Barrick, D. and Baldwin, R.L. 1993. Three-state analysis of sperm whale apomyoglobin folding. Biochemistry 32: 3790-3796.
Basova, L.V., Tiktopulo, E.I., Kashparov, I.A., and Bychkova, V.E. 2004. Conformational state of apomyoglobin in the presence of phospholipid vesicles at neutral pH. Mol. Biol. (Mosk.) 38: 323-332.
Bennett, M.J., Choe, S., and Eisenberg, D. 1994. Refined structure of dimeric diphtheria toxin at 2.0 Å resolution. Protein Sci. 3: 1444-1463.
Bernad, S., Oellerich, S., Soulimane, T., Noinville, S., Baron, M.H., Paternostre, M., and Lecomte, S. 2004. Interaction of horse heart and thermus thermophilus type c cytochromes with phospholipid vesicles and hydrophobic surfaces. Biophys. J. 86: 3863-3872.
Bigay, J., Gounon, P., Robineau, S., and Antonny, B. 2003. Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Nature 426: 563-566.
Cannon, J.B., Kuo, F.S., Pasternack, R.F., Wong, N.M., and Muller-Eberhard, U. 1984. Kinetics of the interaction of hemin liposomes with heme binding proteins. Biochemistry 16: 3715-3721.
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.
Chenal, A., Vernier, G., Savarin, P., Bushmarina, N.A., Geze, A., Guillain, F., Gillet, D., and Forge, V. 2005. Conformational states and thermodynamics of α-lactalbumin bound to membranes: A case study of the effects of pH, calcium, lipid membrane curvature and charge. J. Mol. Biol. 349: 890-905.
Choe, S., Bennett, M.J., Fujii, G., Curmi, P.M., Kantardjieff, K.A., Collier, R.J., and Eisenberg, D. 1992. The crystal structure of diphtheria toxin. Nature 357: 216-222.
Eliezer, D. and Wright, P.E. 1996. Is apomyoglobin a molten globule? Structural characterization by NMR. J. Mol. Biol. 263: 531-538.
Eliezer, D., Yao, J., Dyson, H.J., and Wright, P.E. 1998. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat. Struct. Biol. 5: 148-155.
Eliezer, D., Chung, J., Dyson, H.J., and Wright, P.E. 2000. Native and nonnative secondary structure and dynamics in the pH 4 intermediate of apomyoglobin. Biochemistry 39: 2894-2901.
Falnes, P.O., Madshus, I.H., Sandvig, K., and Olsnes, S. 1992. Replacement of negative by positive charges in the presumed membrane-inserted part of diphtheria toxin B fragment. Effect on membrane translocation and on formation of cation channels. J. Biol. Chem. 267: 12284-12290.
Fesik, S.W. 2000. Insights into programmed cell death through structural biology. Cell 103: 273-282.
Griko, Y.V., Privalov, P.L., Venyaminov, S.Y., and Kutyshenko, V.P. 1988. Thermodynamic study of the apomyoglobin structure. J. Mol. Biol. 202: 127-138.
Gulotta, M., Rogatsky, E., Callender, R.H., and Dyer, R.B. 2003. Primary folding dynamics of sperm whale apomyoglobin: Core formation. Biophys. J. 84: 1909-1918.
Heerklotz, H. and Epand, R.M. 2001. The enthalpy of acyl chain packing and the apparent water-accessible apolar surface area of phospholipids. Biophys. J. 80: 271-279.
Holm, L. and Sander, C. 1993a. Globin fold in a bacterial toxin. Nature 361: 309.
Holm, L. and Sander, C. 1993b. Structural alignment of globins, phycocyanins and colicin A. FEBS Lett. 315: 301-306.
Hughson, F.M., Wright, P.E., and Baldwin, R.L. 1990. Structural characterization of a partly folded apomyoglobin intermediate. Science 249: 1544-1548.
Jakoby, W.B. 1978. The glutathione S-transferases: A group of multifunctional detoxification proteins. Adv. Enzymol. Relat. Areas Mol. Biol. 46: 383-414.
Jamin, M. 2005. The folding process of apomyoglobin. Protein Pept. Lett. 3: 229-234.
Jamin, M. and Baldwin, R.L. 1998. Two forms of the pH 4 folding intermediate of apomyoglobin. J. Mol. Biol. 276: 491-504.
Johnson, J.E. and Cornell, R.B. 1999. Amphitropic proteins: Regulation by reversible membrane interactions. Mol. Membr. Biol. 16: 217-235.
Kataoka, M., Nishii, I., Fujisawa, T., Ueki, T., Tokunaga, F., and Goto, Y. 1995. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249: 215-228.
