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Volumn 45, Issue 26, 2006, Pages 8124-8134

Topography of the hydrophilic helices of membrane-inserted diphtheria toxin T domain: TH1-TH3 as a hydrophilic tether

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MATERIALS; HYDROPHILICITY; HYDROPHOBICITY; ISOMERS; PH EFFECTS; TOXIC MATERIALS;

EID: 33745626479     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060587f     Document Type: Article
Times cited : (17)

References (52)
  • 1
    • 0037053367 scopus 로고    scopus 로고
    • Topography of helices 5-7 in membrane-inserted diphtheria toxin T domain: Identification and insertion boundaries of two hydrophobic sequences that do not form a stable transmembrane hairpin
    • Rosconi, M. P., and London, E. (2002) Topography of helices 5-7 in membrane-inserted diphtheria toxin T domain: Identification and insertion boundaries of two hydrophobic sequences that do not form a stable transmembrane hairpin, J. Biol. Chem 277, 16517-16527.
    • (2002) J. Biol. Chem , vol.277 , pp. 16517-16527
    • Rosconi, M.P.1    London, E.2
  • 2
    • 0030803672 scopus 로고    scopus 로고
    • Identification of shallow and deep membrane-penetrating forms of diphtheria toxin T domain that are regulated by protein concentration and bilayer width
    • Wang, Y., Malenbaum, S. E., Kachel, K., Zhan, H., Collier, R. J., and London, E. (1997) Identification of shallow and deep membrane-penetrating forms of diphtheria toxin T domain that are regulated by protein concentration and bilayer width, J. Biol. Chem. 272, 25091-25098.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25091-25098
    • Wang, Y.1    Malenbaum, S.E.2    Kachel, K.3    Zhan, H.4    Collier, R.J.5    London, E.6
  • 3
    • 0032483451 scopus 로고    scopus 로고
    • Identifying transmembrane states and defining the membrane insertion boundaries of hydrophobic helices in membrane-inserted diphtheria toxin T domain
    • Kachel, K., Ren, J., Collier, R. J., and London, E. (1998) Identifying transmembrane states and defining the membrane insertion boundaries of hydrophobic helices in membrane-inserted diphtheria toxin T domain, J. Biol. Chem. 273, 22950-22956.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22950-22956
    • Kachel, K.1    Ren, J.2    Collier, R.J.3    London, E.4
  • 5
    • 0027495717 scopus 로고
    • Evidence for involvement of furin in cleavage and activation of diphtheria toxin
    • Tsuneoka, M., Nakayama, K., Hatsuzawa, K., Komada, M., Kitamura, N., and Mekada, E. (1993) Evidence for involvement of furin in cleavage and activation of diphtheria toxin, J. Biol. Chem. 268, 26461-26465.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26461-26465
    • Tsuneoka, M.1    Nakayama, K.2    Hatsuzawa, K.3    Komada, M.4    Kitamura, N.5    Mekada, E.6
  • 6
    • 0028304478 scopus 로고
    • Cleavage of pseudomonas exotoxin and diphtheria toxin by a furin-like enzyme prepared from beef liver
    • Chiron, M. F., Fryling, C. M., and FitzGerald, D. J. (1994) Cleavage of pseudomonas exotoxin and diphtheria toxin by a furin-like enzyme prepared from beef liver, J. Biol. Chem. 269, 18167-18176.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18167-18176
    • Chiron, M.F.1    Fryling, C.M.2    Fitzgerald, D.J.3
  • 7
    • 0026747170 scopus 로고
    • Expression cloning of a diphtheria toxin receptor: Identity with a heparin-binding EGF-like growth factor precursor
    • Naglich, J. G., Metherall, J. E., Russell, D. W., and Eidels, L. (1992) Expression cloning of a diphtheria toxin receptor: Identity with a heparin-binding EGF-like growth factor precursor, Cell 69, 1051-1061.
    • (1992) Cell , vol.69 , pp. 1051-1061
    • Naglich, J.G.1    Metherall, J.E.2    Russell, D.W.3    Eidels, L.4
  • 8
    • 0026574178 scopus 로고
    • Diphtheria toxin: Membrane interaction and membrane translocation
    • London, E. (1992) Diphtheria toxin: Membrane interaction and membrane translocation, Biochim. Biophys. Acta 1113, 25-51.
