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Volumn 43, Issue 19, 2004, Pages 5575-5582

No Need to Be HAMLET or BAMLET to Interact with Histones: Binding of Monomeric α-Lactalbumin to Histones and Basic Poly-Amino Acids

Author keywords

[No Author keywords available]

Indexed keywords

AGENTS; AGGLOMERATION; AMINO ACIDS; CELLS; ELECTROSTATICS; MONOMERS; PROTEINS; STOICHIOMETRY; TUMORS;

EID: 2442575245     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049584y     Document Type: Article
Times cited : (44)

References (48)
  • 1
    • 0034685838 scopus 로고    scopus 로고
    • α-lactalbumin: Structure and function
    • Permyakov, E. A., and Berliner, L. J. (2000) α-Lactalbumin: structure and function, FEBS Lett. 473, 269-274.
    • (2000) FEBS Lett. , vol.473 , pp. 269-274
    • Permyakov, E.A.1    Berliner, L.J.2
  • 4
    • 0021095471 scopus 로고
    • A distinct zinc-binding site in the α-lactalbumins regulates calcium-binding: Is there a physiological role for this control
    • Murakami, K., and Berliner, L. J. (1983) A distinct zinc-binding site in the α-lactalbumins regulates calcium-binding: Is there a physiological role for this control, Biochemistry 22, 3370-3374.
    • (1983) Biochemistry , vol.22 , pp. 3370-3374
    • Murakami, K.1    Berliner, L.J.2
  • 8
    • 0033022708 scopus 로고    scopus 로고
    • Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule
    • Pellegrini, A., Thomas, U., Bramaz, N., Hunziker, P., and von Fellenberg, R. (1999) Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule, Biochim. Biophys. Acta 1426, 439-448.
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 439-448
    • Pellegrini, A.1    Thomas, U.2    Bramaz, N.3    Hunziker, P.4    Von Fellenberg, R.5
  • 11
    • 0037584357 scopus 로고    scopus 로고
    • Multimeric α-lactalbumin from human milk induces apoptosis through a direct effect on cell nuclei
    • Hakansson, A., Andreasson, J., Zhivotovsky, B., Karpman, D., Orrenius, S., and Svanborg, C. (1999) Multimeric α-lactalbumin from human milk induces apoptosis through a direct effect on cell nuclei, Exp. Cell Res. 246, 451-460.
    • (1999) Exp. Cell Res. , vol.246 , pp. 451-460
    • Hakansson, A.1    Andreasson, J.2    Zhivotovsky, B.3    Karpman, D.4    Orrenius, S.5    Svanborg, C.6
  • 13
    • 10744223979 scopus 로고    scopus 로고
    • α-lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human α-lactalbumin made lethal to tumor cells)
    • Svensson, M., Fast, J., Mossberg, A. K., Duringer, C., Gustafsson, L., Hallgren, O., Brooks, C. L., Berliner, L., Linse, S., and Svanborg, C. (2003) α-Lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human α-lactalbumin made lethal to tumor cells), Protein Sci. 12, 2794-2804.
    • (2003) Protein Sci. , vol.12 , pp. 2794-2804
    • Svensson, M.1    Fast, J.2    Mossberg, A.K.3    Duringer, C.4    Gustafsson, L.5    Hallgren, O.6    Brooks, C.L.7    Berliner, L.8    Linse, S.9    Svanborg, C.10
  • 14
    • 0142242197 scopus 로고    scopus 로고
    • HAMLET interacts with histories and chromatin in tumor cell nuclei
    • Duringer, C., Hamiche, A., Gustafsson, L., Kimura, H., and Svanborg, C. (2003) HAMLET interacts with histories and chromatin in tumor cell nuclei, J. Biol. Chem. 278, 42131-42135.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42131-42135
    • Duringer, C.1    Hamiche, A.2    Gustafsson, L.3    Kimura, H.4    Svanborg, C.5
  • 15
    • 0037110569 scopus 로고    scopus 로고
    • Molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: A comparative analysis by circular dichroism spectroscopy and limited proteolysis
    • de Laureto, P. P., Frare, E., Gottardo, R., and Fontana, A. (2002) Molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: A comparative analysis by circular dichroism spectroscopy and limited proteolysis, Proteins: Struct., Funct., Genet. 49, 385-397.
    • (2002) Proteins: Struct., Funct., Genet. , vol.49 , pp. 385-397
    • De Laureto, P.P.1    Frare, E.2    Gottardo, R.3    Fontana, A.4
  • 16
    • 0016746053 scopus 로고
    • Isolation and purification of α-lactalbumin, a component of lactose synthetase
    • Kaplanas, R. I., and Antanavichyus, A. I. (1975) Isolation and purification of α-lactalbumin, a component of lactose synthetase, Biochemistry (Moscow) 40, 493-495.
    • (1975) Biochemistry (Moscow) , vol.40 , pp. 493-495
