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Volumn 41, Issue 3, 2009, Pages 162-176

Can misfolded proteins be beneficial? the HAMLET case

Author keywords

Amyloid; Cancer; Cell death; HAMLET complex; Lactalbumin; Oleic acid; Prions; Protein folding

Indexed keywords

ALPHA LACTALBUMIN; AMYLOID; AMYLOID BETA PROTEIN; AMYLOID PROTEIN; CELL NUCLEUS RECEPTOR; HUMAN ALBUMIN; LACTOSE; LIPID; OLEIC ACID; PLACEBO; POLYPEPTIDE; PRION PROTEIN; PROTEASOME; PROTEIN HAMLET; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; ANTINEOPLASTIC AGENT; CALCIUM; HAMLET COMPLEX, HUMAN; LACTALBUMIN;

EID: 67650379261     PISSN: 07853890     EISSN: 13652060     Source Type: Journal    
DOI: 10.1080/07853890802502614     Document Type: Review
Times cited : (36)

References (106)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science. 1973;181:223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 3042617720 scopus 로고    scopus 로고
    • How do proteins avoid becoming too stable? Biophysical studies into metastable proteins
    • Cabrita LD, Bottomley SP. How do proteins avoid becoming too stable? Biophysical studies into metastable proteins. Eur Biophys J. 2004;33:83-88.
    • (2004) Eur Biophys J , vol.33 , pp. 83-88
    • Cabrita, L.D.1    Bottomley, S.P.2
  • 6
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • Shorter J, Lindquist S. Prions as adaptive conduits of memory and inheritance. Nat Rev Genet. 2005;6:435-450.
    • (2005) Nat Rev Genet , vol.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 7
    • 0001194208 scopus 로고
    • Genetic control of biochemical reactions in neurospora
    • Beadle GW, Tatum EL. Genetic control of biochemical reactions in neurospora. Proc Natl Acad Sci USA. 1941; 27:499-506.
    • (1941) Proc Natl Acad Sci USA , vol.27 , pp. 499-506
    • Beadle, G.W.1    Tatum, E.L.2
  • 8
    • 0035002013 scopus 로고    scopus 로고
    • The human genome sequence expedition: Views from the base camp?
    • Green ED, Chakravarti A. The human genome sequence expedition: views from the base camp?. Genome Res. 2001;11:645-651.
    • (2001) Genome Res , vol.11 , pp. 645-651
    • Green, E.D.1    Chakravarti, A.2
  • 10
    • 7244245762 scopus 로고    scopus 로고
    • Finishing the euchromatic sequence of the human genome
    • nternational Human Genome Sequencing Consortium
    • International Human Genome Sequencing Consortium. Finishing the euchromatic sequence of the human genome. Nature. 2004;431:931-935.
    • (2004) Nature , vol.431 , pp. 931-935
  • 11
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson CM. Protein misfolding, evolution and disease. Trends Biochem Sci. 1999;24:329-332.
    • (1999) Trends Biochem Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 12
    • 0035895513 scopus 로고    scopus 로고
    • Gene number What if there are only 30,000 human genes?
    • Claverie JM. Gene number. What if there are only 30,000 human genes? Science. 2001;291:1255-1257.
    • (2001) Science , vol.291 , pp. 1255-1257
    • Claverie, J.M.1
  • 15
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • Jeffery CJ. Moonlighting proteins. Trends Biochem Sci. 1999;24:8-11.
    • (1999) Trends Biochem Sci , vol.24 , pp. 8-11
    • Jeffery, C.J.1
  • 16
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa P, Szasz C, Buday L. Structural disorder throws new light on moonlighting. Trends Biochem Sci. 2005;30:484-489.
    • (2005) Trends Biochem Sci , vol.30 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 17
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl FU, Hayer-Hartl M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science. 2002;295:1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 18
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell. 2006;125:443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 19
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething MJ, Sambrook J. Protein folding in the cell. Nature. 1992;355:33-35pp.
    • (1992) Nature , vol.355 , pp. 33-35
    • Gething, M.J.1    Sambrook, J.2
  • 20
    • 3242875302 scopus 로고    scopus 로고
    • Photo-CIDNP NMR methods for studying protein folding
    • Mok KH, Hore PJ. Photo-CIDNP NMR methods for studying protein folding. Methods. 2004;34:75-87.
