| Year |
Citation |
Score |
| 2023 |
Kimura T, Kimura AK, Epand RM. Systematic crosstalk in plasmalogen and diacyl lipid biosynthesis for their differential yet concerted molecular functions in the cell. Progress in Lipid Research. 91: 101234. PMID 37169310 DOI: 10.1016/j.plipres.2023.101234 |
0.336 |
|
| 2023 |
Pedrera L, Ros U, Fanani ML, Lanio ME, Epand RM, García-Sáez AJ, Álvarez C. The Important Role of Membrane Fluidity on the Lytic Mechanism of the α-Pore-Forming Toxin Sticholysin I. Toxins. 15. PMID 36668899 DOI: 10.3390/toxins15010080 |
0.342 |
|
| 2021 |
Bozelli JC, Yune J, Takahashi D, Sakane F, Epand RM. Membrane morphology determines diacylglycerol kinase α substrate acyl chain specificity. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 35: e21602. PMID 33977628 DOI: 10.1096/fj.202100264R |
0.322 |
|
| 2021 |
Bozelli JC, Aulakh SS, Epand RM. Membrane shape as determinant of protein properties. Biophysical Chemistry. 273: 106587. PMID 33865153 DOI: 10.1016/j.bpc.2021.106587 |
0.328 |
|
| 2020 |
Jennings W, Epand RM. CDP-diacylglycerol, a critical intermediate in lipid metabolism. Chemistry and Physics of Lipids. 230: 104914. PMID 32360136 DOI: 10.1016/j.chemphyslip.2020.104914 |
0.333 |
|
| 2020 |
Bozelli JC, Yune J, Dang X, Narayana JL, Wang G, Epand RM. Membrane activity of two short Trp-rich amphipathic peptides. Biochimica Et Biophysica Acta. Biomembranes. 1862: 183280. PMID 32220553 DOI: 10.1016/j.bbamem.2020.183280 |
0.405 |
|
| 2020 |
Bozelli JC, Hou YH, Schreier S, Epand RM. Lipid asymmetry of a model mitochondrial outer membrane affects Bax-dependent permeabilization. Biochimica Et Biophysica Acta. Biomembranes. 183241. PMID 32126227 DOI: 10.1016/j.bbamem.2020.183241 |
0.386 |
|
| 2019 |
Mesa-Galloso H, Valiente PA, Valdés-Tresanco ME, Epand RF, Lanio ME, Epand RM, Alvarez C, Tieleman DP, Ros U. Membrane Remodeling by the Lytic Fragment of SticholysinII: Implications for the Toroidal Pore Model. Biophysical Journal. PMID 31587828 DOI: 10.1016/j.bpj.2019.09.018 |
0.397 |
|
| 2019 |
Fantini J, Epand RM, Barrantes FJ. Cholesterol-Recognition Motifs in Membrane Proteins. Advances in Experimental Medicine and Biology. 1135: 3-25. PMID 31098808 DOI: 10.1007/978-3-030-14265-0_1 |
0.345 |
|
| 2019 |
Epand RM. Anionic Lipid Clustering Model. Advances in Experimental Medicine and Biology. 1117: 65-71. PMID 30980353 DOI: 10.1007/978-981-13-3588-4_5 |
0.366 |
|
| 2018 |
Bozelli JC, Jennings W, Black S, Hou YH, Lameire D, Chatha P, Kimura T, Berno B, Khondker A, Rheinstädter M, Epand RM. Membrane curvature allosterically regulates the phosphatidylinositol cycle, controlling its rate and acyl chain composition of its lipid intermediates. The Journal of Biological Chemistry. PMID 30237168 DOI: 10.1074/jbc.RA118.005293 |
0.348 |
|
| 2018 |
Dötsch V, Epand R, Millet O. Decision letter: Insights into the key determinants of membrane protein topology enable the identification of new monotopic folds Elife. DOI: 10.7554/Elife.40889.026 |
0.324 |
|
| 2017 |
Bozelli JC, Hou YH, Epand RM. Thermodynamics of methyl-β-cyclodextrin-induced lipid vesicle solubilization: Effect of lipid headgroup and backbone. Langmuir : the Acs Journal of Surfaces and Colloids. PMID 29120189 DOI: 10.1021/acs.langmuir.7b03447 |
0.342 |
|
| 2017 |
Epand RM. Features of the Phosphatidylinositol Cycle and its Role in Signal Transduction. The Journal of Membrane Biology. 250: 353-366. PMID 27278236 DOI: 10.1007/s00232-016-9909-y |
0.326 |
|
| 2016 |
