메뉴 건너뛰기




Volumn 16, Issue 3, 2015, Pages 228-242

Disorder in milk proteins: Caseins, intrinsically disordered colloids

Author keywords

Casein; Colloid; Intrinsically disordered protein; Milk protein; Phosphoprotein

Indexed keywords

CALCIUM PHOSPHATE; CASEIN; CASEINOMACROPEPTIDE; CHAPERONE; GLYCOPROTEIN; INTRINSICALLY DISORDERED PROTEIN; KAPPA CASEIN; MILK PROTEIN; UNCLASSIFIED DRUG; COLLOID;

EID: 84928806599     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/1389203716666150224145900     Document Type: Article
Times cited : (39)

References (208)
  • 1
    • 84884353426 scopus 로고    scopus 로고
    • Invited review: Caseins and the casein micelle: Their biological functions, structures, and behavior in foods
    • Holt, C.; Carver, J.A.; Ecroyd, H.; Thorn, D.C. Invited review: Caseins and the casein micelle: their biological functions, structures, and behavior in foods. J. Dairy Sci., 2013, 96, 6127-6146.
    • (2013) J. Dairy Sci. , vol.96 , pp. 6127-6146
    • Holt, C.1    Carver, J.A.2    Ecroyd, H.3    Thorn, D.C.4
  • 2
    • 67649836543 scopus 로고    scopus 로고
    • Dephosphorylation of alpha(S)-and beta-caseins and its effect on chaperone activity: A structural and functional investigation
    • Koudelka, T.; Hoffmann, P.; Carver, J.A. Dephosphorylation of alpha(s)-and beta-caseins and its effect on chaperone activity: a structural and functional investigation. J. Agric. Food Chem., 2009, 57, 5956-5964.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 5956-5964
    • Koudelka, T.1    Hoffmann, P.2    Carver, J.A.3
  • 3
    • 79959478941 scopus 로고    scopus 로고
    • The evolution of milk casein genes from tooth genes before the origin of mammals
    • Kawasaki, K.; Lafont, A.G.; Sire, J.Y. The evolution of milk casein genes from tooth genes before the origin of mammals. Mol. Biol. Evol., 2011, 28, 2053-2061.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2053-2061
    • Kawasaki, K.1    Lafont, A.G.2    Sire, J.Y.3
  • 5
    • 0025190584 scopus 로고
    • Human-milk proteins: Analysis of casein and casein subunits by anion-exchange chromatography, gel electrophoresis, and specific staining methods
    • Kunz, C.; Lonnerdal, B. Human-milk proteins: analysis of casein and casein subunits by anion-exchange chromatography, gel electrophoresis, and specific staining methods. Am. J. Clin. Nutr., 1990, 51, 37-46.
    • (1990) Am. J. Clin. Nutr. , vol.51 , pp. 37-46
    • Kunz, C.1    Lonnerdal, B.2
  • 6
    • 0002409037 scopus 로고    scopus 로고
    • Formation and structure of casein micelles
    • McKenzie, H.A., Editor. 1971, Academic Press: New York
    • Waugh, D.F. Formation and structure of casein micelles, in Milk Proteins: Chemistry and Molecular Biology, McKenzie, H.A., Editor. 1971, Academic Press: New York. p. 3-79.
    • Milk Proteins: Chemistry and Molecular Biology , pp. 3-79
    • Waugh, D.F.1
  • 7
    • 4143054391 scopus 로고    scopus 로고
    • Chemistry of caseins
    • Fox, P.F., Editor. 1992, Elsevier Applied Science: London, U.K
    • Swaisgood, H.E. Chemistry of caseins, in Advanced Dairy Chemistry, Fox, P.F., Editor. 1992, Elsevier Applied Science: London, U.K. p. 139-201.
    • Advanced Dairy Chemistry , pp. 139-201
    • Swaisgood, H.E.1
  • 8
    • 4143054391 scopus 로고    scopus 로고
    • Chemistry of the caseins
    • Fox, P.F.; Sweeney, P.L.H., Editors. 2003, Kluwer Academic/Plenum: New York
    • Swaisgood, H.E. Chemistry of the caseins, in Advanced Dairy Chemistry-1, Proteins, Fox, P.F.; Sweeney, P.L.H., Editors. 2003, Kluwer Academic/Plenum: New York. p. 139-201.
    • Advanced Dairy Chemistry-1, Proteins , pp. 139-201
    • Swaisgood, H.E.1
  • 9
    • 0018463652 scopus 로고
    • The kinetics of the precipitation of chemically modified alpha S1-casein by calcium
    • Horne, D.S. The kinetics of the precipitation of chemically modified alpha S1-casein by calcium. J. Dairy Res., 1979, 46, 265-269.
    • (1979) J. Dairy Res. , vol.46 , pp. 265-269
    • Horne, D.S.1
  • 10
    • 0016606712 scopus 로고
    • The thermochemistry of reactions between alpha-s1-casein and calcium chloride
    • Holt, C.; Parker, T.G.; Dalgleish, D.G. The thermochemistry of reactions between alpha-s1-casein and calcium chloride. Biochim. Biophys. Acta., 1975, 379, 638-644.
    • (1975) Biochim. Biophys. Acta. , vol.379 , pp. 638-644
    • Holt, C.1    Parker, T.G.2    Dalgleish, D.G.3
  • 11
    • 79952584407 scopus 로고    scopus 로고
    • Structure and stabilizing interactions of casein micelles probed by high-pressure light scattering and FTIR
    • Gebhardt, R.; Takeda, N.; Kulozik, U.; Doster, W. Structure and stabilizing interactions of casein micelles probed by high-pressure light scattering and FTIR. J. Phys. Chem. B, 2011, 115, 2349-2359.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 2349-2359
    • Gebhardt, R.1    Takeda, N.2    Kulozik, U.3    Doster, W.4
  • 13
    • 41849125311 scopus 로고    scopus 로고
    • Studies of casein micelle structure: The past and the present
    • Qi, P.X. Studies of casein micelle structure: the past and the present. Lait, 2007, 87, 363-383.
    • (2007) Lait , vol.87 , pp. 363-383
    • Qi, P.X.1
  • 14
    • 84894041409 scopus 로고    scopus 로고
    • Interspecies comparison of milk proteins: Quantitative variability and molecular diversity
    • McSweeney, P.L.H.; Fox, P.F., Editors. 2013, SpringerNew York, NY, USA
    • Martin, P.; Cebo, C.; Miranda, G. Interspecies comparison of milk proteins: quantitative variability and molecular diversity, in Advanced Dairy Chemistry, McSweeney, P.L.H.; Fox, P.F., Editors. 2013, Springer: New York, NY, USA. p. 386-429.
    • Advanced Dairy Chemistry , pp. 386-429
    • Martin, P.1    Cebo, C.2    Miranda, G.3
  • 15
    • 33744991713 scopus 로고    scopus 로고
    • Casein micelle structure: Models and muddles
    • Horne, D.S. Casein micelle structure: Models and muddles. Curr. Opin. Colloid Interface Sci., 2006, 11, 148-153.