    • (2004) Methods , vol.34 , pp. 75-87
    • Mok, K.H.1    Hore, P.J.2
  • 21
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson CM. The structural basis of protein folding and its links with human disease. Philos Trans R Soc Lond B Biol Sci. 2001;356:133-135.
    • (2001) Philos Trans R Soc Lond B Biol Sci , vol.356 , pp. 133-135
    • Dobson, C.M.1
  • 22
    • 0345598912 scopus 로고    scopus 로고
    • Structures and relative free energies of partially folded states of proteins
    • Vendruscolo M, Paci E, Karplus M, Dobson CM. Structures and relative free energies of partially folded states of proteins. Proc Natl Acad Sci USA. 2003;100:14817-14821.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 14817-14821
    • Vendruscolo, M.1    Paci, E.2    Karplus, M.3    Dobson, C.M.4
  • 23
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal C. Are there pathways for protein folding? J Chim Phys. 1968;65:44-45.
    • (1968) J Chim Phys , vol.65 , pp. 44-45
    • Levinthal, C.1
  • 24
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill KA, Chan HS. From Levinthal to pathways to funnels. Nat Struct Biol. 1997;4:10-19.
    • (1997) Nat Struct Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 25
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin RL. The nature of protein folding pathways: the classical versus the new view. JBiomolNMR. 1995;5:103-109.
    • (1995) JBiomolNMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 26
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins. 1995;21:167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 27
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; Protein refolding and therapy
    • Soto C. Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 2001;498:204-207.
    • (2001) FEBS Lett , vol.498 , pp. 204-207
    • Soto, C.1
  • 29
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem. 2006;75:333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 31
    • 0001067847 scopus 로고
    • Beta-amyloid precursor protein of Alzheimer disease occurs as 110- to 135-kilodalton membrane-associated proteins in neural and nonneural tissues
    • Selkoe DJ, Podlisny MB, Joachim CL, Vickers EA, Lee G, Fritz LC, et al. Beta-amyloid precursor protein of Alzheimer disease occurs as 110- to 135-kilodalton membrane-associated proteins in neural and nonneural tissues. Proc Natl Acad Sci USA. 1988;85:7341-7345.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7341-7345
    • Selkoe, D.J.1    Podlisny, M.B.2    Joachim, C.L.3    Vickers, E.A.4    Lee, G.5    Fritz, L.C.6    Al, E.7
  • 32
    • 0028980362 scopus 로고
    • The a-helical to b-strand transition in the amino-terminal fragment of the amyloid -peptide modulates amyloid formation
    • Soto C, Castano EM, Frangione B, Inestrosa NC. The a-helical to b-strand transition in the amino-terminal fragment of the amyloid -peptide modulates amyloid formation. J Biol Chem. 1995;270:3063-3067.
    • (1995) J Biol Chem , vol.270 , pp. 3063-3067
    • Soto, C.1    Castano, E.M.2    Frangione, B.3    Inestrosa, N.C.4
  • 33
    • 0026682931 scopus 로고
    • Solution conformations and aggregational properties of synthetic amyloid b-peptides of Alzheimer's disease. Analysis of circular dichroism spectra
    • Barrow CJ, Yasuda A, Kenny PT, Zagorski MG. Solution conformations and aggregational properties of synthetic amyloid b-peptides of Alzheimer's disease. Analysis of circular dichroism spectra. J Mol Biol. 1992;225:1075-1093.
    • (1992) J Mol Biol , vol.225 , pp. 1075-1093
    • Barrow, C.J.1    Yasuda, A.2    Kenny, P.T.3    Zagorski, M.G.4
  • 34
    • 0026619343 scopus 로고
    • Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides
    • Hilbich C, Kisters-Woike B, Reed J, Masters CL, Beyr-euther K. Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer's disease beta A4 peptides. J Mol Biol. 1992;228:460-473.
