity of antimicrobial peptides. Journal of Medicinal Chemistry. 50: 6545-53. PMID 18062663 DOI: 10.1021/Jm070884Y |
0.493 |
|
2007 |
Hicks RP, Bhonsle JB, Venugopal D, Koser BW, Magill AJ. De novo design of selective antibiotic peptides by incorporation of unnatural amino acids. Journal of Medicinal Chemistry. 50: 3026-36. PMID 17547385 DOI: 10.1021/Jm061489V |
0.506 |
|
2004 |
Hicks RP, Bhattacharjee AK, Koser BW, Traficante DD. The anthrax protective antigen (PA63) bound conformation of a peptide inhibitor of the binding of lethal factor to PA63: as determined by trNOESY NMR and molecular modeling. Journal of Medicinal Chemistry. 47: 5347-55. PMID 15481973 DOI: 10.1021/Jm040139A |
0.402 |
|
2004 |
Hartell MG, Hicks R, Bhattacharjee AK, Koser BW, Carvalho K, Van Hamont JE. Nuclear magnetic resonance and molecular modeling analysis of the interaction of the antimalarial drugs artelinic acid and artesunic acid with beta-cyclodextrin. Journal of Pharmaceutical Sciences. 93: 2076-89. PMID 15236456 DOI: 10.1002/Jps.20106 |
0.353 |
|
2004 |
Whitehead TL, Jones LM, Hicks RP. PFG-NMR investigations of the binding of cationic neuropeptides to anionic and zwitterionic micelles. Journal of Biomolecular Structure & Dynamics. 21: 567-76. PMID 14692800 DOI: 10.1080/07391102.2004.10506949 |
0.443 |
|
2004 |
Kennedy A, Long CJ, Hmel PJ, Hicks R, Reid TJ. The association of dimethylsulfoxide and model membranes studied by pulse-field gradient NMR Spectroscopy. 18: 265-269. DOI: 10.1155/2004/814213 |
0.334 |
|
2003 |
Hicks RP, Mones E, Kim H, Koser BW, Nichols DA, Bhattacharjee AK. Comparison of the conformation and electrostatic surface properties of magainin peptides bound to sodium dodecyl sulfate and dodecylphosphocholine micelles. Biopolymers. 68: 459-70. PMID 12666172 DOI: 10.1002/Bip.10325 |
0.436 |
|
2001 |
Whitehead TL, Jones LM, Hicks RP. Effects of the incorporation of CHAPS into SDS micelles on neuropeptide-micelle binding: separation of the role of electrostatic interactions from hydrophobic interactions. Biopolymers. 58: 593-605. PMID 11285556 DOI: 10.1002/1097-0282(200106)58:7<593::Aid-Bip1033>3.0.Co;2-P |
0.47 |
|
2001 |
Hicks RP. Recent advances in NMR: Expanding its role in rational drug design Current Medicinal Chemistry. 8: 627-650. PMID 11281846 DOI: 10.2174/0929867013373237 |
0.318 |
|
2001 |
Hicks RP. Methods in Molecular Biology, Volume 146. Mass Spectrometry of Proteins and Peptides Edited by John R. Chapman. Humana Press, Totowa, NJ. 2000. xiv + 538 pp. 15.5 × 23.5 cm. ISBN 0-89603-609-x. $125.00. Journal of Medicinal Chemistry. 44: 849-850. DOI: 10.1021/Jm0005297 |
0.343 |
|
2000 |
Perrine SA, Whitehead TL, Hicks RP, Szarek JL, Krause JE, Simmons MA. Solution structures in SDS micelles and functional activity at the bullfrog substance P receptor of ranatachykinin peptides. Journal of Medicinal Chemistry. 43: 1741-53. PMID 10794691 DOI: 10.1021/Jm000093V |
0.457 |
|
1998 |
Whitehead TL, McNair SD, Hadden CE, Young JK, Hicks RP. Membrane-induced secondary structures of neuropeptides: a comparison of the solution conformations adopted by agonists and antagonists of the mammalian tachykinin NK1 receptor. Journal of Medicinal Chemistry. 41: 1497-506. PMID 9554882 DOI: 10.1021/Jm970789X |
0.37 |
|
1998 |
Young JK, Hicks RP, Wright GE, Morrison TG. The role of leucine residues in the structure and function of a leucine zipper peptide inhibitor of paramyxovirus (NDV) fusion. Virology. 243: 21-31. PMID 9527912 DOI: 10.1006/Viro.1998.9044 |
0.461 |
|
1997 |
Young JK, Hicks RP, Wright GE, Morrison TG. Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays, NMR, and molecular modeling. Virology. 238: 291-304. PMID 9400602 DOI: 10.1006/Viro.1997.8834 |
0.447 |
|
1997 |
Hicks RP. The study of membrane- or receptor-bound neuropeptides by NMR Methods in Molecular Biology (Clifton, N.J.). 73: 185-207. PMID 9031208 DOI: 10.1385/0-89603-399-6:185 |
0.346 |
|
1996 |
Saebo S, Keene E, Fang T, Lynn BC, Hicks RP. Modeling of the recognition site of the NK1 receptor Journal of Molecular Structure: Theochem. 366: 65-77. DOI: 10.1016/0166-1280(96)04552-6 |
0.353 |
|
1994 |
Young JK, Hicks RP. Nmr and molecular modeling investigations of the neuropeptide bradykinin in three different solvent systems: DMSO, 9:1 dioxane/water, and in the presence of 7.4 mM lyso phosphatidylcholine micelles. Biopolymers. 34: 611-23. PMID 8003621 DOI: 10.1002/Bip.360340504 |
0.321 |
|
1994 |
Young JK, Anklin C, Hicks RP. NMR and molecular modeling investigations of the neuropeptide substance P in the presence of 15 mM sodium dodecyl sulfate micelles. Biopolymers. 34: 1449-62. PMID 7530057 DOI: 10.1002/bip.360341102 |
0.339 |
|
1992 |
Graham WH, Carter ES, Hicks RP. Conformational analysis of Met-enkephalin in both aqueous solution and in the presence of sodium dodecyl sulfate micelles using multidimensional NMR and molecular modeling Biopolymers. 32: 1755-1764. PMID 1472657 DOI: 10.1002/Bip.360321216 |
0.35 |
|
1992 |
Young JK, Graham WH, Beard DJ, Hicks RP. The use of UV-visible spectroscopy for the determination of hydrophobic interactions between neuropeptides and membrane model systems. Biopolymers. 32: 1061-4. PMID 1420972 DOI: 10.1002/Bip.360320815 |
0.413 |
|
1992 |
Hicks RP, Beard DJ, Young JK. The interactions of neuropeptides with membrane model systems: a case study. Biopolymers. 32: 85-96. PMID 1377514 DOI: 10.1002/Bip.360320111 |
0.41 |
|
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