    • (2006) Curr. Opin. Colloid Interface Sci. , vol.11 , pp. 148-153
    • Horne, D.S.1
  • 16
    • 0037433089 scopus 로고    scopus 로고
    • Casein micelles as hard spheres: Limitations of the model in acidified gel formation. Colloids Surf A: Physicochem
    • Horne, D.S. Casein micelles as hard spheres: limitations of the model in acidified gel formation. Colloids Surf A: Physicochem. Eng. Aspects, 2003, 213, 255-263.
    • (2003) Eng. Aspects , vol.213 , pp. 255-263
    • Horne, D.S.1
  • 17
    • 0001871181 scopus 로고    scopus 로고
    • The hairy casein micelle: Evolution of the concept and its implications for dairy processing
    • Holt, C.; Horne, D.S. The hairy casein micelle: Evolution of the concept and its implications for dairy processing. Neth. Milk Dairy J., 1996, 50, 1-27.
    • (1996) Neth. Milk Dairy J. , vol.50 , pp. 1-27
    • Holt, C.1    Horne, D.S.2
  • 18
    • 0032520111 scopus 로고    scopus 로고
    • Core-shell model of calcium phosphate nanoclusters stabilized by beta-casein phosphopeptides, derived from sedimentation equilibrium and small-angle X-ray and neutron-scattering measurements
    • Holt, C.; Timmins, P.A.; Errington, N.; Leaver, J. A core-shell model of calcium phosphate nanoclusters stabilized by beta-casein phosphopeptides, derived from sedimentation equilibrium and small-angle X-ray and neutron-scattering measurements. Eur. J. Biochem., 1998, 252, 73-78.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 73-78
    • Holt, C.1    Timmins, P.A.2    Errington, N.3    Leaver, J.A.4
  • 19
    • 0002429127 scopus 로고
    • Association of caseins and casein micelle structure
    • Fox, P.F., Editor. , Applied Science Publishers: Barking, UK
    • Schmidt, D.G. Association of caseins and casein micelle structure, in Developments in Dairy Chemistry, Fox, P.F., Editor. 1982, Applied Science Publishers: Barking, UK. p. 61-86.
    • (1982) Developments in Dairy Chemistry , pp. 61-86
    • Schmidt, D.G.1
  • 20
    • 0017000653 scopus 로고
    • Review: Casein micelle structure; an examination of models
    • Slattery, C.W. Review: Casein micelle structure; an examination of models. J. Dairy Sci., 1976, 59, 1547-1556.
    • (1976) J. Dairy Sci. , vol.59 , pp. 1547-1556
    • Slattery, C.W.1
  • 21
    • 0020198223 scopus 로고
    • Stable and unstable casein micelles
    • Payens, T.A. Stable and unstable casein micelles. J. Dairy Sci., 1982, 65, 1863-1873.
    • (1982) J. Dairy Sci. , vol.65 , pp. 1863-1873
    • Payens, T.A.1
  • 22
    • 0000529133 scopus 로고    scopus 로고
    • Casein Association and Micelle Formation
    • Fox, P.F., Editor. 1992, Elsevier Applied Science: Barking, Essex, UK
    • Rollema, H.S. Casein Association and Micelle Formation, in Advanced Dairy Chemistry, Fox, P.F., Editor. 1992, Elsevier Applied Science: Barking, Essex, UK p. 111-140.
    • Advanced Dairy Chemistry , pp. 111-140
    • Rollema, H.S.1
  • 23
    • 0026668858 scopus 로고
    • Structure and stability of bovine casein micelles
    • Holt, C. Structure and stability of bovine casein micelles. Adv. Protein Chem., 1992, 43, 63-151.
    • (1992) Adv. Protein Chem. , vol.43 , pp. 63-151
    • Holt, C.1
  • 24
    • 0027685785 scopus 로고
    • Review and update of casein chemistry
    • Swaisgood, H.E. Review and update of casein chemistry. J. Dairy Sci., 1993, 76, 3054-3061.
    • (1993) J. Dairy Sci. , vol.76 , pp. 3054-3061
    • Swaisgood, H.E.1
  • 25
    • 0036866003 scopus 로고    scopus 로고
    • Casein structure, self-assembly and gelation
    • Horne, D.S. Casein structure, self-assembly and gelation. Curr. Opin. Colloid Interface Sci., 2002, 7, 456-461.
    • (2002) Curr. Opin. Colloid Interface Sci. , vol.7 , pp. 456-461
    • Horne, D.S.1
  • 26
    • 0036912357 scopus 로고    scopus 로고
    • The self-assembly and structure of caseins in solution
    • Morris, G.A. The self-assembly and structure of caseins in solution. Biotechnol. Genet. Eng. Rev., 2002, 19, 357-376.
    • (2002) Biotechnol. Genet. Eng. Rev. , vol.19 , pp. 357-376
    • Morris, G.A.1
  • 27
    • 0348114294 scopus 로고    scopus 로고
    • Casein micelle structure, functions and interactions
    • Proteins, Fox, P.F.; McSweeney, P.L.H., Editors. 2003, Kluwer Academic/Plenum Publishers: New York
    • De Kruif, C.G.; Holt, C. Casein micelle structure, functions and interactions, in Advanced Dairy Chemistry, Proteins, Fox, P.F.; McSweeney, P.L.H., Editors. 2003, Kluwer Academic/Plenum Publishers: New York. p. 233-276.
    • Advanced Dairy Chemistry , pp. 233-276
    • De Kruif, C.G.1    Holt, C.2
  • 28
    • 33744998881 scopus 로고    scopus 로고
    • Casein micelle structure: What can be learned from milk synthesis and structural biology
    • Farrell, H.M.J.; Malin, E.L.; Brown, E.M.; Qi, P.X. Casein micelle structure: What can be learned from milk synthesis and structural biology? Curr. Opin. Colloid Interface Sci., 2006, 11, 135-147.
    • (2006) Curr. Opin. Colloid Interface Sci. , vol.11 , pp. 135-147
    • Farrell, H.1    Malin, E.L.2    Brown, E.M.3    Qi, P.X.4
  • 29
    • 44549088735 scopus 로고    scopus 로고
    • The casein micelle: Historical aspects, current concepts and significance
    • Fox, P.F.; Brodkorb, A. The casein micelle: Historical aspects, current concepts and significance. Int. Dairy J., 2008, 18, 677-684.
    • (2008) Int. Dairy J. , vol.18 , pp. 677-684
    • Fox, P.F.1    Brodkorb, A.2
  • 30
    • 84862647834 scopus 로고    scopus 로고
    • The structure of the casein micelle of milk and its changes during processing
    • Dalgleish, D.G.; Corredig, M. The structure of the casein micelle of milk and its changes during processing. Annu. Rev. Food Sci. Technol., 2012, 3, 449-467.
    • (2012) Annu. Rev. Food Sci. Technol. , vol.3 , pp. 449-467
    • Dalgleish, D.G.1    Corredig, M.2
  • 31
    • 0038737944 scopus 로고    scopus 로고
    • Thermodynamics of micellization of bovine betacasein studied by high-sensitivity differential scanning calorimetry
    • Mikheeva, L.M.; Grinberg, N.V.; Grinberg, V.Y.; Khokhlov, A.R.; de Kruif, C.G. Thermodynamics of micellization of bovine betacasein studied by high-sensitivity differential scanning calorimetry. Langmuir, 2003, 19, 2913-2921.