    • (1992) J Mol Biol , vol.228 , pp. 460-473
    • Hilbich, C.1    Kisters-Woike, B.2    Reed, J.3    Masters, C.L.4    Beyr-Euther, K.5
  • 35
    • 0031824782 scopus 로고    scopus 로고
    • Aging renders the brain vulnerable to amyloid b-protein neurotoxicity
    • Geula C, Wu CK, Saroff D, Lorenzo A, Yuan M, Yankner BA. Aging renders the brain vulnerable to amyloid b-protein neurotoxicity. Nat Med. 1998;4:827-831.
    • (1998) Nat Med , vol.4 , pp. 827-831
    • Geula, C.1    Wu, C.K.2    Saroff, D.3    Lorenzo, A.4    Yuan, M.5    Yankner, B.A.6
  • 36
    • 0031873102 scopus 로고    scopus 로고
    • Frangione B. b-sheet breaker peptides inhibit fibrillo-genesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy
    • Soto C, Sigurdsson EM, Morelli L, Kumar RA, Castano EM, Frangione B. b-sheet breaker peptides inhibit fibrillo-genesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat Med. 1998;4:822-826.
    • (1998) Nat Med , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5
  • 37
    • 33750310849 scopus 로고    scopus 로고
    • Prions and their partners in crime
    • Caughey B, Baron GS. Prions and their partners in crime. Nature. 2006;443:803-810.
    • (2006) Nature , vol.443 , pp. 803-810
    • Caughey, B.1    Baron, G.S.2
  • 39
    • 0027332116 scopus 로고
    • Conversion of a-helices into -sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, et al. Conversion of a-helices into -sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA. 1993;90:10962-10966.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3    Gasset, M.4    Serban, A.5    Groth, D.6    Al, E.7
  • 40
    • 33748857338 scopus 로고    scopus 로고
    • Pathogenesis of prion diseases: Current status and future outlook
    • Aguzzi A, Heikenwalder M. Pathogenesis of prion diseases: current status and future outlook. Nat Rev Microbiol. 2006;4:765-775.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 765-775
    • Aguzzi, A.1    Heikenwalder, M.2
  • 41
    • 17444413067 scopus 로고    scopus 로고
    • In vitro generation of infectious scrapie prions
    • Castilla J, Saa P, Hetz C, Soto C. In vitro generation of infectious scrapie prions. Cell. 2005;121:195-206.
    • (2005) Cell , vol.121 , pp. 195-206
    • Castilla, J.1    Saa, P.2    Hetz, C.3    Soto, C.4
  • 42
    • 0348077417 scopus 로고    scopus 로고
    • A neuronal isoform of the aplysia CPEB has prion-like properties
    • Si K, Lindquist S, Kandel ER. A neuronal isoform of the aplysia CPEB has prion-like properties. Cell. 2003;115: 879-891.
    • (2003) Cell , vol.115 , pp. 879-891
    • Si, K.1    Lindquist, S.2    Kandel, E.R.3
  • 44
    • 0029888121 scopus 로고    scopus 로고
    • Propagation of the yeast prion-like [psi + ] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor
    • Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD. Propagation of the yeast prion-like [psi + ] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor. EMBO J. 1996;15:3127-3134.
    • (1996) EMBO J , vol.15 , pp. 3127-3134
    • Paushkin, S.V.1    Kushnirov, V.V.2    Smirnov, V.N.3    Ter-Avanesyan, M.D.4
  • 46
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • Arai M, Kuwajima K. Role of the molten globule state in protein folding. Adv Protein Chem. 2000;53:209-282.
    • (2000) Adv Protein Chem , vol.53 , pp. 209-282
    • Arai, M.1    Kuwajima, K.2
  • 47
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn OB. Molten globule and protein folding. Adv Protein Chem. 1995;47:83-229.
    • (1995) Adv Protein Chem , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 48
    • 70350756300 scopus 로고
    • The proteids of milk
    • Halliburton WD. The proteids of milk. J Physiol. 1890; 11:448-463pp
    • (1890) J Physiol , vol.11 , pp. 448-463
    • Halliburton, W.D.1
  • 49
    • 0025756737 scopus 로고
    • The importance of a-lactalbumin in infant nutrition
    • Heine WE, Klein PD, Reeds PJ. The importance of a-lactalbumin in infant nutrition. J Nutr. 1991;121:277-283.