Kimura T, Jennings W, Epand RM. Roles of specific lipid species in the cell and their molecular mechanism. Progress in Lipid Research. 62: 75-92. PMID 26875545 DOI: 10.1016/j.plipres.2016.02.001 |
0.318 |
|
| 2015 |
Epand RM, Walker C, Epand RF, Magarvey NA. Molecular mechanisms of membrane targeting antibiotics. Biochimica Et Biophysica Acta. PMID 26514603 DOI: 10.1016/J.Bbamem.2015.10.018 |
0.337 |
|
| 2015 |
Epand RM. Introduction to membrane lipids. Methods in Molecular Biology (Clifton, N.J.). 1232: 1-6. PMID 25331123 DOI: 10.1007/978-1-4939-1752-5_1 |
0.378 |
|
| 2015 |
Epand RM, D'Souza K, Berno B, Schlame M. Membrane curvature modulation of protein activity determined by NMR. Biochimica Et Biophysica Acta. 1848: 220-8. PMID 24835017 DOI: 10.1016/j.bbamem.2014.05.004 |
0.314 |
|
| 2014 |
Schlattner U, Tokarska-Schlattner M, Rousseau D, Boissan M, Mannella C, Epand R, Lacombe ML. Mitochondrial cardiolipin/phospholipid trafficking: the role of membrane contact site complexes and lipid transfer proteins. Chemistry and Physics of Lipids. 179: 32-41. PMID 24373850 DOI: 10.1016/J.Chemphyslip.2013.12.008 |
0.427 |
|
| 2013 |
Ros U, Edwards MA, Epand RF, Lanio ME, Schreier S, Yip CM, Alvarez C, Epand RM. The sticholysin family of pore-forming toxins induces the mixing of lipids in membrane domains. Biochimica Et Biophysica Acta. 1828: 2757-62. PMID 23954588 DOI: 10.1016/j.bbamem.2013.08.001 |
0.375 |
|
| 2013 |
Brown AC, Balashova NV, Epand RM, Epand RF, Bragin A, Kachlany SC, Walters MJ, Du Y, Boesze-Battaglia K, Lally ET. Aggregatibacter actinomycetemcomitans leukotoxin utilizes a cholesterol recognition/amino acid consensus site for membrane association. The Journal of Biological Chemistry. 288: 23607-21. PMID 23792963 DOI: 10.1074/jbc.M113.486654 |
0.314 |
|
| 2012 |
Schlame M, Acehan D, Berno B, Xu Y, Valvo S, Ren M, Stokes DL, Epand RM. The physical state of lipid substrates provides transacylation specificity for tafazzin. Nature Chemical Biology. 8: 862-9. PMID 22941046 DOI: 10.1038/Nchembio.1064 |
0.348 |
|
| 2012 |
Tokarska-Schlattner M, Epand RF, Meiler F, Zandomeneghi G, Neumann D, Widmer HR, Meier BH, Epand RM, Saks V, Wallimann T, Schlattner U. Phosphocreatine interacts with phospholipids, affects membrane properties and exerts membrane-protective effects. Plos One. 7: e43178. PMID 22912820 DOI: 10.1371/journal.pone.0043178 |
0.326 |
|
| 2012 |
Wadhwani P, Epand RF, Heidenreich N, Bürck J, Ulrich AS, Epand RM. Membrane-active peptides and the clustering of anionic lipids. Biophysical Journal. 103: 265-74. PMID 22853904 DOI: 10.1016/j.bpj.2012.06.004 |
0.388 |
|
| 2012 |
Brown AC, Boesze-Battaglia K, Du Y, Stefano FP, Kieba IR, Epand RF, Kakalis L, Yeagle PL, Epand RM, Lally ET. Aggregatibacter actinomycetemcomitans leukotoxin cytotoxicity occurs through bilayer destabilization. Cellular Microbiology. 14: 869-81. PMID 22309134 DOI: 10.1111/J.1462-5822.2012.01762.X |
0.377 |
|
| 2012 |
Aoki S, Epand RM. Caveolin-1 hydrophobic segment peptides insertion into membrane mimetic systems: role of proline residue. Biochimica Et Biophysica Acta. 1818: 12-8. PMID 21958667 DOI: 10.1016/j.bbamem.2011.09.009 |
0.365 |
|
| 2012 |
Epand RM. Recognition of polyunsaturated acyl chains by enzymes acting on membrane lipids. Biochimica Et Biophysica Acta. 1818: 957-62. PMID 21819965 DOI: 10.1016/j.bbamem.2011.07.018 |
0.311 |
|
| 2012 |
Epand RF, Wadhwani P, Heidenrich N, Burck J, Ulrich AS, Epand RM. The Clustering of Anionic Lipids by Highly Cationic Cell Penetrating Peptides, as with Antimicrobial Peptides, can Contribute to their Antimicrobial Activity Biophysical Journal. 102: 487a. DOI: 10.1016/J.BPJ.2011.11.2670 |
