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Research papers

  1. Zhang, T. et al. (2016) Membrane binding and oligomer formation of the calcium-dependent lipopeptide antibiotic A54145: a quantitative study with pyrene excimer fluorescence. Biophys J (in press):x-x
  2. Taylor, R. M. et al. (2016) Two successive calcium-dependent transitions mediate membrane binding and oligomerization of daptomycin and the related antibiotic A54145. BBA Biomembranes 1858:1999-2005
  3. Lohani, Chuda Raj et al. (2016) α-Azido Acids in Solid-Phase Peptide Synthesis: Compatibility with Fmoc Chemistry and an Alternative Approach to the Solid Phase Synthesis of Daptomycin Analogs. J Org Chem 81:2624-8
  4. Ellis, R. and Palmer, M. (2016) Modulation of ice ages via precession and dust-albedo feedbacks. Geoscience Frontiers in press:x-x
  5. Lohani, C. et al. (2015) Solid-Phase Total Synthesis of Daptomycin and Analogs. Organic Letters 17:748-751
  6. Lohani, Chuda Raj et al. (2015) Solid-phase synthesis and in vitro biological activity of a Thr4→Ser4 analog of daptomycin. Bioorg Med Chem Lett 25:5490-4
  7. Zhang, T. et al. (2014) Daptomycin forms cation- and size-selective pores in model membranes. Biochim Biophys Acta 1838:2425-2430
  8. Zhang, TianHua et al. (2014) Cardiolipin prevents membrane translocation and permeabilization by daptomycin. J Biol Chem 289:11584-91
  9. Pokrajac, Lisa et al. (2013) Oligomerization and hemolytic properties of the C-terminal domain of pyolysin, a cholesterol-dependent cytolysin. Biochem Cell Biol 91:59-66
  10. Zhang, Tianhua et al. (2013) Mutual inhibition through hybrid oligomer formation of daptomycin and the semisynthetic lipopeptide antibiotic CB-182,462. Biochim Biophys Acta 1828:302-8
  11. Palmer, Michael (2013) Combination treatment of epilepsy with ketogenic diet and concurrent pharmacological inhibition of cytochrome P450 2E1. Med Hypotheses 80:481-5
  12. Brefo-Mensah, Eric K. and Palmer, Michael (2012) mol2chemfig, a tool for rendering chemical structures from molfile or SMILES format to LaTeX code. J Cheminform 4:24
  13. Muraih, Jawad K. et al. (2012) Characterization of daptomycin oligomerization with perylene excimer fluorescence: stoichiometric binding of phosphatidylglycerol triggers oligomer formation. Biochim Biophys Acta 1818:673-8
  14. Muraih, Jawad K. and Palmer, Michael (2012) Estimation of the subunit stoichiometry of the membrane-associated daptomycin oligomer by FRET. Biochim Biophys Acta 1818:1642-1647
  15. Pokrajac, Lisa et al. (2012) Partial oligomerization of pyolysin induced by a disulfide-tethered mutant. Biochem Cell Biol 90:709-717
  16. Harris, J. Robin et al. (2011) Cholesterol microcrystals and cochleate cylinders: attachment of pyolysin oligomers and domain 4. J Struct Biol 173:38-45
  17. Muraih, Jawad K. et al. (2011) Oligomerization of daptomycin on membranes. Biochim Biophys Acta 1808:1154-60
  18. Löhner, Sabine et al. (2009) Pore formation by Vibrio cholerae cytolysin follows the same archetypical mode as β-barrel toxins from gram-positive organisms. FASEB J 23:2521-8
  19. Spratt, Donald E. et al. (2008) FRET conformational analysis of calmodulin binding to nitric oxide synthase peptides and enzymes. Biochemistry 47:12006-17
  20. Wu, Xiaoming et al. (2008) Synthesis and biological evaluation of sperm CD52 GPI anchor and related derivatives as binding receptors of pore-forming CAMP factor. Carbohydr Res 343:1718-29
  21. El-Huneidi, Waseem et al. (2007) Streptococcus agalactiae CAMP factor/protein B does not bind to human IgG. Med Microbiol Immunol 196:73-7
  22. Lang, Shenhui et al. (2007) Streptococcus agalactiae CAMP factor binds to GPI-anchored proteins. Med Microbiol Immunol 196:1-10
  23. Spratt, Donald E. et al. (2007) Differential binding of calmodulin domains to constitutive and inducible nitric oxide synthase enzymes. Biochemistry 46:8288-300
  24. Lang, Shenhui et al. (2006) Selective labeling of selenomethionine residues in proteins with a fluorescent derivative of benzyl bromide. Anal Biochem 359:253-8
  25. Lang, Shenhui et al. (2005) Dual-targeted labeling of proteins using cysteine and selenomethionine residues. Anal Biochem 342:271-9
  26. Lang, Shenhui and Palmer, Michael (2003) Characterization of Streptococcus agalactiae CAMP factor as a pore-forming toxin. J Biol Chem 278:38167-73