    • (1991) J Nutr , vol.121 , pp. 277-283
    • Heine, W.E.1    Klein, P.D.2    Reeds, P.J.3
  • 50
    • 0021924964 scopus 로고
    • Casein content of human milk
    • Lonnerdal B, Forsum E. Casein content of human milk. Am J Clin Nutr. 1985;41:113-120.
    • (1985) Am J Clin Nutr , vol.41 , pp. 113-120
    • Lonnerdal, B.1    Forsum, E.2
  • 53
    • 0032492714 scopus 로고    scopus 로고
    • Structural evidence for the presence of a secondary calcium binding site in human a-lactalbumin
    • Chandra N, Brew K, Acharya KR. Structural evidence for the presence of a secondary calcium binding site in human a-lactalbumin. Biochemistry. 1998;37:4767-4772.
    • (1998) Biochemistry , vol.37 , pp. 4767-4772
    • Chandra, N.1    Brew, K.2    Acharya, K.R.3
  • 54
    • 0020484071 scopus 로고
    • Crystallization of human a-lactalbumin
    • Fenna RE. Crystallization of human a-lactalbumin. J Mol Biol. 1982;161:211-215.
    • (1982) J Mol Biol , vol.161 , pp. 211-215
    • Fenna, R.E.1
  • 55
    • 0014940135 scopus 로고
    • The disulfide bonds of bovine a-lactalbumin
    • Vanaman TC, Brew K, Hill RL. The disulfide bonds of bovine a-lactalbumin. J Biol Chem. 1970;245:4583-4590.
    • (1970) J Biol Chem , vol.245 , pp. 4583-4590
    • Vanaman, T.C.1    Brew, K.2    Hill, R.L.3
  • 57
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of a-lactalbumin
    • Kuwajima K. The molten globule state of a-lactalbumin. FASEB J. 1996;10:102-109.
    • (1996) FASEB J , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 58
    • 21144446625 scopus 로고    scopus 로고
    • Multiple subsets of side-chain packing in partially folded states of a-lactalbumins
    • Mok KH, Nagashima T, Day IJ, Hore PJ, Dobson CM. Multiple subsets of side-chain packing in partially folded states of a-lactalbumins. Proc Natl Acad Sci USA. 2005;102:8899-8904.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8899-8904
    • Mok, K.H.1    Nagashima, T.2    Day, I.J.3    Hore, P.J.4    Dobson, C.M.5
  • 59
    • 0028334906 scopus 로고
    • A protein dissection study of a molten globule
    • Peng ZY, Kim PS. A protein dissection study of a molten globule. Biochemistry. 1994;33:2136-2141.
    • (1994) Biochemistry , vol.33 , pp. 2136-2141
    • Peng, Z.Y.1    Kim, P.S.2
  • 60
    • 0028866620 scopus 로고
    • Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human a-lactalbumin
    • Schulman BA, Redfield C, Peng ZY, Dobson CM, Kim PS. Different subdomains are most protected from hydrogen exchange in the molten globule and native states of human a-lactalbumin. J Mol Biol. 1995;253:651-657.
    • (1995) J Mol Biol , vol.253 , pp. 651-657
    • Schulman, B.A.1    Redfield, C.2    Peng, Z.Y.3    Dobson, C.M.4    Kim, P.S.5
  • 61
    • 0027280472 scopus 로고
    • Structure and stability of the molten globule state of guinea-pig a-lactalbumin: A hydrogen exchange study
    • Chyan CL, Wormald C, Dobson CM, Evans PA, Baum J. Structure and stability of the molten globule state of guinea-pig a-lactalbumin: a hydrogen exchange study. Biochemistry. 1993;32:5681-5691.
    • (1993) Biochemistry , vol.32 , pp. 5681-5691
    • Chyan, C.L.1    Wormald, C.2    Dobson, C.M.3    Evans, P.A.4    Baum, J.5
  • 62
    • 0037110569 scopus 로고    scopus 로고
    • Molten globule of bovine a-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: A comparative analysis by circular dichroism spectroscopy and limited proteolysis
    • Polverino de Laureto P, Frare E, Gottardo R, Fontana A. Molten globule of bovine a-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis. Proteins. 2002;49:385-397.