0.304 |
|
| 2011 |
Epand RF, Mor A, Epand RM. Lipid complexes with cationic peptides and OAKs; their role in antimicrobial action and in the delivery of antimicrobial agents. Cellular and Molecular Life Sciences : Cmls. 68: 2177-88. PMID 21573783 DOI: 10.1007/s00018-011-0711-9 |
0.36 |
|
| 2011 |
Epand RM, Epand RF. Bacterial membrane lipids in the action of antimicrobial agents. Journal of Peptide Science : An Official Publication of the European Peptide Society. 17: 298-305. PMID 21480436 DOI: 10.1002/psc.1319 |
0.37 |
|
| 2011 |
Epand RF, Sarig H, Ohana D, Papahadjopoulos-Sternberg B, Mor A, Epand RM. Physical properties affecting cochleate formation and morphology using antimicrobial oligo-acyl-lysyl peptide mimetics and mixtures mimicking the composition of bacterial membranes in the absence of divalent cations. The Journal of Physical Chemistry. B. 115: 2287-93. PMID 21332168 DOI: 10.1021/jp111242q |
0.366 |
|
| 2011 |
Guo L, Chen Z, Cox BE, Gragg S, Zhang Y, Amarnath V, van Lenten B, Epand R, Davies SS. Lipid Peroxidation Generates Aldehyde-Modified Phosphatidylethanolamines That Induce Inflammation Free Radical Biology and Medicine. 51: S103-S104. DOI: 10.1016/J.Freeradbiomed.2011.10.369 |
0.362 |
|
| 2010 |
Aoki S, Thomas A, Decaffmeyer M, Brasseur R, Epand RM. The role of proline in the membrane re-entrant helix of caveolin-1. The Journal of Biological Chemistry. 285: 33371-33380. PMID 20729193 DOI: 10.1074/jbc.M110.153569 |
0.332 |
|
| 2010 |
Epand RF, Pollard JE, Wright JO, Savage PB, Epand RM. Depolarization, bacterial membrane composition, and the antimicrobial action of ceragenins. Antimicrobial Agents and Chemotherapy. 54: 3708-13. PMID 20585129 DOI: 10.1128/Aac.00380-10 |
0.337 |
|
| 2010 |
Epand RF, Maloy L, Ramamoorthy A, Epand RM. Amphipathic helical cationic antimicrobial peptides promote rapid formation of crystalline states in the presence of phosphatidylglycerol: lipid clustering in anionic membranes. Biophysical Journal. 98: 2564-73. PMID 20513400 DOI: 10.1016/J.Bpj.2010.03.002 |
0.515 |
|
| 2010 |
Epand RF, Maloy WL, Ramamoorthy A, Epand RM. Probing the "charge cluster mechanism" in amphipathic helical cationic antimicrobial peptides. Biochemistry. 49: 4076-84. PMID 20387900 DOI: 10.1021/Bi100378M |
0.487 |
|
| 2010 |
Epand RM, Epand RF, Arnusch CJ, Papahadjopoulos-Sternberg B, Wang G, Shai Y. Lipid clustering by three homologous arginine-rich antimicrobial peptides is insensitive to amino acid arrangement and induced secondary structure. Biochimica Et Biophysica Acta. 1798: 1272-80. PMID 20302840 DOI: 10.1016/J.Bbamem.2010.03.012 |
0.404 |
|
| 2010 |
Epand RM, Thomas A, Brasseur R, Epand RF. Cholesterol interaction with proteins that partition into membrane domains: an overview. Sub-Cellular Biochemistry. 51: 253-78. PMID 20213547 DOI: 10.1007/978-90-481-8622-8_9 |
0.36 |
|
| 2010 |
Oreopoulos J, Epand RF, Epand RM, Yip CM. Peptide-induced domain formation in supported lipid bilayers: direct evidence by combined atomic force and polarized total internal reflection fluorescence microscopy. Biophysical Journal. 98: 815-23. PMID 20197035 DOI: 10.1016/j.bpj.2009.12.4327 |
0.364 |
|
| 2010 |
Sackett K, Nethercott MJ, Epand RF, Epand RM, Kindra DR, Shai Y, Weliky DP. Comparative analysis of membrane-associated fusion peptide secondary structure and lipid mixing function of HIV gp41 constructs that model the early pre-hairpin intermediate and final hairpin conformations. Journal of Molecular Biology. 397: 301-15. PMID 20080102 DOI: 10.1016/J.Jmb.2010.01.018 |