    • (2003) Langmuir , vol.19 , pp. 2913-2921
    • Mikheeva, L.M.1    Grinberg, N.V.2    Grinberg, V.Y.3    Khokhlov, A.R.4    De Kruif, C.G.5
  • 32
    • 33746967183 scopus 로고    scopus 로고
    • Micellization of bovine beta-casein studied by isothermal titration microcalorimetry and cryogenic transmission electron microscopy
    • Portnaya, I.; Cogan, U.; Livney, Y.D.; Ramon, O.; Shimoni, K.; Rosenberg, M.; Danino, D. Micellization of bovine beta-casein studied by isothermal titration microcalorimetry and cryogenic transmission electron microscopy. J. Agric. Food Chem., 2006, 54, 5555-5561.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 5555-5561
    • Portnaya, I.1    Cogan, U.2    Livney, Y.D.3    Ramon, O.4    Shimoni, K.5    Rosenberg, M.6    Danino, D.7
  • 33
    • 55949111633 scopus 로고    scopus 로고
    • Casein interactions: Does the chemistry really matter?
    • E.; Leser, M.E., Editors. 2007, Royal Society of Chemistry Special Publications: London, UK
    • Horne, D.S.; Lucey, J.A.; Choi, J.-W. Casein interactions: Does the chemistry really matter?, in Food Colloids: Self-Assembly and Material Science Dickinson, E.; Leser, M.E., Editors. 2007, Royal Society of Chemistry Special Publications: London, UK. p. 155-166.
    • Food Colloids: Self-Assembly and Material Science Dickinson , pp. 155-166
    • Horne, D.S.1    Lucey, J.A.2    Choi, J.-W.3
  • 34
    • 0042856750 scopus 로고    scopus 로고
    • Environmental influences on bovine kappa-casein: Reduction and conversion to fibrillar (amyloid) structures
    • Farrell, H.M. Jr.; Cooke, P.H.; Wickham, E.D.; Piotrowski, E.G.; Hoagland, P.D. Environmental influences on bovine kappa-casein: reduction and conversion to fibrillar (amyloid) structures. J. Protein Chem., 2003, 22, 259-273.
    • (2003) J. Protein Chem. , vol.22 , pp. 259-273
    • Farrell, H.M.1    Cooke, P.H.2    Wickham, E.D.3    Piotrowski, E.G.4    Hoagland, P.D.5
  • 35
    • 29344455729 scopus 로고    scopus 로고
    • Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS-and beta-casein
    • Thorn, D.C.; Meehan, S.; Sunde, M.; Rekas, A.; Gras, S.L.; MacPhee, C.E.; Dobson, C.M.; Wilson, M.R.; Carver, J.A. Amyloid fibril formation by bovine milk kappa-casein and its inhibition by the molecular chaperones alphaS-and beta-casein. Biochemistry, 2005, 44, 17027-17036.
    • (2005) Biochemistry , vol.44 , pp. 17027-17036
    • Thorn, D.C.1    Meehan, S.2    Sunde, M.3    Rekas, A.4    Gras, S.L.5    Macphee, C.E.6    Dobson, C.M.7    Wilson, M.R.8    Carver, J.A.9
  • 36
    • 35748971792 scopus 로고    scopus 로고
    • Evidence for fibril-like structure in bovine casein micelles
    • Lencki, R.W. Evidence for fibril-like structure in bovine casein micelles. J. Dairy Sci., 2007, 90, 75-89.
    • (2007) J. Dairy Sci. , vol.90 , pp. 75-89
    • Lencki, R.W.1
  • 37
    • 36749037242 scopus 로고    scopus 로고
    • Monitoring the prevention of amyloid fibril formation by alphacrystallin. Temperature dependence and the nature of the aggregating species
    • Rekas, A.; Jankova, L.; Thorn, D.C.; Cappai, R.; Carver, J.A. Monitoring the prevention of amyloid fibril formation by alphacrystallin. Temperature dependence and the nature of the aggregating species. FEBS J., 2007, 274, 6290-6304.
    • (2007) FEBS J. , vol.274 , pp. 6290-6304
    • Rekas, A.1    Jankova, L.2    Thorn, D.C.3    Cappai, R.4    Carver, J.A.5
  • 38
    • 44049105911 scopus 로고    scopus 로고
    • Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein
    • Ecroyd, H.; Koudelka, T.; Thorn, D.C.; Williams, D.M.; Devlin, G.; Hoffmann, P.; Carver, J.A. Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein. J. Biol. Chem., 2008, 283, 9012-9022.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9012-9022
    • Ecroyd, H.1    Koudelka, T.2    Thorn, D.C.3    Williams, D.M.4    Devlin, G.5    Hoffmann, P.6    Carver, J.A.7
  • 39
    • 41149181268 scopus 로고    scopus 로고
    • Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein
    • Thorn, D.C.; Ecroyd, H.; Sunde, M.; Poon, S.; Carver, J.A. Amyloid fibril formation by bovine milk alpha s2-casein occurs under physiological conditions yet is prevented by its natural counterpart, alpha s1-casein. Biochemistry, 2008, 47, 3926-3936.
    • (2008) Biochemistry , vol.47 , pp. 3926-3936
    • Thorn, D.C.1    Ecroyd, H.2    Sunde, M.3    Poon, S.4    Carver, J.A.5
  • 40
    • 48949106204 scopus 로고    scopus 로고
    • Kinetics of fibril formation of bovine kappa-casein indicate a conformational rearrangement as a critical step in the process
    • Leonil, J.; Henry, G.; Jouanneau, D.; Delage, M.M.; Forge, V.; Putaux, J.L. Kinetics of fibril formation of bovine kappa-casein indicate a conformational rearrangement as a critical step in the process. J. Mol. Biol., 2008, 381, 1267-1280.
    • (2008) J. Mol. Biol. , vol.381 , pp. 1267-1280
    • Leonil, J.1    Henry, G.2    Jouanneau, D.3    Delage, M.M.4    Forge, V.5    Putaux, J.L.6
  • 41
    • 77954710921 scopus 로고    scopus 로고
    • The dissociated form of kappa-casein is the precursor to its amyloid fibril formation
    • Ecroyd, H.; Thorn, D.C.; Liu, Y.; Carver, J.A. The dissociated form of kappa-casein is the precursor to its amyloid fibril formation. Biochem. J., 2010, 429, 251-260.
    • (2010) Biochem. J. , vol.429 , pp. 251-260
    • Ecroyd, H.1    Thorn, D.C.2    Liu, Y.3    Carver, J.A.4
  • 42
    • 78149466716 scopus 로고    scopus 로고
    • AlphaBCrystallin inhibits the cell toxicity associated with amyloid fibril formation by kappa-casein and the amyloid-beta peptide
    • Dehle, F.C.; Ecroyd, H.; Musgrave, I.F.; Carver, J.A. alphaBCrystallin inhibits the cell toxicity associated with amyloid fibril formation by kappa-casein and the amyloid-beta peptide. Cell Stress Chaperones, 2010, 15, 1013-1026.
    • (2010) Cell Stress Chaperones , vol.15 , pp. 1013-1026
    • Dehle, F.C.1    Ecroyd, H.2    Musgrave, I.F.3    Carver, J.A.4
  • 44
    • 12244312611 scopus 로고    scopus 로고
    • Milk proteins in retrospect
    • McKenzie, H.A., Editor. 1970, Academic Press: New York, NYUSA and London, UK
    • McMeekin, T.L. Milk proteins in retrospect, in Milk proteins chemistry and molecular biology, McKenzie, H.A., Editor. 1970, Academic Press: New York, NY, USA and London, UK. p. 3-15.