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 25-51
    • London, E.1
  • 10
    • 0022397324 scopus 로고
    • Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration
    • Blewitt, M. G., Chung, L. A., and London, E. (1985) Effect of pH on the conformation of diphtheria toxin and its implications for membrane penetration, Biochemistry 24, 5458-5464.
    • (1985) Biochemistry , vol.24 , pp. 5458-5464
    • Blewitt, M.G.1    Chung, L.A.2    London, E.3
  • 11
    • 0021126510 scopus 로고
    • Evidence for direct insertion of fragments A and B of diphtheria toxin into model membranes
    • Hu, V. W., and Holmes, R. K. (1984) Evidence for direct insertion of fragments A and B of diphtheria toxin into model membranes, J. Biol. Chem. 259, 12226-12233.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12226-12233
    • Hu, V.W.1    Holmes, R.K.2
  • 12
    • 0023696942 scopus 로고
    • Conformation and model membrane interactions of diphtheria toxin fragment A
    • Zhao, J. M., and London, E. (1988) Conformation and model membrane interactions of diphtheria toxin fragment A, J. Biol. Chem. 263, 15369-15377.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15369-15377
    • Zhao, J.M.1    London, E.2
  • 13
    • 0027989890 scopus 로고
    • Mutational analysis of the helical hairpin region of diphtheria toxin transmembrane domain
    • Silverman, J. A., Mindell, J. A., Finkelstein, A., Shen, W. H., and Collier, R. J. (1994) Mutational analysis of the helical hairpin region of diphtheria toxin transmembrane domain, J. Biol. Chem. 269, 22524-22532.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22524-22532
    • Silverman, J.A.1    Mindell, J.A.2    Finkelstein, A.3    Shen, W.H.4    Collier, R.J.5
  • 14
    • 0028846613 scopus 로고
    • Immunochemical analysis shows all three domains of diphtheria toxin penetrate across model membranes
    • Tortorella, D., Sesardic, D., Dawes, C. S., and London, E. (1995) Immunochemical analysis shows all three domains of diphtheria toxin penetrate across model membranes, J. Biol. Chem. 270, 27446-27452.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27446-27452
    • Tortorella, D.1    Sesardic, D.2    Dawes, C.S.3    London, E.4
  • 16
    • 0034697302 scopus 로고    scopus 로고
    • Organization of diphtheria toxin in membranes. A hydrophobic photolabeling study
    • D'Silva, P. R., and Lala, A. K. (2000) Organization of diphtheria toxin in membranes. A hydrophobic photolabeling study, J. Biol. Chem. 275, 11771-11777.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11771-11777
    • D'Silva, P.R.1    Lala, A.K.2
  • 17
    • 13544273837 scopus 로고    scopus 로고
    • Topography of diphtheria toxin A chain inserted into lipid vesicles
    • Hayashibara, M., and London, E. (2005) Topography of diphtheria toxin A chain inserted into lipid vesicles, Biochemistry 44, 2183-2196.
    • (2005) Biochemistry , vol.44 , pp. 2183-2196
    • Hayashibara, M.1    London, E.2
  • 18
    • 0000483941 scopus 로고    scopus 로고
    • Translocation of the catalytic domain of diphtheria toxin across planar phospholipid bilayers by its own T domain
    • Oh, K. J., Senzel, L., Collier, R. J., and Finkelstein, A. (1999) Translocation of the catalytic domain of diphtheria toxin across planar phospholipid bilayers by its own T domain, Proc. Natl. Acad. Sci. U.S.A. 96, 8467-8470.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 8467-8470
    • Oh, K.J.1    Senzel, L.2    Collier, R.J.3    Finkelstein, A.4
  • 19
    • 0019819794 scopus 로고
    • Diphtheria toxin fragment forms large pores in phospholipid bilayer membranes
    • Kagan, B. L., Finkelstein, A., and Colombini, M. (1981) Diphtheria toxin fragment forms large pores in phospholipid bilayer membranes, Proc. Natl. Acad. Sci. U.S.A. 78, 4950-4954.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 4950-4954
    • Kagan, B.L.1    Finkelstein, A.2    Colombini, M.3
  • 20
    • 0033214894 scopus 로고    scopus 로고
    • The effects of inhibitors upon pore formation by diphtheria toxin and diphtheria toxin T domain
    • Sharpe, J. C., Kachel, K., and London, E. (1999) The effects of inhibitors upon pore formation by diphtheria toxin and diphtheria toxin T domain, J. Membr. Biol. 171, 223-233.