0.331 |
|
| 2010 |
Epand RM, Epand RF. Breaching the Membrane Barrier with Antimicrobial Agents that Cluster Anionic Lipids Biophysical Journal. 98: 436a. DOI: 10.1016/J.BPJ.2009.12.2366 |
0.334 |
|
| 2010 |
Epand RF, Epand RM, Arnusch CJ, Papahadjopoulos-Sternberg B, Wang G, Shai Y. Lipid Clustering by Three Homologous Arginine-Rich Antimicrobial Peptides is Insensitive to Amino Acid Arrangement Biophysical Journal. 98: 2-8. DOI: 10.1016/J.Bpj.2009.12.1175 |
0.392 |
|
| 2009 |
Epand RF, Wang G, Berno B, Epand RM. Lipid segregation explains selective toxicity of a series of fragments derived from the human cathelicidin LL-37. Antimicrobial Agents and Chemotherapy. 53: 3705-14. PMID 19581460 DOI: 10.1128/AAC.00321-09 |
0.349 |
|
| 2009 |
Epand RM, Epand RF. Domains in bacterial membranes and the action of antimicrobial agents. Molecular Biosystems. 5: 580-7. PMID 19462015 DOI: 10.1039/b900278m |
0.322 |
|
| 2009 |
Lev N, Fridmann-Sirkis Y, Blank L, Bitler A, Epand RF, Epand RM, Shai Y. Conformational stability and membrane interaction of the full-length ectodomain of HIV-1 gp41: implication for mode of action. Biochemistry. 48: 3166-75. PMID 19206186 DOI: 10.1021/Bi802243J |
0.337 |
|
| 2009 |
Epand RM, Rotem S, Mor A, Berno B, Epand RF. Lipid Domains in Bacterial Membranes as a Predictor of Antimicrobial Potency Biophysical Journal. 96: 450a. DOI: 10.1016/J.BPJ.2008.12.2312 |
0.33 |
|
| 2008 |
Vishwanathan SA, Thomas A, Brasseur R, Epand RF, Hunter E, Epand RM. Large changes in the CRAC segment of gp41 of HIV do not destroy fusion activity if the segment interacts with cholesterol. Biochemistry. 47: 11869-76. PMID 18937430 DOI: 10.1021/Bi8014828 |
0.342 |
|
| 2008 |
Epand RM, Rotem S, Mor A, Berno B, Epand RF. Bacterial membranes as predictors of antimicrobial potency. Journal of the American Chemical Society. 130: 14346-52. PMID 18826221 DOI: 10.1021/ja8062327 |
0.308 |
|
| 2008 |
Epand RM, Epand RF. Lipid domains in bacterial membranes and the action of antimicrobial agents. Biochimica Et Biophysica Acta. 1788: 289-94. PMID 18822270 DOI: 10.1016/j.bbamem.2008.08.023 |
0.366 |
|
| 2008 |
Epand RM. Proteins and cholesterol-rich domains. Biochimica Et Biophysica Acta. 1778: 1576-82. PMID 18423371 DOI: 10.1016/j.bbamem.2008.03.016 |
0.347 |
|
| 2008 |
Greenwood AI, Pan J, Mills TT, Nagle JF, Epand RM, Tristram-Nagle S. CRAC motif peptide of the HIV-1 gp41 protein thins SOPC membranes and interacts with cholesterol. Biochimica Et Biophysica Acta. 1778: 1120-30. PMID 18262490 DOI: 10.1016/J.Bbamem.2008.01.008 |
0.326 |
|
| 2008 |
Bach D, Epand RF, Epand RM, Wachtel E. Interaction of 7-ketocholesterol with two major components of the inner leaflet of the plasma membrane: phosphatidylethanolamine and phosphatidylserine. Biochemistry. 47: 3004-12. PMID 18247524 DOI: 10.1021/bi702070b |
0.349 |
|
| 2008 |
Epand RF, Zhang YL, Mirzabekov T, Kagan B, Silberstein A, Hubbell WL, Epand RM, Chakraborti S, Dimitrov DS, Anderson WF, Rozenberg-Adler Y. Membrane activity of an amphiphilic alpha-helical membrane-proximal cytoplasmic domain of the MoMuLV envelope glycoprotein. Experimental and Molecular Pathology. 84: 9-17. PMID 18206141 DOI: 10.1016/j.yexmp.2007.11.003 |
0.385 |
|
| 2008 |
Benatti CR, Lamy MT, Epand RM. Cationic amphiphiles and the solubilization of cholesterol crystallites in membrane bilayers. Biochimica Et Biophysica Acta. 1778: 844-53. PMID 18201547 DOI: 10.1016/j.bbamem.2007.12.011 |
0.363 |
|
| 2008 |