  27. Palmer, Michael (2003) Efflux of cytoplasmically acting antibiotics from gram-negative bacteria: periplasmic substrate capture by multicomponent efflux pumps inferred from their cooperative action with single-component transporters. J Bacteriol 185:5287-9
  28. Zitzer, Alexander et al. (2003) Differential interaction of the two cholesterol-dependent, membrane-damaging toxins, streptolysin O and Vibrio cholerae cytolysin, with enantiomeric cholesterol. FEBS Lett 553:229-31
  29. Harris, J. Robin et al. (2002) Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: a TEM study. J Struct Biol 139:122-35
  30. Schindel, C. et al. (2001) Interaction of Escherichia coli hemolysin with biological membranes. A study using cysteine scanning mutagenesis. Eur J Biochem 268:800-8
  31. Valeva, A. et al. (2001) Membrane insertion of the heptameric staphylococcal α-toxin pore. A domino-like structural transition that is allosterically modulated by the target cell membrane. J Biol Chem 276:14835-41
  32. Zitzer, A. et al. (2001) Coupling of cholesterol and cone-shaped lipids in bilayers augments membrane permeabilization by the cholesterol-specific toxins streptolysin O and Vibrio cholerae cytolysin. J Biol Chem 276:14628-33
  33. Weis, S. and Palmer, M. (2001) Streptolysin O: the C-terminal, tryptophan-rich domain carries functional sites for both membrane binding and self-interaction but not for stable oligomerization. Biochim Biophys Acta 1510:292-9
  34. Valeva, A. et al. (2000) Staphylococcal α-toxin: repair of a calcium-impermeable pore in the target cell membrane. Mol Microbiol 36:467-76
  35. Zitzer, A. et al. (2000) Vibrio cholerae cytolysin: assembly and membrane insertion of the oligomeric pore are tightly linked and are not detectably restricted by membrane fluidity. Biochim Biophys Acta 1509:264-74
  36. Abdel Ghani, E. M. et al. (1999) Streptolysin O: inhibition of the conformational change during membrane binding of the monomer prevents oligomerization and pore formation. Biochemistry 38:15204-11
  37. Zitzer, A. et al. (1999) Oligomerization of Vibrio cholerae cytolysin yields a pentameric pore and has a dual specificity for cholesterol and sphingolipids in the target membrane. J Biol Chem 274:1375-80
  38. Gonelle-Gispert, C. et al. (1999) SNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretion. Biochem J 339 ( Pt 1):159-65
  39. Engel, F. et al. (1998) Bacterial cytolysin perturbs round window membrane permeability barrier in vivo: possible cause of sensorineural hearing loss in acute otitis media. Infect Immun 66:343-6
  40. Harris, JR et al. (1998) Cholesterol-Streptolysin O Interaction: An EM Study of Wild-Type and Mutant Streptolysin O. J Struct Biol 121:343-55
  41. Jahn, B. et al. (1998) Accumulation of amphotericin B in human macrophages enhances activity against Aspergillus fumigatus conidia: quantification of conidial kill at the single-cell level. Antimicrob Agents Chemother 42:2569-75
  42. Palmer, M. et al. (1998) Streptolysin O: a proposed model of allosteric interaction between a pore-forming protein and its target lipid bilayer. Biochemistry 37:2378-83
  43. Palmer, M. et al. (1998) Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization. EMBO J 17:1598-605
  44. Palmer, M. et al. (1997) Cysteine-specific radioiodination of proteins with fluorescein maleimide. Anal Biochem 253:175-9
  45. Valeva, A. et al. (1997) Staphylococcal α-toxin: formation of the heptameric pore is partially cooperative and proceeds through multiple intermediate stages. Biochemistry 36:13298-304
  46. Valeva, A. et al. (1997) Staphylococcal α-toxin: the role of the N-terminus in formation of the heptameric pore -- a fluorescence study. Biochim Biophys Acta 1325:281-6
  47. Valeva, A. et al. (1997) Transmembrane β-barrel of staphylococcal α-toxin forms in sensitive but not in resistant cells. Proc Natl Acad Sci U S A 94:11607-11
  48. Zitzer, A. et al. (1997) Mode of primary binding to target membranes and pore formation induced by Vibrio cholerae cytolysin (hemolysin). Eur J Biochem 247:209-16
  49. Palmer, M. et al. (1996) Membrane-penetrating domain of streptolysin O identified by cysteine scanning mutagenesis. J Biol Chem 271:26664-7
  50. Valeva, A. et al. (1996) Molecular architecture of a toxin pore: a 15-residue sequence lines the transmembrane channel of staphylococcal α-toxin. EMBO J 15:1857-64