    • (2002) Proteins , vol.49 , pp. 385-397
    • Polverino De Laureto, P.1    Frare, E.2    Gottardo, R.3    Fontana, A.4
  • 63
    • 0028952169 scopus 로고
    • Bipartite structure of the a-lactalbumin molten globule
    • Wu LC, Peng ZY, Kim PS. Bipartite structure of the a-lactalbumin molten globule. Nat Struct Biol. 1995;2:281-286.
    • (1995) Nat Struct Biol , vol.2 , pp. 281-286
    • Wu, L.C.1    Peng, Z.Y.2    Kim, P.S.3
  • 64
    • 0032479440 scopus 로고    scopus 로고
    • A specific hydrophobic core in the alpha-lactalbumin molten globule
    • Wu LC, Kim PS. A specific hydrophobic core in the alpha-lactalbumin molten globule. J Mol Biol. 1998;280: 175-182.
    • (1998) J Mol Biol , vol.280 , pp. 175-182
    • Wu, L.C.1    Kim, P.S.2
  • 65
    • 33646386189 scopus 로고    scopus 로고
    • Commun Res Biophys Biochem Death. Cell Tumor And Formation Hamlet Variation Species A-Lactalbumin C. Svanborg M.Ak
    • Pettersson J, Mossberg AK, Svanborg C. a-Lactalbumin species variation, HAMLET formation, and tumor cell death. Biochem Biophys Res Commun. 2006;345:260-270.
    • (2006) , vol.345 , pp. 260-270
    • Pettersson, J.1    Mossberg, A.K.2    Svanborg, C.3
  • 66
    • 4544250589 scopus 로고    scopus 로고
    • Kinetics of folding and unfolding of goat a-lactalbumin
    • Chedad A, Van Dael H. Kinetics of folding and unfolding of goat a-lactalbumin. Proteins. 2004;57:345-356.
    • (2004) Proteins , vol.57 , pp. 345-356
    • Chedad, A.1    Van Dael, H.2
  • 70
    • 10744223979 scopus 로고    scopus 로고
    • A-Lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human a-lactalbumin made lethal to tumor cells)
    • Svensson M, Fast J, Mossberg AK, Duringer C, Gustafsson L, Hallgren O, et al. a-Lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human a-lactalbumin made lethal to tumor cells). Protein Sci. 2003;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    Al, E.7
  • 71
    • 0030025082 scopus 로고    scopus 로고
    • Disulfide determinants of calcium-induced packing in a-lactalbumin
    • Wu LC, Schulman BA, Peng ZY, Kim PS. Disulfide determinants of calcium-induced packing in a-lactalbumin. Biochemistry. 1996;35:859-863.
    • (1996) Biochemistry , vol.35 , pp. 859-863
    • Wu, L.C.1    Schulman, B.A.2    Peng, Z.Y.3    Kim, P.S.4
  • 72
    • 0030013938 scopus 로고    scopus 로고
    • The lipids in human milk
    • Jensen RG. The lipids in human milk. Prog Lipid Res. 1996;35:53-92.
    • (1996) Prog Lipid Res , vol.35 , pp. 53-92
    • Jensen, R.G.1
  • 73
    • 0344201898 scopus 로고    scopus 로고
    • Lipids as cofactors in protein folding: Stereo-specific lipid-protein interactions are required to form HAMLET (human a-lactalbumin made lethal to tumor cells)
    • Svensson M, Mossberg AK, Pettersson J, Linse S, Svanborg C. Lipids as cofactors in protein folding: Stereo-specific lipid-protein interactions are required to form HAMLET (human a-lactalbumin made lethal to tumor cells). Protein Sci. 2003;12:2805-2814.
    • (2003) Protein Sci , vol.12 , pp. 2805-2814
    • Svensson, M.1    Mossberg, A.K.2    Pettersson, J.3    Linse, S.4    Svanborg, C.5
  • 76
    • 0035160316 scopus 로고    scopus 로고
    • A folding variant of human a-lactalbumin induces mitochondrial permeability transition in isolated mitochondria
    • Kohler C, Gogvadze V, Hakansson A, Svanborg C, Orrenius S, Zhivotovsky B. A folding variant of human a-lactalbumin induces mitochondrial permeability transition in isolated mitochondria. Eur J Biochem. 2001;268:186-191.