Shaw JE, Epand RF, Hsu JC, Mo GC, Epand RM, Yip CM. Cationic peptide-induced remodelling of model membranes: direct visualization by in situ atomic force microscopy. Journal of Structural Biology. 162: 121-38. PMID 18180166 DOI: 10.1016/j.jsb.2007.11.003 |
0.339 |
|
| 2007 |
Atkinson J, Epand RF, Epand RM. Tocopherols and tocotrienols in membranes: a critical review. Free Radical Biology & Medicine. 44: 739-64. PMID 18160049 DOI: 10.1016/J.FREERADBIOMED.2007.11.010 |
0.368 |
|
| 2007 |
Epand RM. Membrane lipid polymorphism: relationship to bilayer properties and protein function. Methods in Molecular Biology (Clifton, N.J.). 400: 15-26. PMID 17951724 DOI: 10.1007/978-1-59745-519-0_2 |
0.372 |
|
| 2007 |
Glukhov E, Shulga YV, Epand RF, Dicu AO, Topham MK, Deber CM, Epand RM. Membrane interactions of the hydrophobic segment of diacylglycerol kinase epsilon. Biochimica Et Biophysica Acta. 1768: 2549-58. PMID 17669357 DOI: 10.1016/J.Bbamem.2007.06.012 |
0.405 |
|
| 2007 |
Epand RF, Savage PB, Epand RM. Bacterial lipid composition and the antimicrobial efficacy of cationic steroid compounds (Ceragenins). Biochimica Et Biophysica Acta. 1768: 2500-9. PMID 17599802 DOI: 10.1016/J.Bbamem.2007.05.023 |
0.312 |
|
| 2006 |
Epand RF, Schlattner U, Wallimann T, Lacombe ML, Epand RM. Novel lipid transfer property of two mitochondrial proteins that bridge the inner and outer membranes. Biophysical Journal. 92: 126-37. PMID 17028143 DOI: 10.1529/BIOPHYSJ.106.092353 |
0.361 |
|
| 2006 |
Shaw JE, Epand RF, Sinnathamby K, Li Z, Bittman R, Epand RM, Yip CM. Tracking peptide-membrane interactions: insights from in situ coupled confocal-atomic force microscopy imaging of NAP-22 peptide insertion and assembly. Journal of Structural Biology. 155: 458-69. PMID 16889981 DOI: 10.1016/J.Jsb.2006.04.015 |
0.323 |
|
| 2006 |
Epand RF, Thomas A, Brasseur R, Vishwanathan SA, Hunter E, Epand RM. Juxtamembrane protein segments that contribute to recruitment of cholesterol into domains. Biochemistry. 45: 6105-14. PMID 16681383 DOI: 10.1021/BI060245+ |
0.352 |
|
| 2006 |
Epand RF, Ramamoorthy A, Epand RM. Membrane lipid composition and the interaction of pardaxin: the role of cholesterol. Protein and Peptide Letters. 13: 1-5. PMID 16454662 DOI: 10.2174/092986606774502063 |
0.489 |
|
| 2005 |
Epand RM, Rychnovsky SD, Belani JD, Epand RF. Role of chirality in peptide-induced formation of cholesterol-rich domains. The Biochemical Journal. 390: 541-8. PMID 15929726 DOI: 10.1042/Bj20050649 |
0.361 |
|
| 2005 |
Epand RF, Sayer BG, Epand RM. Induction of raft-like domains by a myristoylated NAP-22 peptide and its Tyr mutant. The Febs Journal. 272: 1792-803. PMID 15794765 DOI: 10.1111/j.1742-4658.2005.04612.x |
0.317 |
|
| 2005 |
Epand RM, Sayer BG, Epand RF. Caveolin scaffolding region and cholesterol-rich domains in membranes. Journal of Molecular Biology. 345: 339-50. PMID 15571726 DOI: 10.1016/J.JMB.2004.10.064 |
0.356 |
|
| 2005 |
Epand RM. Do proteins facilitate the formation of cholesterol-rich domains? Biochimica Et Biophysica Acta. 1666: 227-38. PMID 15519317 DOI: 10.1016/j.bbamem.2004.07.004 |
0.347 |
|
| 2004 |
Epand RM, Epand RF, Sayer BG, Datta G, Chaddha M, Anantharamaiah GM. Two homologous apolipoprotein AI mimetic peptides. Relationship between membrane interactions and biological activity. Journal of Biological Chemistry. 279: 51404-51414. PMID 15358763 DOI: 10.1074/Jbc.M408581200 |
0.32 |
|
| 2004 |
Epand RM, Epand RF, Sayer BG, Melacini G, Palgulachari MN, Segrest JP, Anantharamaiah GM. An Apolipoprotein AI Mimetic Peptide: Membrane Interactions and the Role of Cholesterol Biochemistry. 43: 5073-5083. PMID 15109266 DOI: 10.1021/Bi049786U |