    • Kaplanas, R.I.1    Antanavichyus, A.I.2
  • 17
    • 0001501417 scopus 로고
    • Inter-and intramolecular interactions of α-lactalbumin. II. Aggregation reactions at acid pH
    • Kronman, M. S., Andreotti, R. E., and Vitols, R. (1964) Inter-and intramolecular interactions of α-lactalbumin. II. Aggregation reactions at acid pH, Biochemistry 3, 1152-1160.
    • (1964) Biochemistry , vol.3 , pp. 1152-1160
    • Kronman, M.S.1    Andreotti, R.E.2    Vitols, R.3
  • 18
    • 0015500799 scopus 로고
    • Two chemically and metabolically distinct forms of calf thymus histone F3
    • Marzluff, W. F., Jr., Sanders, L. A., Miller, D. M., and McCarty, K. S. (1972) Two chemically and metabolically distinct forms of calf thymus histone F3, J. Biol. Chem. 247, 2026-2033.
    • (1972) J. Biol. Chem. , vol.247 , pp. 2026-2033
    • Marzluff Jr., W.F.1    Sanders, L.A.2    Miller, D.M.3    McCarty, K.S.4
  • 19
    • 0016662144 scopus 로고
    • Histone III. VI. Two forms of calf thymus histone III
    • Patthy, L., and Smith, E. L. (1975) Histone III. VI. Two forms of calf thymus histone III, J. Biol. Chem. 250, 1919-1920.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1919-1920
    • Patthy, L.1    Smith, E.L.2
  • 20
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 21
    • 0017622799 scopus 로고
    • Luminescence of phenylalanine residues in duperoxide-dismutase from green pea
    • Permyakov, E. A., Burstein, E. A., Sawada, Y., and Yamazaki, I. (1977) Luminescence of phenylalanine residues in duperoxide-dismutase from green pea, Biochim. Biophys. Acta 491, 149-154.
    • (1977) Biochim. Biophys. Acta , vol.491 , pp. 149-154
    • Permyakov, E.A.1    Burstein, E.A.2    Sawada, Y.3    Yamazaki, I.4
  • 22
    • 0029850169 scopus 로고    scopus 로고
    • Log-normal description of fluorescence spectra of organic fluorophores
    • Burstein, E. A., and Emelyanenko, V. I. (1996) Log-normal description of fluorescence spectra of organic fluorophores, Photochem. Photobiol. 64, 316-320.
    • (1996) Photochem. Photobiol. , vol.64 , pp. 316-320
    • Burstein, E.A.1    Emelyanenko, V.I.2
  • 23
    • 0000169232 scopus 로고
    • An algorithm for least squares estimation of nonlinear parameters
    • Marquardt, D. W. (1963) An algorithm for least squares estimation of nonlinear parameters, J. Soc. Ind. Appl. Math. 11, 431-441.
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 24
    • 0021435096 scopus 로고
    • Some aspects of studies of thermal transitions in proteins by means of their intrinsic fluorescence
    • Permyakov, E. A., and Burstein, E. A. (1984) Some aspects of studies of thermal transitions in proteins by means of their intrinsic fluorescence, Biophys. Chem. 19, 265-271.
    • (1984) Biophys. Chem. , vol.19 , pp. 265-271
    • Permyakov, E.A.1    Burstein, E.A.2
  • 26
    • 0019880942 scopus 로고
    • Calcium-binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes
    • Permyakov, E. A., Yarmolenko, V. V., Kalinichenko, L. P., Morozova, L. A., and Burstein, E. A. (1981) Calcium-binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes, Biochem. Biophys. Res. Commun. 100, 191-197.
    • (1981) Biochem. Biophys. Res. Commun. , vol.100 , pp. 191-197
    • Permyakov, E.A.1    Yarmolenko, V.V.2    Kalinichenko, L.P.3    Morozova, L.A.4    Burstein, E.A.5
  • 27
    • 0036712109 scopus 로고    scopus 로고
    • Photoexcitation of tryptophan groups induces reduction of two disulfide bonds in goat α-lactalbumin
    • Vanhooren, A., Devreese, B., Vanhee, K., Van Beeumen, J., and Hanssens, I. (2002) Photoexcitation of tryptophan groups induces reduction of two disulfide bonds in goat α-lactalbumin, Biochemistry 41, 11035-11043.
    • (2002) Biochemistry , vol.41 , pp. 11035-11043
    • Vanhooren, A.1    Devreese, B.2    Vanhee, K.3    Van Beeumen, J.4    Hanssens, I.5
  • 30
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky, V. N., Gillespie, J. R., and Fink, A. L. (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41, 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 31
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002) Natively unfolded proteins: a point where biology waits for physics, Protein Sci. 11, 739-756.
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 32
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded?