    • (2001) Eur J Biochem , vol.268 , pp. 186-191
    • Kohler, C.1    Gogvadze, V.2    Hakansson, A.3    Svanborg, C.4    Orrenius, S.5    Zhivotovsky, B.6
  • 79
    • 27644466759 scopus 로고    scopus 로고
    • Autophagy and signaling: Their role in cell survival and cell death
    • Codogno P, Meijer AJ. Autophagy and signaling: their role in cell survival and cell death. Cell Death Differ. 2005;12 Suppl 2:1509-1518.
    • (2005) Cell Death Differ , vol.12 , Issue.SUPPL. 2 , pp. 1509-1518
    • Codogno, P.1    Meijer, A.J.2
  • 80
    • 20344387475 scopus 로고    scopus 로고
    • Autophagy: Dual roles in life and death?
    • Baehrecke EH. Autophagy: dual roles in life and death? Nat Rev Mol Cell Biol. 2005;6:505-510.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 505-510
    • Baehrecke, E.H.1
  • 81
  • 83
    • 1542405871 scopus 로고    scopus 로고
    • Human a-lactalbumin made lethal to tumor cells (HAMLET) kills human glioblastoma cells in brain xenografts by an apoptosis-like mechanism and prolongs survival
    • Fischer W, Gustafsson L, Mossberg AK, Gronli J, Mork S, Bjerkvig R, et al. Human a-lactalbumin made lethal to tumor cells (HAMLET) kills human glioblastoma cells in brain xenografts by an apoptosis-like mechanism and prolongs survival. Cancer Res. 2004;64:2105-2112.
    • (2004) Cancer Res , vol.64 , pp. 2105-2112
    • Fischer, W.1    Gustafsson, L.2    Mossberg, A.K.3    Gronli, J.4    Mork, S.5    Bjerkvig, R.6    Al, E.7
  • 84
  • 85
    • 0028985861 scopus 로고
    • Baumeister W Conformational constraints in protein degradation by the 20S proteasome
    • Wenzel T, Baumeister W Conformational constraints in protein degradation by the 20S proteasome. Nat Struct Biol. 1995;2:199-204.
    • (1995) Nat Struct Biol , vol.2 , pp. 199-204
    • Wenzel, T.1
  • 88
    • 34548073069 scopus 로고    scopus 로고
    • Bladder cancers respond to intravesical instillation of HAMLET (human a-lactalbumin made lethal to tumor cells)
    • Mossberg AK, Wullt B, Gustafsson L, Mansson W, Ljungg-ren E, Svanborg C. Bladder cancers respond to intravesical instillation of HAMLET (human a-lactalbumin made lethal to tumor cells). Int J Cancer. 2007;121:1352-1359.
    • (2007) Int J Cancer , vol.121 , pp. 1352-1359
    • Mossberg, A.K.1    Wullt, B.2    Gustafsson, L.3    Mansson, W.4    Ljungg-Ren, E.5    Svanborg, C.6
  • 90
    • 0038425042 scopus 로고    scopus 로고
    • Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis
    • Fernandez A, Berry RS. Proteins with H-bond packing defects are highly interactive with lipid bilayers: implications for amyloidogenesis. Proc Natl Acad Sci USA. 2003; 100:2391-2396.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2391-2396
    • Fernandez, A.1    Berry, R.S.2
  • 91
    • 7544245555 scopus 로고    scopus 로고
    • Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers
    • Sparr E, Engel MF, Sakharov DV, Sprong M, Jacobs J, de Kruijff B, et al. Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers. FEBS Lett. 2004;577:117-120.
    • (2004) FEBS Lett , vol.577 , pp. 117-120
    • Sparr, E.1    Engel, M.F.2    Sakharov, D.V.3    Sprong, M.4    Jacobs, J.5    De Kruijff, B.6    Al, E.7
  • 92
    • 14344250143 scopus 로고    scopus 로고
    • Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers
    • Zhao H, Jutila A, Nurminen T, Wickstrom SA, Keski-Oja J, Kinnunen PK. Binding of endostatin to phosphatidylserine-containing membranes and formation of amyloid-like fibers. Biochemistry. 2005;44:2857-2863.