    • (1999) J. Membr. Biol. , vol.171 , pp. 223-233
    • Sharpe, J.C.1    Kachel, K.2    London, E.3
  • 21
    • 0033215457 scopus 로고    scopus 로고
    • Diphtheria toxin forms pores of different sizes depending on its concentration in membranes: Probable relationship to oligomerization
    • Sharpe, J. C., and London, E. (1999) Diphtheria toxin forms pores of different sizes depending on its concentration in membranes: Probable relationship to oligomerization, J. Membr. Biol. 171, 209-221.
    • (1999) J. Membr. Biol. , vol.171 , pp. 209-221
    • Sharpe, J.C.1    London, E.2
  • 22
    • 3142667679 scopus 로고    scopus 로고
    • Analyzing topography of membrane-inserted diphtheria toxin T domain using BODIPY-streptavidin: At low pH, helices 8 and 9 form a transmembrane hairpin but helices 5-7 form stable nonclassical inserted segments on the cis side of the bilayer
    • Rosconi, M. P., Zhao, G., and London, E. (2004) Analyzing topography of membrane-inserted diphtheria toxin T domain using BODIPY-streptavidin: At low pH, helices 8 and 9 form a transmembrane hairpin but helices 5-7 form stable nonclassical inserted segments on the cis side of the bilayer, Biochemistry 43, 9127-9139.
    • (2004) Biochemistry , vol.43 , pp. 9127-9139
    • Rosconi, M.P.1    Zhao, G.2    London, E.3
  • 23
    • 0033532355 scopus 로고    scopus 로고
    • Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation
    • Ren, J., Kachel, K., Kim, H., Malenbaum, S. E., Collier, R. J., and London, E. (1999) Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation, Science 284, 955-957.
    • (1999) Science , vol.284 , pp. 955-957
    • Ren, J.1    Kachel, K.2    Kim, H.3    Malenbaum, S.E.4    Collier, R.J.5    London, E.6
  • 24
    • 0037022793 scopus 로고    scopus 로고
    • Interaction of the membrane-inserted diphtheria toxin T domain with peptides and its possible implications for chaperone-like T domain behavior
    • Hammond, K., Caputo, G. A., and London, E. (2002) Interaction of the membrane-inserted diphtheria toxin T domain with peptides and its possible implications for chaperone-like T domain behavior, Biochemistry 41, 3243-3253.
    • (2002) Biochemistry , vol.41 , pp. 3243-3253
    • Hammond, K.1    Caputo, G.A.2    London, E.3
  • 25
    • 27344460405 scopus 로고    scopus 로고
    • A conserved motif in transmembrane helix 1 of diphtheria toxin mediates catalytic domain delivery to the cytosol
    • Ratts, R., Trujillo, C., Bharti, A., vanderSpek, J., Harrison, R., and Murphy, J. R. (2005) A conserved motif in transmembrane helix 1 of diphtheria toxin mediates catalytic domain delivery to the cytosol, Proc. Natl. Acad. Sci. U.S.A. 102, 15635-15640.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15635-15640
    • Ratts, R.1    Trujillo, C.2    Bharti, A.3    Vanderspek, J.4    Harrison, R.5    Murphy, J.R.6
  • 26
    • 0345668477 scopus 로고    scopus 로고
    • The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex
    • Ratts, R., Zeng, H., Berg, E. A., Blue, C., McComb, M. E., Costello, C. E., vanderSpek, J. C., and Murphy, J. R. (2003) The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex, J. Cell Biol. 160, 1139-1150.