    • Uversky, V. N. (2002) What does it mean to be natively unfolded? Eur. J. Biochem. 269, 2-12.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 33
    • 4444311182 scopus 로고    scopus 로고
    • Formation of amyloid fibrils from the core histones in vitro
    • in press
    • Munishkina, L. A., Fink, A. L., and Uversky, V. N. (2004) Formation of amyloid fibrils from the core histones in vitro, J. Mol. Biol. (in press).
    • (2004) J. Mol. Biol.
    • Munishkina, L.A.1    Fink, A.L.2    Uversky, V.N.3
  • 35
    • 0014810985 scopus 로고
    • An investigation of the conformational changes in histones F1 and F2a1 by proton magnetic resonance spectroscopy
    • Boublik, M., Bradbury, E. M., and Crane-Robinson, C. (1970) An investigation of the conformational changes in histones F1 and F2a1 by proton magnetic resonance spectroscopy, Eur. J. Biochem. 14, 486-497.
    • (1970) Eur. J. Biochem. , vol.14 , pp. 486-497
    • Boublik, M.1    Bradbury, E.M.2    Crane-Robinson, C.3
  • 37
    • 0015385029 scopus 로고
    • Salt effects on histone IV conformation
    • Wickett, R. R., Li, H. J., and Isenberg, I. (1972) Salt effects on histone IV conformation, Biochemistry 11, 2952-2957.
    • (1972) Biochemistry , vol.11 , pp. 2952-2957
    • Wickett, R.R.1    Li, H.J.2    Isenberg, I.3
  • 39
    • 11344291497 scopus 로고
    • The ultraviolet circular dichroism of polypeptides
    • Holzwarth, G., and Doty, P. (1965) The ultraviolet circular dichroism of polypeptides, J. Am. Chem. Soc. 87, 218-228.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 218-228
    • Holzwarth, G.1    Doty, P.2
  • 40
    • 0014023633 scopus 로고
    • Calorimetric heat of the helix-coil transition of poly-L-glutamic acid
    • Rialdi, G., and Hermans, J., Jr. (1966) Calorimetric heat of the helix-coil transition of poly-L-glutamic acid, J. Am. Chem. Soc. 88, 5719-5720.
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 5719-5720
    • Rialdi, G.1    Hermans Jr., J.2
  • 41
    • 0014227144 scopus 로고
    • New chain conformations of poly(glutamic acid) and polylysine
    • Tiffany, M. L., and Krimm, S. (1968) New chain conformations of poly(glutamic acid) and polylysine, Biopolymers 6, 1379-1382.
    • (1968) Biopolymers , vol.6 , pp. 1379-1382
    • Tiffany, M.L.1    Krimm, S.2
  • 43
    • 0033053602 scopus 로고    scopus 로고
    • Energetics of solvent and ligand-induced conformational changes in α-lactalbumin
    • Griko, Y. V., and Remeta, D. P. (1999) Energetics of solvent and ligand-induced conformational changes in α-lactalbumin, Protein Sci. 8, 554-561.
    • (1999) Protein Sci. , vol.8 , pp. 554-561
    • Griko, Y.V.1    Remeta, D.P.2
  • 44
    • 0027136749 scopus 로고
    • Complexes of the polyamines spermine, spermidine and putrescine with α-lactalbumins
    • Morozova, L., Desmet, J., and Joniau, M. (1993) Complexes of the polyamines spermine, spermidine and putrescine with α-lactalbumins, Eur. J. Biochem. 218, 303-309.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 303-309
    • Morozova, L.1    Desmet, J.2    Joniau, M.3
  • 45
    • 0035701464 scopus 로고    scopus 로고
    • Growth rates of a human colon adenocarcinoma cell line are regulated by the milk protein α-lactalbumin
    • Sternhagen, L. G., and Allen, J. C. (2001) Growth rates of a human colon adenocarcinoma cell line are regulated by the milk protein α-lactalbumin, Adv. Exp. Med. Biol. 501, 115-120.
    • (2001) Adv. Exp. Med. Biol. , vol.501 , pp. 115-120
    • Sternhagen, L.G.1    Allen, J.C.2
  • 47
    • 0030014802 scopus 로고    scopus 로고
    • Membrane-bound states of α-lactalbumin: Implications for the protein stability and conformation
    • Cawthern, K. M., Permyakov, E., and Berliner, L. J. (1996) Membrane-bound states of α-lactalbumin: implications for the protein stability and conformation, Protein Sci. 5, 1394-1405.
    • (1996) Protein Sci. , vol.5 , pp. 1394-1405
    • Cawthern, K.M.1    Permyakov, E.2    Berliner, L.J.3
  • 48
    • 0018599424 scopus 로고
    • Interaction between DMPC vesicles and the peripheral protein α-lactalbumin
    • Hanssens, L, Houthuys, C., and Cauwelaert, F. H. (1979) Interaction between DMPC vesicles and the peripheral protein α-lactalbumin, Arch. Int. Physiol. Biochim. 87, 1017-1018.
    • (1979) Arch. Int. Physiol. Biochim. , vol.87 , pp. 1017-1018
    • Hanssens, L.1    Houthuys, C.2    Cauwelaert, F.H.3


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