0.373 |
|
| 2004 |
Shmulevitz M, Epand RF, Epand RM, Duncan R. Structural and functional properties of an unusual internal fusion peptide in a nonenveloped virus membrane fusion protein. Journal of Virology. 78: 2808-18. PMID 14990700 DOI: 10.1128/Jvi.78.6.2808-2818.2004 |
0.333 |
|
| 2004 |
Epand RM, Sayer BG, Epand RF. Peptide-induced formation of cholesterol-rich domains. Biochemistry. 42: 14677-89. PMID 14661981 DOI: 10.1021/BI035587J |
0.373 |
|
| 2004 |
Epand RF, Martinou JC, Montessuit S, Epand RM. Transbilayer lipid diffusion promoted by Bax: implications for apoptosis. Biochemistry. 42: 14576-82. PMID 14661970 DOI: 10.1021/BI035348W |
0.326 |
|
| 2004 |
Peggion C, Formaggio F, Crisma M, Epand RF, Epand RM, Toniolo C. Trichogin: a paradigm for lipopeptaibols. Journal of Peptide Science : An Official Publication of the European Peptide Society. 9: 679-89. PMID 14658789 DOI: 10.1002/PSC.500 |
0.322 |
|
| 2004 |
Epand RF, Maekawa S, Epand RM. Specificity of membrane binding of the neuronal protein NAP-22. The Journal of Membrane Biology. 193: 171-6. PMID 12962277 DOI: 10.1007/s00232-003-2015-y |
0.321 |
|
| 2004 |
Bertocco A, Formaggio F, Toniolo C, Broxterman QB, Epand RF, Epand RM. Design and function of a conformationally restricted analog of the influenza virus fusion peptide. The Journal of Peptide Research : Official Journal of the American Peptide Society. 62: 19-26. PMID 12787447 DOI: 10.1034/J.1399-3011.2003.00063.X |
0.314 |
|
| 2004 |
Epand RM. Cholesterol in bilayers of sphingomyelin or dihydrosphingomyelin at concentrations found in ocular lens membranes. Biophysical Journal. 84: 3102-10. PMID 12719240 DOI: 10.1016/S0006-3495(03)70035-6 |
0.306 |
|
| 2003 |
Epand RM. Fusion peptides and the mechanism of viral fusion. Biochimica Et Biophysica Acta. 1614: 116-21. PMID 12873772 DOI: 10.1016/s0005-2736(03)00169-x |
0.303 |
|
| 2003 |
Epand RF, Lehrer RI, Waring A, Wang W, Maget-Dana R, Lelièvre D, Epand RM. Direct comparison of membrane interactions of model peptides composed of only Leu and Lys residues. Biopolymers. 71: 2-16. PMID 12712497 DOI: 10.1002/bip.10372 |
0.347 |
|
| 2003 |
Epand RM, Epand RF, Maekawa S. The arrangement of cholesterol in membranes and binding of NAP-22. Chemistry and Physics of Lipids. 122: 33-9. PMID 12598036 DOI: 10.1016/S0009-3084(02)00176-7 |
0.391 |
|
| 2002 |
Schibli DJ, Epand RF, Vogel HJ, Epand RM. Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 80: 667-77. PMID 12440706 DOI: 10.1139/O02-147 |
0.349 |
|
| 2002 |
Terashita A, Funatsu N, Umeda M, Shimada Y, Ohno-Iwashita Y, Epand RM, Maekawa S. Lipid binding activity of a neuron-specific protein NAP-22 studied in vivo and in vitro. Journal of Neuroscience Research. 70: 172-9. PMID 12271466 DOI: 10.1002/jnr.10407 |
0.325 |
|
| 2002 |
Tachi T, Epand RF, Epand RM, Matsuzaki K. Position-dependent hydrophobicity of the antimicrobial magainin peptide affects the mode of peptide-lipid interactions and selective toxicity. Biochemistry. 41: 10723-31. PMID 12186559 DOI: 10.1021/BI0256983 |
0.333 |
|
| 2002 |
Epand RF, Martinou JC, Montessuit S, Epand RM. Membrane perturbations induced by the apoptotic Bax protein. The Biochemical Journal. 367: 849-55. PMID 12180909 DOI: 10.1042/BJ20020986 |
0.313 |
|
| 2002 |
Epand RF, Martinou JC, Fornallaz-Mulhauser M, Hughes DW, Epand RM. The apoptotic protein tBid promotes leakage by altering membrane curvature. The Journal of Biological Chemistry. 277: 32632-9. PMID 12082098 DOI: 10.1074/jbc.M202396200 |