    • (2003) J. Cell Biol. , vol.160 , pp. 1139-1150
    • Ratts, R.1    Zeng, H.2    Berg, E.A.3    Blue, C.4    McComb, M.E.5    Costello, C.E.6    Vanderspek, J.C.7    Murphy, J.R.8
  • 27
    • 0033579873 scopus 로고    scopus 로고
    • Membrane translocation of charged residues at the tips of hydrophobic helices in the T domain of diphtheria toxin
    • Ren, J., Sharpe, J. C., Collier, R. J., and London, E. (1999) Membrane translocation of charged residues at the tips of hydrophobic helices in the T domain of diphtheria toxin, Biochemistry 38, 976-984.
    • (1999) Biochemistry , vol.38 , pp. 976-984
    • Ren, J.1    Sharpe, J.C.2    Collier, R.J.3    London, E.4
  • 28
    • 0032558976 scopus 로고    scopus 로고
    • Membrane topography of the T domain of diphtheria toxin probed with single tryptophan mutants
    • Malenbaum, S. E., Collier, R. J., and London, E. (1998) Membrane topography of the T domain of diphtheria toxin probed with single tryptophan mutants, Biochemistry 37, 17915-17922.
    • (1998) Biochemistry , vol.37 , pp. 17915-17922
    • Malenbaum, S.E.1    Collier, R.J.2    London, E.3
  • 29
    • 0030886648 scopus 로고    scopus 로고
    • Probing the structure of the diphtheria toxin channel. Reactivity in planar lipid bilayer membranes of cysteine-substituted mutant channels with methanethiosulfonate derivatives
    • Huynh, P. D., Cui, C., Zhan, H., Oh, K. J., Collier, R. J., and Finkelstein, A. (1997) Probing the structure of the diphtheria toxin channel. Reactivity in planar lipid bilayer membranes of cysteine-substituted mutant channels with methanethiosulfonate derivatives, J. Gen. Physiol. 110, 229-242.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 229-242
    • Huynh, P.D.1    Cui, C.2    Zhan, H.3    Oh, K.J.4    Collier, R.J.5    Finkelstein, A.6
  • 32
    • 0028297567 scopus 로고
    • Structure-function relationships in diphtheria toxin channels: III. Residues which affect the cis pH dependence of channel conductance
    • Mindell, J. A., Silverman, J. A., Collier, R. J., and Finkelstein, A. (1994) Structure-function relationships in diphtheria toxin channels: III. Residues which affect the cis pH dependence of channel conductance, J. Membr. Biol. 137, 45-57.
    • (1994) J. Membr. Biol. , vol.137 , pp. 45-57
    • Mindell, J.A.1    Silverman, J.A.2    Collier, R.J.3    Finkelstein, A.4
  • 33
    • 0028269946 scopus 로고
    • Structure-function relationships in diphtheria toxin channels: I. Determining a minimal channel-forming domain
    • Silverman, J. A., Mindell, J. A., Zhan, H., Finkelstein, A., and Collier, R. J. (1994) Structure-function relationships in diphtheria toxin channels: I. Determining a minimal channel-forming domain, J. Membr. Biol. 137, 17-28.
    • (1994) J. Membr. Biol. , vol.137 , pp. 17-28
    • Silverman, J.A.1    Mindell, J.A.2    Zhan, H.3    Finkelstein, A.4    Collier, R.J.5
  • 34
    • 15544385169 scopus 로고    scopus 로고
    • Behavior of diphtheria toxin T domain containing substitutions that block normal membrane insertion at Pro345 and Leu307: Control of deep membrane insertion and coupling between deep insertion of hydrophobic subdomains
    • Zhao, G., and London, E. (2005) Behavior of diphtheria toxin T domain containing substitutions that block normal membrane insertion at Pro345 and Leu307: Control of deep membrane insertion and coupling between deep insertion of hydrophobic subdomains, Biochemistry 44, 4488-4498.
    • (2005) Biochemistry , vol.44 , pp. 4488-4498
    • Zhao, G.1    London, E.2
  • 35
    • 0033735495 scopus 로고    scopus 로고
    • The diphtheria toxin channel-forming T-domain translocates its own NH-terminal region and the catalytic domain across planar phospholipid bilayers
    • Finkelstein, A., Oh, K. J., Senzel, L., Gordon, M., Blaustein, R. O., and Collier, R. J. (2000) The diphtheria toxin channel-forming T-domain translocates its own NH-terminal region and the catalytic domain across planar phospholipid bilayers, Int. J. Med. Microbiol. 290, 435-440.