    • Milk Proteins Chemistry and Molecular Biology , pp. 3-15
    • McMeekin, T.L.1
  • 45
    • 84927804854 scopus 로고    scopus 로고
    • Casein structures in the context of unfolded proteins
    • in press
    • Thorn, D.C.; Ecroyd, H.; Carver, J.A.; Holt, C. Casein structures in the context of unfolded proteins. Int. Dairy J., 2014, in press.
    • (2014) Int. Dairy J
    • Thorn, D.C.1    Ecroyd, H.2    Carver, J.A.3    Holt, C.4
  • 46
    • 84879179668 scopus 로고    scopus 로고
    • Unfolded phosphopolypeptides enable soft and hard tissues to coexist in the same organism with relative ease
    • Holt, C. Unfolded phosphopolypeptides enable soft and hard tissues to coexist in the same organism with relative ease. Curr. Opin. Struct. Biol., 2013, 23, 420-425.
    • (2013) Curr. Opin. Struct. Biol. , vol.23 , pp. 420-425
    • Holt, C.1
  • 47
    • 80053639107 scopus 로고    scopus 로고
    • Examination of the activity of camel milk casein against hepatitis C virus (Genotype-4a) and its apoptotic potential in hepatoma and hela cell lines
    • Almahdy, O.; El-Fakharany, E.M.; El-Dabaa, E.; Ng, T.B.; Redwan, E.M. Examination of the activity of camel milk casein against hepatitis C virus (genotype-4a) and its apoptotic potential in hepatoma and hela cell lines. Hepat. Mon., 2011, 11, 724-730.
    • (2011) Hepat. Mon. , vol.11 , pp. 724-730
    • Almahdy, O.1    El-Fakharany, E.M.2    El-Dabaa, E.3    Ng, T.B.4    Redwan, E.M.5
  • 48
    • 84892117495 scopus 로고    scopus 로고
    • in Casein: Production, Uses and Health Effects, Ventimiglia, A.M.; Birkenhager, J.M. Editors, Nova Science Publishers: New York
    • Ng, T.B. Health effects of casein, in Casein: Production, Uses and Health Effects, Ventimiglia, A.M.; Birkenhager, J.M. Editors. 2012, Nova Science Publishers: New York.
    • (2012) Health Effects of Casein
    • Ng, T.B.1
  • 50
    • 0033060521 scopus 로고    scopus 로고
    • Molecular chaperone-like properties of an unfolded protein, alpha(S)-casein
    • Bhattacharyya, J.; Das, K.P. Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein. J. Biol. Chem., 1999, 274, 15505-15509.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15505-15509
    • Bhattacharyya, J.1    Das, K.P.2
  • 51
    • 3242804263 scopus 로고    scopus 로고
    • Ability of alphas-Casein to suppress the heat aggregation of ovotransferrin
    • Matsudomi, N.; Kanda, Y.; Yoshika, Y.; Moriwaki, H. Ability of alphas-Casein to suppress the heat aggregation of ovotransferrin. J. Agric. Food Chem., 2004, 52, 4882-4886.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4882-4886
    • Matsudomi, N.1    Kanda, Y.2    Yoshika, Y.3    Moriwaki, H.4
  • 55
    • 48749116996 scopus 로고    scopus 로고
    • Appraisal of casein's inhibitory effects on aggregation accompanying carbonic anhydrase refolding and heat-induced ovalbumin fibrillogenesis
    • Khodarahmi, R.; Beyrami, M.; Soori, H. Appraisal of casein's inhibitory effects on aggregation accompanying carbonic anhydrase refolding and heat-induced ovalbumin fibrillogenesis. Arch. Biochem. Biophys., 2008, 477, 67-76.
    • (2008) Arch. Biochem. Biophys. , vol.477 , pp. 67-76
    • Khodarahmi, R.1    Beyrami, M.2    Soori, H.3
  • 58
    • 74849105568 scopus 로고    scopus 로고
    • Caseins: Utilizing molecular chaperone properties to control protein aggregation in foods
    • Yong, Y.H.; Foegeding, E.A. Caseins: utilizing molecular chaperone properties to control protein aggregation in foods. J. Agric. Food Chem., 2010, 58, 685-693.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 685-693
    • Yong, Y.H.1    Foegeding, E.A.2
  • 59
    • 78650920422 scopus 로고    scopus 로고
    • Alpha casein micelles show not only molecular chaperone-like aggregation inhibition properties but also protein refolding activity from the denatured state
    • Sakono, M.; Motomura, K.; Maruyama, T.; Kamiya, N.; Goto, M. Alpha casein micelles show not only molecular chaperone-like aggregation inhibition properties but also protein refolding activity from the denatured state. Biochem. Biophys. Res. Commun., 2010, 404, 494-497.
    • (2010) Biochem. Biophys. Res. Commun. , vol.404 , pp. 494-497
    • Sakono, M.1    Motomura, K.2    Maruyama, T.3    Kamiya, N.4    Goto, M.5
  • 60
    • 79955901948 scopus 로고    scopus 로고
    • The chaperone action of bovine milk alphaS1-and alphaS2-caseins and their associated form alphaS-casein
    • Treweek, T.M.; Thorn, D.C.; Price, W.E.; Carver, J.A. The chaperone action of bovine milk alphaS1-and alphaS2-caseins and their associated form alphaS-casein. Arch. Biochem. Biophys., 2011, 510, 42-52.
    • (2011) Arch. Biochem. Biophys. , vol.510 , pp. 42-52
    • Treweek, T.M.1    Thorn, D.C.2    Price, W.E.3    Carver, J.A.4
  • 64
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa, P.; Csermely, P. The role of structural disorder in the function of RNA and protein chaperones. FASEB J., 2004, 18, 1169-1175.
    • (2004) FASEB J. , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 65
    • 50649098927 scopus 로고    scopus 로고
    • Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins
    • Kovacs, D.; Kalmar, E.; Torok, Z.; Tompa, P. Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol., 2008, 147, 381-390.
    • (2008) Plant Physiol. , vol.147 , pp. 381-390
    • Kovacs, D.1    Kalmar, E.2    Torok, Z.3    Tompa, P.4
  • 66
    • 50949128448 scopus 로고    scopus 로고
    • Disordered plant LEA proteins as molecular chaperones
    • Kovacs, D.; Agoston, B.; Tompa, P. Disordered plant LEA proteins as molecular chaperones. Plant Signal Behav., 2008, 3, 710-713.
    • (2008) Plant Signal Behav. , vol.3 , pp. 710-713
    • Kovacs, D.1    Agoston, B.2    Tompa, P.3
  • 67
    • 49849101215 scopus 로고    scopus 로고
    • Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities
    • Szollosi, E.; Bokor, M.; Bodor, A.; Perczel, A.; Klement, E.; Medzihradszky, K.F.; Tompa, K.; Tompa, P. Intrinsic structural disorder of DF31, a Drosophila protein of chromatin decondensation and remodeling activities. J. Proteome Res., 2008, 7, 2291-2299.