  51. Walev, I. et al. (1996) Pore-forming toxins trigger shedding of receptors for interleukin 6 and lipopolysaccharide. Proc Natl Acad Sci U S A 93:7882-7
  52. Weller, U. et al. (1996) Expression of active streptolysin O in Escherichia coli as a maltose-binding-protein--streptolysin-O fusion protein. The N-terminal 70 amino acids are not required for hemolytic activity. Eur J Biochem 236:34-9
  53. Palmer, M. et al. (1995) Kinetics of streptolysin O self-assembly. Eur J Biochem 231:388-95
  54. Pinkney, M. et al. (1995) Different forms of streptolysin O produced by Streptococcus pyogenes and by Escherichia coli expressing recombinant toxin: cleavage by streptococcal cysteine protease. Infect Immun 63:2776-9
  55. Valeva, A. et al. (1995) Correct oligomerization is a prerequisite for insertion of the central molecular domain of staphylococcal α-toxin into the lipid bilayer. Biochim Biophys Acta 1236:213-8
  56. Walev, I. et al. (1995) Binding, oligomerization, and pore formation by streptolysin O in erythrocytes and fibroblast membranes: detection of nonlytic polymers. Infect Immun 63:1188-94
  57. Walev, I. et al. (1995) Potassium-inhibited processing of IL-1 β in human monocytes. EMBO J 14:1607-14
  58. Zitzer, A. et al. (1995) Characterization of Vibrio cholerae El Tor cytolysin as an oligomerizing pore-forming toxin. Med Microbiol Immunol 184:37-44
  59. Regazzi, R. et al. (1995) VAMP-2 and cellubrevin are expressed in pancreatic β-cells and are essential for Ca2+- but not for GTP γ S-induced insulin secretion. EMBO J 14:2723-30
  60. Engel, F. et al. (1995) Breakdown of the round window membrane permeability barrier evoked by streptolysin O: possible etiologic role in development of sensorineural hearing loss in acute otitis media. Infect Immun 63:1305-10
  61. Jonas, D. et al. (1994) Novel path to apoptosis: small transmembrane pores created by staphylococcal α-toxin in T lymphocytes evoke internucleosomal DNA degradation. Infect Immun 62:1304-12
  62. Walev, I. et al. (1994) Recovery of human fibroblasts from attack by the pore-forming α-toxin of Staphylococcus aureus. Microb Pathog 17:187-201
  63. Ward, R. J. et al. (1994) Identification of a putative membrane-inserted segment in the α-toxin of Staphylococcus aureus. Biochemistry 33:7477-84
  64. Jonas, J. C. et al. (1994) Dynamics of Ca2+ and guanosine 5'-[γ-thio]triphosphate action on insulin secretion from α-toxin-permeabilized HIT-T15 cells. Biochem J 301 ( Pt 2):523-9
  65. Palmer, M. et al. (1993) Staphylococcus aureus α-toxin. Production of functionally intact, site-specifically modifiable protein by introduction of cysteine at positions 69, 130, and 186. J Biol Chem 268:11959-62
  66. Palmer, M. et al. (1993) Altered pore-forming properties of proteolytically nicked staphylococcal α-toxin. J Biol Chem 268:11963-7


  1. Taylor, S. D. and Palmer, M. (2016) The action mechanism of daptomycin. Bioorganic and Medicinal Chemistry in press:x-x
  2. Harris, J. Robin and Palmer, Michael (2010) Cholesterol specificity of some heptameric β-barrel pore-forming bacterial toxins: structural and functional aspects. Subcell Biochem 51:579-96
  3. Palmer, Michael (2004) Cholesterol and the activity of bacterial toxins. FEMS Microbiol Lett 238:281-9
  4. Palmer, M. (2001) The family of thiol-activated, cholesterol-binding cytolysins. Toxicon 39:1681-9
  5. Bhakdi, S. et al. (1998) Pore-forming bacterial cytolysins. Symp Ser Soc Appl Microbiol 27:15S-25S
  6. Palmer, M. (1998) Staphyloccal α toxin. Symp Ser Soc Appl Microbiol 27:125S-126S
  7. Bhakdi, S. et al. (1996) Staphylococcal α-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins. Arch Microbiol 165:73-9
  8. Bhakdi, S. et al. (1996) Pathogenesis of sepsis syndrome: possible relevance of pore-forming bacterial toxins. Curr Top Microbiol Immunol 216:101-18
  9. Bhakdi, S. et al. (1993) A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes. Med Microbiol Immunol 182:167-75


  1. Palmer, M. (2014) Lecture notes on human metabolism (self-published).
  2. Palmer, M. et al. (2013) Notes to Biochemical Pharmacology (John Wiley and Sons).
  3. Palmer, M. et al. (2012) Biochemical Pharmacology (John Wiley and Sons).
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