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 435-440
    • Finkelstein, A.1    Oh, K.J.2    Senzel, L.3    Gordon, M.4    Blaustein, R.O.5    Collier, R.J.6
  • 36
    • 0029152161 scopus 로고
    • Cell-mediated reduction and incomplete membrane translocation of diphtheria toxin mutants with internal disulfides in the A fragment
    • Falnes, P. O., and Olsnes, S. (1995) Cell-mediated reduction and incomplete membrane translocation of diphtheria toxin mutants with internal disulfides in the A fragment, J. Biol. Chem. 270, 20787-20793.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20787-20793
    • Falnes, P.O.1    Olsnes, S.2
  • 37
    • 0027241029 scopus 로고
    • Structure/function analysis of the transmembrane domain of DAB389-interleukin-2, an interleukin-2 receptor-targeted fusion toxin. The amphipathic helical region of the transmembrane domain is essential for the efficient delivery of the catalytic domain to the cytosol of target cells
    • vanderSpek, J. C., Mindell, J. A., Finkelstein, A., and Murphy, J. R. (1993) Structure/function analysis of the transmembrane domain of DAB389-interleukin-2, an interleukin-2 receptor-targeted fusion toxin. The amphipathic helical region of the transmembrane domain is essential for the efficient delivery of the catalytic domain to the cytosol of target cells, J. Biol. Chem. 268, 12077-12082.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12077-12082
    • VanderSpek, J.C.1    Mindell, J.A.2    Finkelstein, A.3    Murphy, J.R.4
  • 38
    • 0028025127 scopus 로고
    • Maintenance of the hydrophobic face of the diphtheria toxin amphipathic transmembrane helix 1 is essential for the efficient delivery of the catalytic domain to the cytosol of target cells
    • vanderSpek, J. C., Howland, K., Friedman, T., and Murphy, J. R. (1994) Maintenance of the hydrophobic face of the diphtheria toxin amphipathic transmembrane helix 1 is essential for the efficient delivery of the catalytic domain to the cytosol of target cells, Protein Eng. 7, 985-989.
    • (1994) Protein Eng. , vol.7 , pp. 985-989
    • VanderSpek, J.C.1    Howland, K.2    Friedman, T.3    Murphy, J.R.4
  • 39
    • 0028180162 scopus 로고
    • The N-terminal α-helix of fragment B of diphtheria toxin promotes translocation of fragment A into the cytoplasm of eukaryotic cells
    • Madshus, I. H. (1994) The N-terminal α-helix of fragment B of diphtheria toxin promotes translocation of fragment A into the cytoplasm of eukaryotic cells, J. Biol. Chem. 269, 17723-17729.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17723-17729
    • Madshus, I.H.1
  • 40
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 41
    • 0028144832 scopus 로고
    • Dynamic transitions of the transmembrane domain of diphtheria toxin: Disulfide trapping and fluorescence proximity studies
    • Zhan, H., Choe, S., Huynh, P. D., Finkelstein, A., Eisenberg, D., and Collier, R. J. (1994) Dynamic transitions of the transmembrane domain of diphtheria toxin: Disulfide trapping and fluorescence proximity studies, Biochemistry 33, 11254-11263.
    • (1994) Biochemistry , vol.33 , pp. 11254-11263
    • Zhan, H.1    Choe, S.2    Huynh, P.D.3    Finkelstein, A.4    Eisenberg, D.5    Collier, R.J.6
  • 42
    • 0028983351 scopus 로고
    • Imaging of endosome fusion in BHK fibroblasts based on a novel fluorimetric avidin-biotin binding assay
    • Emans, N., Biwersi, J., and Verkman, A. S. (1995) Imaging of endosome fusion in BHK fibroblasts based on a novel fluorimetric avidin-biotin binding assay, Biophys. J. 69, 716-728.