    • (2008) J. Proteome Res. , vol.7 , pp. 2291-2299
    • Szollosi, E.1    Bokor, M.2    Bodor, A.3    Perczel, A.4    Klement, E.5    Medzihradszky, K.F.6    Tompa, K.7    Tompa, P.8
  • 68
  • 69
    • 77950597578 scopus 로고    scopus 로고
    • Intrinsically disordered chaperones in plants and animals
    • Tompa, P.; Kovacs, D. Intrinsically disordered chaperones in plants and animals. Biochem. Cell Biol., 2010, 88, 167-174.
    • (2010) Biochem. Cell Biol. , vol.88 , pp. 167-174
    • Tompa, P.1    Kovacs, D.2
  • 70
    • 84866644698 scopus 로고    scopus 로고
    • Diverse functional manifestations of intrinsic structural disorder in molecular chaperones
    • Kovacs, D.; Tompa, P. Diverse functional manifestations of intrinsic structural disorder in molecular chaperones. Biochem. Soc. Trans, 2012, 40, 963-968.
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 963-968
    • Kovacs, D.1    Tompa, P.2
  • 71
    • 0024405475 scopus 로고
    • Caseins of various origins and biologically active casein peptides and oligosaccharides: Structural and physiological aspects
    • Fiat, A.M.; Jolles, P. Caseins of various origins and biologically active casein peptides and oligosaccharides: structural and physiological aspects. Mol. Cell Biochem., 1989, 87, 5-30.
    • (1989) Mol. Cell Biochem. , vol.87 , pp. 5-30
    • Fiat, A.M.1    Jolles, P.2
  • 72
    • 0021749271 scopus 로고
    • Novel opioid peptides derived from human beta-casein: Human beta-casomorphins
    • Brantl, V. Novel opioid peptides derived from human beta-casein: human beta-casomorphins. Eur. J. Pharmacol., 1984, 106, 213-214.
    • (1984) Eur. J. Pharmacol. , vol.106 , pp. 213-214
    • Brantl, V.1
  • 73
    • 0019209053 scopus 로고
    • Novel opioid peptides derived from casein (Beta-casomorphins). III. Synthetic peptides corresponding to components from bovine casein peptone
    • Lottspeich, F.; Henschen, A.; Brantl, V.; Teschemacher, H. Novel opioid peptides derived from casein (beta-casomorphins). III. Synthetic peptides corresponding to components from bovine casein peptone. Hoppe Seylers Z Physiol. Chem., 1980, 361, 1835-1839.
    • (1980) Hoppe Seylers Z Physiol. Chem. , vol.361 , pp. 1835-1839
    • Lottspeich, F.1    Henschen, A.2    Brantl, V.3    Teschemacher, H.4
  • 74
    • 0018671846 scopus 로고
    • Novel opioid peptides derived from casein (Beta-casomorphins). II. Structure of active components from bovine casein peptone
    • Henschen, A.; Lottspeich, F.; Brantl, V.; Teschemacher, H. Novel opioid peptides derived from casein (beta-casomorphins). II. Structure of active components from bovine casein peptone. Hoppe Seylers Z Physiol. Chem., 1979, 360, 1217-1224.
    • (1979) Hoppe Seylers Z Physiol. Chem. , vol.360 , pp. 1217-1224
    • Henschen, A.1    Lottspeich, F.2    Brantl, V.3    Teschemacher, H.4
  • 75
    • 0018687626 scopus 로고
    • Novel opioid peptides derived from casein (Beta-casomorphins). I. Isolation from bovine casein peptone
    • Brantl, V.; Teschemacher, H.; Henschen, A.; Lottspeich, F. Novel opioid peptides derived from casein (beta-casomorphins). I. Isolation from bovine casein peptone. Hoppe Seylers Z Physiol. Chem., 1979, 360, 1211-1216.
    • (1979) Hoppe Seylers Z Physiol. Chem. , vol.360 , pp. 1211-1216
    • Brantl, V.1    Teschemacher, H.2    Henschen, A.3    Lottspeich, F.4
  • 78
    • 0020516601 scopus 로고
    • Opioid activities and structures of alpha-casein-derived exorphins
    • Loukas, S.; Varoucha, D.; Zioudrou, C.; Streaty, R.A.; Klee, W.A. Opioid activities and structures of alpha-casein-derived exorphins. Biochemistry, 1983, 22, 4567-4573.
    • (1983) Biochemistry , vol.22 , pp. 4567-4573
    • Loukas, S.1    Varoucha, D.2    Zioudrou, C.3    Streaty, R.A.4    Klee, W.A.5
  • 79
    • 0022862613 scopus 로고
    • Purification and characterization of an opioid antagonist from a peptic digest of bovine kappa-casein
    • Yoshikawa, M.; Tani, F.; Ashikaga, T.; Yoshimura, T.; Chiba, H. Purification and characterization of an opioid antagonist from a peptic digest of bovine kappa-casein. Agric. Biol. Chem., 1986, 50, 2951-2954.
    • (1986) Agric. Biol. Chem , vol.50 , pp. 2951-2954
    • Yoshikawa, M.1    Tani, F.2    Ashikaga, T.3    Yoshimura, T.4    Chiba, H.5
  • 80
    • 0023855229 scopus 로고
    • Casein, a prohormone with an immunomodulating role for the newborn?
    • Migliore-Samour, D.; Jolles, P. Casein, a prohormone with an immunomodulating role for the newborn? Experientia, 1988, 44, 188-193.
    • (1988) Experientia , vol.44 , pp. 188-193
    • Migliore-Samour, D.1    Jolles, P.2
  • 81
    • 5044224700 scopus 로고    scopus 로고
    • Adjunct effect of immunostimulating hexapeptide analogous to human betacasein fragment (54-59) to sodium stibogluconate against experimental visceral leishmaniasis. Immunopharmacol
    • Gupta, S.; Srivastava, V.M.; Puri, A.; Pandey, D.; Haq, W. Adjunct effect of immunostimulating hexapeptide analogous to human betacasein fragment (54-59) to sodium stibogluconate against experimental visceral leishmaniasis. Immunopharmacol. Immunotoxicol., 2004, 26, 425-434.
    • (2004) Immunotoxicol. , vol.26 , pp. 425-434
    • Gupta, S.1    Srivastava, V.M.2    Puri, A.3    Pandey, D.4    Haq, W.5
  • 83
    • 0023218568 scopus 로고
    • Suzuki, H. Studies on the active site and antihypertensive activity of angiotensin I-converting enzyme inhibitors derived from casein
    • Maruyama, S.; Mitachi, H.; Tanaka, H.; Tomizuka, N.; Suzuki, H. Studies on the active site and antihypertensive activity of angiotensin I-converting enzyme inhibitors derived from casein. Agric. Biol. Chem., 1987, 51, 1581-1586.
    • (1987) Agric. Biol. Chem , vol.51 , pp. 1581-1586
    • Maruyama, S.1    Mitachi, H.2    Tanaka, H.3    Tomizuka, N.4
  • 84
    • 0023491123 scopus 로고
    • Angiotensin I-converting enzyme inhibitory activity of the C-terminal hexapeptide of alpha(S1)-casein
    • Maruyama, S.; Mitachi, H.; Awaya, J.; Kurono, M.; Tomizuka, N.; Suzuki, H. Angiotensin I-converting enzyme inhibitory activity of the C-terminal hexapeptide of alpha(S1)-casein. Agric. Biol. Chem., 1987, 51, 2557-2561.