    • (2005) Biochemistry , vol.44 , pp. 2857-2863
    • Zhao, H.1    Jutila, A.2    Nurminen, T.3    Wickstrom, S.A.4    Keski-Oja, J.5    Kinnunen, P.K.6
  • 93
    • 4043100348 scopus 로고    scopus 로고
    • Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
    • Zhao H, Tuominen EK, Kinnunen PK. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry. 2004;43:10302-10307.
    • (2004) Biochemistry , vol.43 , pp. 10302-10307
    • Zhao, H.1    Tuominen, E.K.2    Kinnunen, P.K.3
  • 94
    • 0025743796 scopus 로고
    • Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes
    • Utsugi T, Schroit AJ, Connor J, Bucana CD, Fidler IJ. Elevated expression of phosphatidylserine in the outer membrane leaflet of human tumor cells and recognition by activated human blood monocytes. Cancer Res. 1991;51: 3062-3066.
    • (1991) Cancer Res , vol.51 , pp. 3062-3066
    • Utsugi, T.1    Schroit, A.J.2    Connor, J.3    Bucana, C.D.4    Fidler, I.J.5
  • 95
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM. Protein folding and misfolding. Nature. 2003; 426:884-890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 96
    • 33750576527 scopus 로고    scopus 로고
    • Prions: Protein only or something more? Overview of potential prion cofactors
    • Fasano C, Campana V, Zurzolo C. Prions: protein only or something more? Overview of potential prion cofactors. J Mol Neurosci. 2006;29:195-214.
    • (2006) J Mol Neurosci , vol.29 , pp. 195-214
    • Fasano, C.1    Campana, V.2    Zurzolo, C.3
  • 100
    • 33748286734 scopus 로고    scopus 로고
    • Liang y Oleic acid inhibits amyloid formation of the intermediate of a-lactalbumin at moderately acidic pH
    • Yang F Jr, Zhang M, Zhou BR, Chen J, Liang Y Oleic acid inhibits amyloid formation of the intermediate of a-lactalbumin at moderately acidic pH. J Mol Biol. 2006;362: 821-834.
    • (2006) J Mol Biol , vol.362 , pp. 821-834
    • Yang Jr, F.1    Zhang, M.2    Zhou, B.R.3    Chen, J.4
  • 101
    • 33748942106 scopus 로고    scopus 로고
    • Interaction of the antimicrobial peptide pheromone plantaricin A with model membranes: Implications for a novel mechanism of action
    • Zhao H, Sood R, Jutila A, Bose S, Fimland G, Nissen-Meyer J, et al. Interaction of the antimicrobial peptide pheromone plantaricin A with model membranes: implications for a novel mechanism of action. Biochim Biophys Acta. 2006;1758:1461-1474pp
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1461-1474
    • Zhao, H.1    Sood, R.2    Jutila, A.3    Bose, S.4    Fimland, G.5    Nissen-Meyer, J.6    Al, E.7
  • 104
    • 0027220867 scopus 로고
    • Acharya KR. a-lactalbumin possesses a distinct zinc binding site
    • Ren J, Stuart DI, Acharya KR. a-lactalbumin possesses a distinct zinc binding site. J Biol Chem. 1993;268:19292-19298.
    • (1993) J Biol Chem , vol.268 , pp. 19292-19298
    • Ren, J.1    Stuart, D.I.2
  • 105
    • 0030986132 scopus 로고    scopus 로고
    • BanaszakL. the crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates
    • Thompson J, Winter N, Terwey D, Bratt J, BanaszakL. The crystal structure of the liver fatty acid-binding protein. A complex with two bound oleates. J Biol Chem. 1997;272: 7140-7150.
    • (1997) J Biol Chem , vol.272 , pp. 7140-7150
    • Thompson, J.1    Winter, N.2    Terwey, D.3    Bratt, J.4
  • 106
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph. 1996;14:51-5, 29-32pp
    • (1996) J Mol Graph , vol.14 , Issue.5-51 , pp. 29-32
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3


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