    • (1995) Biophys. J. , vol.69 , pp. 716-728
    • Emans, N.1    Biwersi, J.2    Verkman, A.S.3
  • 43
    • 0033058273 scopus 로고    scopus 로고
    • Orientation of the pore-forming peptide GALA in POPC vesicles determined by a BODIPY-avidin/biotin binding assay
    • Nicol, F., Nir, S., and Szoka, F. C., Jr. (1999) Orientation of the pore-forming peptide GALA in POPC vesicles determined by a BODIPY-avidin/biotin binding assay, Biophys. J. 76, 2121-2141.
    • (1999) Biophys. J. , vol.76 , pp. 2121-2141
    • Nicol, F.1    Nir, S.2    Szoka Jr., F.C.3
  • 44
    • 0032903686 scopus 로고    scopus 로고
    • Surface aggregation and membrane penetration by peptides: Relation to pore formation and fusion
    • Nir, S., Nicol, F., and Szoka, F. C., Jr. (1999) Surface aggregation and membrane penetration by peptides: Relation to pore formation and fusion, Mol. Membr. Biol. 16, 95-101.
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 95-101
    • Nir, S.1    Nicol, F.2    Szoka Jr., F.C.3
  • 45
    • 0037044842 scopus 로고    scopus 로고
    • Membrane protein insertion regulated by bringing electrostatic and hydrophobic interactions into play. A case study with the translocation domain of diphtheria toxin
    • Chenal, A., Savarin, P., Nizard, P., Guillain, F., Gillet, D., and Forge, V. (2002) Membrane protein insertion regulated by bringing electrostatic and hydrophobic interactions into play. A case study with the translocation domain of diphtheria toxin, J. Biol. Chem. 277, 43425-43432.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43425-43432
    • Chenal, A.1    Savarin, P.2    Nizard, P.3    Guillain, F.4    Gillet, D.5    Forge, V.6
  • 47
    • 33644854069 scopus 로고    scopus 로고
    • Scanning the membrane-bound conformation of helix 1 in the colicin E1 channel domain by site-directed fluorescence labeling
    • Musse, A. A., Wang, J., Deleon, G. P., Prentice, G. A., London, E., and Merrill, A. R. (2006) Scanning the membrane-bound conformation of helix 1 in the colicin E1 channel domain by site-directed fluorescence labeling, J. Biol. Chem. 281, 885-895.
    • (2006) J. Biol. Chem. , vol.281 , pp. 885-895
    • Musse, A.A.1    Wang, J.2    Deleon, G.P.3    Prentice, G.A.4    London, E.5    Merrill, A.R.6
  • 48
    • 0041589302 scopus 로고    scopus 로고
    • The molecular basis for the pH-activation mechanism in the channel-forming bacterial colicin E1
    • Musse, A. A., and Merrill, A. R. (2003) The molecular basis for the pH-activation mechanism in the channel-forming bacterial colicin E1, J. Biol. Chem. 278, 24491-24499.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24491-24499
    • Musse, A.A.1    Merrill, A.R.2
  • 50
    • 0037176909 scopus 로고    scopus 로고
    • Mapping proximity within proteins using fluorescence spectroscopy. A study of T4 lysozyme showing that tryptophan residues quench bimane fluorescence
    • Mansoor, S. E., McHaourab, H. S., and Farrens, D. L. (2002) Mapping proximity within proteins using fluorescence spectroscopy. A study of T4 lysozyme showing that tryptophan residues quench bimane fluorescence, Biochemistry 41, 2475-2484.
    • (2002) Biochemistry , vol.41 , pp. 2475-2484
    • Mansoor, S.E.1    McHaourab, H.S.2    Farrens, D.L.3
  • 51
    • 0026803128 scopus 로고
    • Interactions of diphtheria toxin B-fragment with cells. Role of amino- and carboxyl-terminal regions
    • Stenmark, H., Ariansen, S., Afanasiev, B. N., and Olsnes, S. (1992) Interactions of diphtheria toxin B-fragment with cells. Role of amino- and carboxyl-terminal regions, J. Biol. Chem. 267, 8957-8962.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8957-8962
    • Stenmark, H.1    Ariansen, S.2    Afanasiev, B.N.3    Olsnes, S.4


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