    • (1987) Agric. Biol. Chem. , vol.51 , pp. 2557-2561
    • Maruyama, S.1    Mitachi, H.2    Awaya, J.3    Kurono, M.4    Tomizuka, N.5    Suzuki, H.6
  • 85
    • 0023156817 scopus 로고
    • Bradykinin potentiating peptides isolated from alpha-casein tryptic hydrolysate
    • Henriques, O.B.; de Deus, R.B.; Santos, R.A. Bradykinin potentiating peptides isolated from alpha-casein tryptic hydrolysate. Biochem. Pharmacol., 1987, 36, 182-184.
    • (1987) Biochem. Pharmacol. , vol.36 , pp. 182-184
    • Henriques, O.B.1    De Deus, R.B.2    Santos, R.A.3
  • 87
    • 47649124388 scopus 로고
    • Milk Proteins
    • McMeekin, T.L. Milk Proteins. J. Food Prot., 1952, 15, 57-63.
    • (1952) J. Food Prot , vol.15 , pp. 57-63
    • McMeekin, T.L.1
  • 88
    • 47649094638 scopus 로고
    • Light-scattering study of effect of electrolytes on alpha-and beta-casein solutions
    • Halwer, M. Light-scattering study of effect of electrolytes on alpha-and beta-casein solutions. Arch. Biochem. Biophys., 1954, 51, 79-87.
    • (1954) Arch. Biochem. Biophys. , vol.51 , pp. 79-87
    • Halwer, M.1
  • 89
    • 78651179797 scopus 로고
    • The conformation of casein in aqueous solution
    • Kresheck, G.C. The conformation of casein in aqueous solution. Acta Chem. Scand., 1965, 19, 375-382.
    • (1965) Acta Chem. Scand. , vol.19 , pp. 375-382
    • Kresheck, G.C.1
  • 90
    • 0001517504 scopus 로고
    • Caseins as rheomorphic proteins-Interpretation of primary and secondary structures of the alpha-S1-caseins, beta-caseins and kappa-caseins
    • Holt, C.; Sawyer, L. Caseins as rheomorphic proteins-Interpretation of primary and secondary structures of the alpha-S1-caseins, beta-caseins and kappa-caseins. J. Chem. Soc. Faraday Trans., 1993, 89, 2683-2692.
    • (1993) J. Chem. Soc. Faraday Trans. , vol.89 , pp. 2683-2692
    • Holt, C.1    Sawyer, L.2
  • 91
    • 0038054816 scopus 로고
    • Kinetic study of a limited proteolysis: Action of rennin on kappa-casein
    • Garnier, J. Kinetic study of a limited proteolysis: action of rennin on kappa-casein. Biochim. Biophys. Acta, 1963, 66, 366-377.
    • (1963) Biochim. Biophys. Acta , vol.66 , pp. 366-377
    • Garnier, J.1
  • 92
    • 0015308579 scopus 로고
    • The rate of proteolysis of casein and ovalbumin and the release and metabolism of free amino acids
    • Quantitative studies on nitrogen metabolism in the bovine rumen
    • Mangan, J.L. Quantitative studies on nitrogen metabolism in the bovine rumen. The rate of proteolysis of casein and ovalbumin and the release and metabolism of free amino acids. Br. J. Nutr., 1972, 27, 261-283.
    • (1972) Br. J. Nutr. , vol.27 , pp. 261-283
    • Mangan, J.L.1
  • 93
    • 0015637453 scopus 로고
    • Casein micelle structure: Susceptibility of various casein systems to proteolysis
    • Fox, P.F.; Guiney, J. Casein micelle structure: susceptibility of various casein systems to proteolysis. J. Dairy Res., 1973, 40, 229-234.
    • (1973) J. Dairy Res. , vol.40 , pp. 229-234
    • Fox, P.F.1    Guiney, J.2
  • 94
    • 0023543294 scopus 로고
    • Determination of protein degradation rates using a rumen in vitro system containing inhibitors of microbial nitrogen metabolism
    • Broderick, G.A. Determination of protein degradation rates using a rumen in vitro system containing inhibitors of microbial nitrogen metabolism. Br. J. Nutr., 1987, 58, 463-475.
    • (1987) Br. J. Nutr , vol.58 , pp. 463-475
    • Broderick, G.A.1
  • 95
    • 0023883139 scopus 로고
    • Studies on the proteolytic activity of Bacteroides fragilis
    • Gibson, S.A.; Macfarlane, G.T. Studies on the proteolytic activity of Bacteroides fragilis. J. Gen. Microbiol., 1988, 134, 19-27.
    • (1988) J. Gen. Microbiol. , vol.134 , pp. 19-27
    • Gibson, S.A.1    Macfarlane, G.T.2
  • 97
    • 0021678506 scopus 로고
    • Anomalous behavior of bovine alpha s1-and beta-caseins on gel electrophoresis in sodium dodecyl sulfate buffers
    • Creamer, L.K.; Richardson, T. Anomalous behavior of bovine alpha s1-and beta-caseins on gel electrophoresis in sodium dodecyl sulfate buffers. Arch. Biochem. Biophys., 1984, 234, 476-486.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 476-486
    • Creamer, L.K.1    Richardson, T.2
  • 98
    • 0023705870 scopus 로고
    • The secondary structure of peptides derived from caseins: A circular dichroism study
    • Chaplin, L.C.; Clark, D.C.; Smith, L.J. The secondary structure of peptides derived from caseins: a circular dichroism study. Biochim. Biophys. Acta, 1988, 956, 162-172.
    • (1988) Biochim. Biophys. Acta , vol.956 , pp. 162-172
    • Chaplin, L.C.1    Clark, D.C.2    Smith, L.J.3
  • 99
    • 0026747034 scopus 로고
    • Characterization of the alpha and beta subunits of casein kinase 2 by far-UV CD spectroscopy
    • Issinger, O.G.; Brockel, C.; Boldyreff, B.; Pelton, J.T. Characterization of the alpha and beta subunits of casein kinase 2 by far-UV CD spectroscopy. Biochemistry, 1992, 31, 6098-6103.
    • (1992) Biochemistry , vol.31 , pp. 6098-6103
    • Issinger, O.G.1    Brockel, C.2    Boldyreff, B.3    Pelton, J.T.4
  • 100
    • 0031201781 scopus 로고    scopus 로고
    • Solution conformation of a peptide corresponding to bovine kappa-casein B residues 130-153 by circular dichroism spectroscopy and 1Hnuclear magnetic resonance spectroscopy
    • Plowman, J.E.; Creamer, L.K.; Liddell, M.J.; Cross, J.J. Solution conformation of a peptide corresponding to bovine kappa-casein B residues 130-153 by circular dichroism spectroscopy and 1Hnuclear magnetic resonance spectroscopy. J. Dairy Res., 1997, 64, 377-397.