Kay, M.S. and Baldwin, R.L. 1998. Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate. Biochemistry 37: 7859-7868.
Kirby, E.P. and Steiner, R.F. 1970. The tryptophan microenvironments in apomyoglobin. J. Biol. Chem. 245: 6300-6306.
Lee, J.W. and Kim, H. 1992. Fragmentation of dimyristoylphosphatidylcholine vesicles by apomyoglobin. Arch. Biochem. Biophys. 297: 354-361.
Leenhouts, J.M., van den Wijngaard, P.W., de Kroon, A.I., and de Kruijff, B. 1995. Anionic phospholipids can mediate membrane insertion of the anionic part of a bound peptide. FEBS Lett. 370: 189-192.
Lepore, L.S., Ellena, J.F., and Cafiso, D.S. 1992. Comparison of the lipid acyl chain dynamics between small and large unilamellar vesicles. Biophys. J. 61: 767-775.
Light 3rd, W.R. and Olson, J.S. 1990. Transmembrane movement of heme. J. Biol. Chem. 265: 15623-15631.
Liu, L.P. and Deber, C.M. 1997. Anionic phospholipids modulate peptide insertion into membranes. Biochemistry 36: 5476-5482.
Loh, S.N., Kay, M.S., and Baldwin, R.L. 1995. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Natl. Acad. Sci. 92: 5446-5450.
Parker, M.W. and Feil, S.C. 2005. Pore-forming protein toxins: From structure to function. Prog. Biophys. Mol. Biol. 88: 91-142.
Parker, M.W., Pattus, F., Tucker, A.D., and Tsernoglou, D. 1989. Structure of the membrane-pore-forming fragment of colicin A. Nature 337: 93-96.
Postnikova, G.B., Komarov, Y.E., and Yumakova, E.M. 1991. Fluorescence study of the conformational properties of myoglobin structure. 1. pH-dependent changes of tryptophanyl fluorescence in intact and chemically modified sperm whale apomyoglobins. Eur. J. Biochem. 198: 223-232.
Rose, M.Y. and Olson, J.S. 1983. The kinetic mechanism of heme binding to human apohemoglobin. J. Biol. Chem. 258: 4298-4303.
Rose, M.Y., Thompson, R.A., Light, W.R., and Olson, J.S. 1985. Heme transfer between phospholipid membranes and uptake by apohemoglobin. J. Biol. Chem. 260: 6632-6640.
Szebeni, J., Di Iorio, E.E., Hauser, H., and Winterhalter, K.H. 1985. Encapsulation of hemoglobin in phospholipid liposomes: Characterization and stability. Biochemistry 24: 2827-2832.
Szebeni, J., Hauser, H., Eskelson, C.D., Watson, R.R., and Winterhalter, K.H. 1988. Interaction of hemoglobin derivatives with liposomes. Membrane cholesterol protects against the changes of hemoglobin. Biochemistry 27: 6425-6434.
van den Berg, B., Wain, R., Dobson, C.M., and Ellis, R.J. 2000. Macromolecular crowding perturbs protein refolding kinetics: Implications for folding inside the cell. EMBO J. 19: 3870-3878.
van der Goot, F.G., Gonzalez-Manas, J.M., Lakey, J.H., and Pattus, F. 1991. A "molten-globule" membrane-insertion intermediate of the pore-forming domain of colicin A. Nature 354: 408-410.
Weisbuch, S., Gerard, F., Pasdeloup, M., Cappadoro, J., Dupont, Y., and Jamin, M. 2005. Cooperative sub-millisecond folding kinetics of apomyoglobin pH 4 intermediate. Biochemistry 44: 7013-7023.
Wittenberg, J.B. and Wittenberg, B.A. 2003. Myoglobin function reassessed. J. Exp. Biol. 206: 2011-2020.
Yoshida, Y., Kinuta, M., Abe, T., Liang, S., Araki, K., and Cremona, O. 2004. The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature. EMBO J. 23: 3483-3491.
Zakharov, S.D., Lindeberg, M., Griko, Y., Salamon, Z., Tollin, G., Prendergast, F.G., and Cramer, W.A. 1998. Membrane-bound state of the colicin E1 channel domain as an extended two-dimensional helical array. Proc. Natl. Acad. Sci. 95: 4282-4287.
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.
Zhan, H., Oh, K.J., Shin, Y.K., Hubbell, W.L., and Collier, R.J. 1995. Interaction of the isolated transmembrane domain of diphtheria toxin with membranes. Biochemistry 34: 4856-4863.