0.356 |
|
| 2002 |
Vogel HJ, Schibli DJ, Jing W, Lohmeier-Vogel EM, Epand RF, Epand RM. Towards a structure-function analysis of bovine lactoferricin and related tryptophan- and arginine-containing peptides. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 80: 49-63. PMID 11908643 DOI: 10.1139/O01-213 |
0.321 |
|
| 2001 |
Toniolo C, Crisma M, Formaggio F, Peggion C, Epand RF, Epand RM. Lipopeptaibols, a novel family of membrane active, antimicrobial peptides. Cellular and Molecular Life Sciences : Cmls. 58: 1179-88. PMID 11577977 DOI: 10.1007/PL00000932 |
0.312 |
|
| 2001 |
Epand RM, Maekawa S, Yip CM, Epand RF. Protein-induced formation of cholesterol-rich domains. Biochemistry. 40: 10514-21. PMID 11523993 DOI: 10.1021/bi010897s |
0.36 |
|
| 2001 |
Epand RM, Epand RF, Martin I, Ruysschaert JM. Membrane interactions of mutated forms of the influenza fusion peptide. Biochemistry. 40: 8800-7. PMID 11467940 DOI: 10.1021/BI0107187 |
0.341 |
|
| 2001 |
Leikina E, LeDuc DL, Macosko JC, Epand R, Epand R, Shin YK, Chernomordik LV. The 1-127 HA2 construct of influenza virus hemagglutinin induces cell-cell hemifusion. Biochemistry. 40: 8378-86. PMID 11444985 DOI: 10.1021/Bi010466+ |
0.387 |
|
| 2001 |
Blazyk J, Wiegand R, Klein J, Hammer J, Epand RM, Epand RF, Maloy WL, Kari UP. A novel linear amphipathic beta-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids. The Journal of Biological Chemistry. 276: 27899-906. PMID 11352918 DOI: 10.1074/JBC.M102865200 |
0.339 |
|
| 2001 |
Boggs JM, Jo E, Polozov IV, Epand RF, Anantharamaiah GM, Blazyk J, Epand RM. Effect of magainin, class L, and class A amphipathic peptides on fatty acid spin labels in lipid bilayers. Biochimica Et Biophysica Acta. 1511: 28-41. PMID 11248202 DOI: 10.1016/S0005-2736(00)00379-5 |
0.374 |
|
| 2001 |
Epand RM, Epand RF. Modulation of membrane curvature by peptides. Biopolymers. 55: 358-63. PMID 11241210 DOI: 10.1002/1097-0282(2000)55:5<358::AID-BIP1009>3.0.CO;2-8 |
0.346 |
|
| 2001 |
Epand RF, Epand RM, Formaggio F, Crisma M, Wu H, Lehrer RI, Toniolo C. Analogs of the antimicrobial peptide trichogin having opposite membrane properties. European Journal of Biochemistry. 268: 703-12. PMID 11168409 DOI: 10.1046/J.1432-1327.2001.01922.X |
0.346 |
|
| 2000 |
Peisajovich SG, Epand RF, Pritsker M, Shai Y, Epand RM. The polar region consecutive to the HIV fusion peptide participates in membrane fusion. Biochemistry. 39: 1826-33. PMID 10677233 DOI: 10.1021/Bi991887I |
0.3 |
|
| 2000 |
Epand RF, Epand RM, Monaco V, Stoia S, Formaggio F, Crisma M, Toniolo C. The antimicrobial peptide trichogin and its interaction with phospholipid membranes. European Journal of Biochemistry. 266: 1021-8. PMID 10583397 DOI: 10.1046/J.1432-1327.1999.00945.X |
0.35 |
|
| 1999 |
Epand RF, Macosko JC, Russell CJ, Shin YK, Epand RM. The ectodomain of HA2 of influenza virus promotes rapid pH dependent membrane fusion. Journal of Molecular Biology. 286: 489-503. PMID 9973566 DOI: 10.1006/Jmbi.1998.2500 |
0.326 |
|
| 1998 |
Davies SM, Epand RF, Bradshaw JP, Epand RM. Modulation of lipid polymorphism by the feline leukemia virus fusion peptide: implications for the fusion mechanism. Biochemistry. 37: 5720-9. PMID 9548958 DOI: 10.1021/BI980227V |
0.335 |
|
| 1997 |
Latal A, Degovics G, Epand RF, Epand RM, Lohner K. Structural aspects of the interaction of peptidyl-glycylleucine-carboxyamide, a highly potent antimicrobial peptide from frog skin, with lipids. European Journal of Biochemistry. 248: 938-46. PMID 9342250 DOI: 10.1111/J.1432-1033.1997.00938.X |