    • (1997) J. Dairy Res , vol.64 , pp. 377-397
    • Plowman, J.E.1    Creamer, L.K.2    Liddell, M.J.3    Cross, J.J.4
  • 101
  • 102
    • 0032923523 scopus 로고    scopus 로고
    • Effect of selfassociation of alphas1-casein and its cleavage fractions alphas1-casein(136-196) and alphas1-casein(1-197),1 on aromatic circular dichroic spectra: Comparison with predicted models
    • Alaimo, M.H.; Wickham, E.D.; Farrell, H.M. Jr. Effect of selfassociation of alphas1-casein and its cleavage fractions alphas1-casein(136-196) and alphas1-casein(1-197),1 on aromatic circular dichroic spectra: comparison with predicted models. Biochim. Biophys. Acta, 1999, 1431, 395-409.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 395-409
    • Alaimo, M.H.1    Wickham, E.D.2    Farrell, H.M.3
  • 103
    • 34250000513 scopus 로고    scopus 로고
    • PH-induced structural transitions of caseins
    • Chakraborty, A.; Basak, S. pH-induced structural transitions of caseins. J. Photochem. Photobiol. B, 2007, 87, 191-199.
    • (2007) J. Photochem. Photobiol. B , vol.87 , pp. 191-199
    • Chakraborty, A.1    Basak, S.2
  • 104
    • 53049097848 scopus 로고    scopus 로고
    • Interaction with Al and Zn induces structure formation and aggregation in natively unfolded caseins
    • Chakraborty, A.; Basak, S. Interaction with Al and Zn induces structure formation and aggregation in natively unfolded caseins. J. Photochem. Photobiol. B, 2008, 93, 36-43.
    • (2008) J. Photochem. Photobiol. B , vol.93 , pp. 36-43
    • Chakraborty, A.1    Basak, S.2
  • 105
    • 0023414233 scopus 로고
    • Water interactions with varying molecular states of bovine casein: 2H NMR relaxation studies
    • Kumosinski, T.F.; Pessen, H.; Prestrelski, S.J.; Farrell, H.M. Jr. Water interactions with varying molecular states of bovine casein: 2H NMR relaxation studies. Arch. Biochem. Biophys., 1987, 257, 259-268.
    • (1987) Arch. Biochem. Biophys. , vol.257 , pp. 259-268
    • Kumosinski, T.F.1    Pessen, H.2    Prestrelski, S.J.3    Farrell, H.M.4
  • 106
    • 0024345058 scopus 로고
    • A 1H-NMR study of bovine casein micelles; influence of pH, temperature and calcium ions on micellar structure
    • Rollema, H.S.; Brinkhuis, J.A. A 1H-NMR study of bovine casein micelles; influence of pH, temperature and calcium ions on micellar structure. J. Dairy Res., 1989, 56, 417-425.
    • (1989) J. Dairy Res. , vol.56 , pp. 417-425
    • Rollema, H.S.1    Brinkhuis, J.A.2
  • 108
    • 0036105116 scopus 로고    scopus 로고
    • Structural features of bovine caseinomacropeptide A and B by 1H nuclear magnetic resonance spectroscopy
    • Smith, M.H.; Edwards, P.J.; Palmano, K.P.; Creamer, L.K. Structural features of bovine caseinomacropeptide A and B by 1H nuclear magnetic resonance spectroscopy. J. Dairy Res., 2002, 69, 85-94.
    • (2002) J. Dairy Res. , vol.69 , pp. 85-94
    • Smith, M.H.1    Edwards, P.J.2    Palmano, K.P.3    Creamer, L.K.4
  • 109
    • 0021101388 scopus 로고
    • NMR studies of the phosphoserine regions of bovine alpha s1-and beta-casein. Assignment of 31P resonances to specific phosphoserines and cation binding studied by measurement of enhancement of 1H relaxation rate
    • Sleigh, R.W.; Mackinlay, A.G.; Pope, J.M. NMR studies of the phosphoserine regions of bovine alpha s1-and beta-casein. Assignment of 31P resonances to specific phosphoserines and cation binding studied by measurement of enhancement of 1H relaxation rate. Biochim. Biophys. Acta, 1983, 742, 175-183.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 175-183
    • Sleigh, R.W.1    Mackinlay, A.G.2    Pope, J.M.3
  • 110
    • 0021947743 scopus 로고
    • Phosphorus-31 NMR as a probe for phosphoproteins
    • James, T.L. Phosphorus-31 NMR as a probe for phosphoproteins. CRC Crit. Rev. Biochem., 1985, 18, 1-30.
    • (1985) CRC Crit. Rev. Biochem. , vol.18 , pp. 1-30
    • James, T.L.1
  • 112
    • 0027249170 scopus 로고
    • Twodimensional nuclear magnetic resonance study of the beta-casein peptide 1-25: Resonance assignments and secondary structure
    • Wahlgren, N.M.; Leonil, J.; Dejmek, P.; Drakenberg, T. Twodimensional nuclear magnetic resonance study of the beta-casein peptide 1-25: resonance assignments and secondary structure. Biochim. Biophys. Acta, 1993, 1202, 121-128.
    • (1993) Biochim. Biophys. Acta , vol.1202 , pp. 121-128
    • Wahlgren, N.M.1    Leonil, J.2    Dejmek, P.3    Drakenberg, T.4
  • 113
    • 0028533901 scopus 로고
    • Secondary structures in beta-casein peptide 1-42: A two dimensional nuclear magnetic resonance study
    • Wahlgren, N.M.; Dejmek, P.; Drakenberg, T. Secondary structures in beta-casein peptide 1-42: a two dimensional nuclear magnetic resonance study. J. Dairy Res., 1994, 61, 495-506.
    • (1994) J. Dairy Res. , vol.61 , pp. 495-506
    • Wahlgren, N.M.1    Dejmek, P.2    Drakenberg, T.3
  • 115
    • 0035144719 scopus 로고    scopus 로고
    • Solution structure of native proteins with irregular folds from Raman optical activity
    • Smyth, E.; Syme, C.D.; Blanch, E.W.; Hecht, L.; Vasak, M.; Barron, L.D. Solution structure of native proteins with irregular folds from Raman optical activity. Biopolymers, 2001, 58, 138-151.
    • (2001) Biopolymers , vol.58 , pp. 138-151
    • Smyth, E.1    Syme, C.D.2    Blanch, E.W.3    Hecht, L.4    Vasak, M.5    Barron, L.D.6
  • 116
    • 0036157963 scopus 로고    scopus 로고
    • Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins
    • Syme, C.D.; Blanch, E.W.; Holt, C.; Jakes, R.; Goedert, M.; Hecht, L.; Barron, L.D. A Raman optical activity study of rheomorphism in caseins, synucleins and tau. New insight into the structure and behaviour of natively unfolded proteins. Eur. J. Biochem., 2002, 269, 148-156.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 148-156
    • Syme, C.D.1    Blanch, E.W.2    Holt, C.3    Jakes, R.4    Goedert, M.5    Hecht, L.6    Barron, L.7
  • 117
    • 80054680038 scopus 로고    scopus 로고
    • The importance of protonation in the investigation of protein phosphorylation using Raman spectroscopy and Raman optical activity
    • Ashton, L.; Johannessen, C.; Goodacre, R. The importance of protonation in the investigation of protein phosphorylation using Raman spectroscopy and Raman optical activity. Anal. Chem., 2011, 83, 7978-7983.
    • (2011) Anal. Chem. , vol.83 , pp. 7978-7983
    • Ashton, L.1    Johannessen, C.2    Goodacre, R.3
  • 118
    • 84888332224 scopus 로고    scopus 로고
    • Selective DMSO-induced conformational changes in proteins from Raman optical activity
    • Batista, A.N.; Batista, J.M. Jr.; Bolzani, V.S.; Furlan, M.; Blanch, E.W. Selective DMSO-induced conformational changes in proteins from Raman optical activity. Phys. Chem. Chem. Phys., 2013, 15, 20147-20152.