0.407 |
|
| 1997 |
Epand RF, Moroder L, Lutz J, Flanagan TD, Nir S, Epand RM. Lipogastrins as potent inhibitors of viral fusion. Biochimica Et Biophysica Acta. 1327: 259-268. PMID 9271268 DOI: 10.1016/S0005-2736(97)00074-6 |
0.389 |
|
| 1995 |
Epand RF, Martin I, Ruysschaert JM, Epand RM. Membrane orientation of the SIV fusion peptide determines its effect on bilayer stability and ability to promote membrane fusion. Biochemical and Biophysical Research Communications. 205: 1938-43. PMID 7811285 DOI: 10.1006/BBRC.1994.2897 |
0.366 |
|
| 1993 |
Epand RM, Epand RF, Richardson CD, Yeagle PL. Structural requirements for the inhibition of membrane fusion by carbobenzoxy-d-Phe-Phe-Gly Bba - Biomembranes. 1152: 128-134. PMID 8399290 DOI: 10.1016/0005-2736(93)90239-V |
0.375 |
|
| 1993 |
Epand RF, Xue CB, Wang SH, Naider F, Becker JM, Epand RM. Role of prenylation in the interaction of the a-factor mating pheromone with phospholipid bilayers. Biochemistry. 32: 8368-73. PMID 8347633 DOI: 10.1021/Bi00083A041 |
0.311 |
|
| 1992 |
Epand RM, Cheetham JJ, Epand RF, Yeagle PL, Richardson CD, Rockwell A, Degrado WF. Peptide models for the membrane destabilizing actions of viral fusion proteins. Biopolymers. 32: 309-14. PMID 1623124 DOI: 10.1002/Bip.360320403 |
0.338 |
|
| 1992 |
Epand RM, Stafford A, Wang J, Epand RF. Zwitterionic amphiphiles that raise the bilayer to hexagonal phase transition temperature inhibit protein kinase C. The exception that proves the rule. Febs Letters. 304: 245-8. PMID 1618330 DOI: 10.1016/0014-5793(92)80629-U |
0.308 |
|
| 1988 |
Epand RM, Epand RF, Orlowski RC. Biologically active calcitonin analogs which have minimal interactions with phospholipids. Biochemical and Biophysical Research Communications. 152: 203-7. PMID 3358761 DOI: 10.1016/S0006-291X(88)80700-9 |
0.314 |
|
| 1986 |
Surewicz WK, Epand RM, Epand RF, Hallett FR, Moscarello MA. Modulation of myelin basic protein-induced aggregation and fusion of liposomes by cholesterol, aliphatic aldehydes and alkanes. Biochimica Et Biophysica Acta. 863: 45-52. PMID 2430621 DOI: 10.1016/0005-2736(86)90385-8 |
0.301 |
|
| 1985 |
Epand RM, Epand RF, Orlowski RC, Flanigan E, Stahl GL. A comparison of the interaction of glucagon, human parathyroid hormone-(1-34)-peptide and calcitonin with dimyristoylphosphatidylglycerol and with dimyristoylphosphatidylcholine Biophysical Chemistry. 23: 39-48. PMID 4092081 DOI: 10.1016/0301-4622(85)80062-4 |
0.301 |
|
| 1985 |
Epand RM, Epand RF, Hui SW, He NB, Rosenblatt M. Formation of water-soluble complex between the 1-34 fragment of parathyroid hormone and dimyristoylphosphatidylcholine International Journal of Peptide and Protein Research. 25: 594-600. PMID 4030217 |
0.322 |
|
| 1984 |
Hui SW, Epand RM, Dell KR, Epand RF, Orlowski RC. Effects of lipid structure on peptide-lipid interactions complexes of salmon calcitonin with phosphatidylglycerol and with phosphatidic acid Bba - Biomembranes. 772: 264-272. PMID 6722149 DOI: 10.1016/0005-2736(84)90143-3 |
0.346 |
|
| 1983 |
Epand RM, Epand RF, Orlowski RC, Schlueter RJ, Boni LT, Hui SW. Amphipathic helix and its relationship to the interaction of calcitonin with phospholipids Biochemistry. 22: 5074-5084. PMID 6652057 |
0.364 |
|
| 1980 |
Epand RM, Epand R. The role of the phospholipid phase transition in the regulation of glucagon binding to lecithin. Biochimica Et Biophysica Acta. 602: 600-609. PMID 7437423 DOI: 10.1016/0005-2736(80)90338-7 |
0.362 |
|
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