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 20147-20152
    • Batista, A.N.1    Batista, J.M.2    Bolzani, V.S.3    Furlan, M.4    Blanch, E.W.5
  • 119
    • 1542276786 scopus 로고    scopus 로고
    • Raman spectroscopic characterization of secondary structure in natively unfolded proteins: Alpha-synuclein
    • Maiti, N.C.; Apetri, M.M.; Zagorski, M.G.; Carey, P.R.; Anderson, V.E. Raman spectroscopic characterization of secondary structure in natively unfolded proteins: alpha-synuclein. J. Am. Chem. Soc., 2004, 126, 2399-2408.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2399-2408
    • Maiti, N.C.1    Apetri, M.M.2    Zagorski, M.G.3    Carey, P.R.4    Anderson, V.E.5
  • 120
    • 0036637706 scopus 로고    scopus 로고
    • Secondary structural studies of bovine caseins: Structure and temperature dependence of beta-casein phosphopeptide (1-25) as analyzed by circular dichroism, FTIR spectroscopy, and analytical ultracentrifugation
    • Farrell, H.M. Jr.; Qi, P.X.; Wickham, E.D.; Unruh, J.J. Secondary structural studies of bovine caseins: structure and temperature dependence of beta-casein phosphopeptide (1-25) as analyzed by circular dichroism, FTIR spectroscopy, and analytical ultracentrifugation. J. Protein Chem., 2002, 21, 307-321.
    • (2002) J. Protein Chem. , vol.21 , pp. 307-321
    • Farrell, H.M.1    Qi, P.X.2    Wickham, E.D.3    Unruh, J.J.4
  • 121
    • 16644392534 scopus 로고    scopus 로고
    • Thermal and alkaline denaturation of bovine beta-casein
    • Qi, P.X.; Wickham, E.D.; Farrell, H.M. Jr. Thermal and alkaline denaturation of bovine beta-casein. Protein J., 2004, 23, 389-402.
    • (2004) Protein J. , vol.23 , pp. 389-402
    • Qi, P.X.1    Wickham, E.D.2    Farrell, H.M.3
  • 122
    • 84878243007 scopus 로고    scopus 로고
    • Consequential secondary structure alterations and aggregation during prolonged casein glycation
    • Jindal, S.; Naeem, A. Consequential secondary structure alterations and aggregation during prolonged casein glycation. J. Fluoresc., 2013, 23, 367-374.
    • (2013) J. Fluoresc. , vol.23 , pp. 367-374
    • Jindal, S.1    Naeem, A.2
  • 124
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V.N. Natively unfolded proteins: a point where biology waits for physics. Protein Sci., 2002, 11, 739-756.
    • (2002) Protein Sci. , vol.11 , pp. 739-756
    • Uversky, V.N.1
  • 125
    • 0036153571 scopus 로고    scopus 로고
    • What does it mean to be natively unfolded
    • Uversky, V.N. What does it mean to be natively unfolded? Eur. J. Biochem., 2002, 269, 2-12.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2-12
    • Uversky, V.N.1
  • 126
    • 0141861067 scopus 로고    scopus 로고
    • Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: Which way to go?
    • Uversky, V.N. Protein folding revisited. A polypeptide chain at the folding-misfolding-nonfolding cross-roads: which way to go? Cell Mol Life Sci., 2003, 60, 1852-1871.
    • (2003) Cell Mol Life Sci. , vol.60 , pp. 1852-1871
    • Uversky, V.N.1
  • 127
  • 128
    • 84878940937 scopus 로고    scopus 로고
    • A decade and a half of protein intrinsic disorder: Biology still waits for physics
    • Uversky, V.N. A decade and a half of protein intrinsic disorder: biology still waits for physics. Protein Sci., 2013, 22, 693-724.
    • (2013) Protein Sci. , vol.22 , pp. 693-724
    • Uversky, V.N.1
  • 129
    • 84876281768 scopus 로고    scopus 로고
    • Unusual biophysics of intrinsically disordered proteins
    • Uversky, V.N. Unusual biophysics of intrinsically disordered proteins. Biochim. Biophys. Acta, 2013, 1834, 932-951.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 932-951
    • Uversky, V.N.1
  • 130
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiologic conditions?
    • Uversky, V.N.; Gillespie, J.R.; Fink, A.L. Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins, 2000, 41, 415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 133
    • 34447539760 scopus 로고    scopus 로고
    • Composition Profiler: A tool for discovery and visualization of amino acid composition differences
    • Vacic, V.; Uversky, V.N.; Dunker, A.K.; Lonardi, S. Composition Profiler: a tool for discovery and visualization of amino acid composition differences. BMC Bioinformatics, 2007, 8, 211.
    • (2007) BMC Bioinformatics , vol.8 , pp. 211
    • Vacic, V.1    Uversky, V.N.2    Dunker, A.K.3    Lonardi, S.4
  • 137
    • 84879209673 scopus 로고    scopus 로고
    • Longitudinal analysis of protein glycosylation and betacasein phosphorylation in term and preterm human milk during the first 2 months of lactation
    • Molinari, C.E.; Casadio, Y.S.; Hartmann, B.T.; Arthur, P.G.; Hartmann, P.E. Longitudinal analysis of protein glycosylation and betacasein phosphorylation in term and preterm human milk during the first 2 months of lactation. Br. J. Nutr., 2013, 110, 105-115.
    • (2013) Br. J. Nutr. , vol.110 , pp. 105-115
    • Molinari, C.E.1    Casadio, Y.S.2    Hartmann, B.T.3    Arthur, P.G.4    Hartmann, P.E.5
  • 138
    • 0019400281 scopus 로고
    • Phosphorylation of caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinases
    • Mercier, J.C. Phosphorylation of caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinases. Biochimie, 1981, 63, 1-17.
    • (1981) Biochimie , vol.63 , pp. 1-17
    • Mercier, J.C.1
  • 139
    • 0014033514 scopus 로고
    • Casein biosynthesis: Evidence for phosphorylation of precursor proteins
    • Turkington, R.W.; Topper, Y.J. Casein biosynthesis: evidence for phosphorylation of precursor proteins. Biochim. Biophys. Acta, 1966, 127, 366-372.
    • (1966) Biochim. Biophys. Acta , vol.127 , pp. 366-372
    • Turkington, R.W.1    Topper, Y.J.2
  • 140
    • 0015517314 scopus 로고
    • Properties of dephosphorylated s1-casein. Precipitation by calcium ions and micelle formation
    • Bingham, E.W.; Farrell, H.M. Jr.; Carroll, R.J. Properties of dephosphorylated s1-casein. Precipitation by calcium ions and micelle formation. Biochemistry, 1972, 11, 2450-2454.
    • (1972) Biochemistry , vol.11 , pp. 2450-2454
    • Bingham, E.W.1    Farrell, H.M.2    Carroll, R.J.3
  • 142
    • 10244247716 scopus 로고    scopus 로고
    • Biopeptides of milk: Caseinophosphopeptides and mineral bioavailability
    • Bouhallab, S.; Bougle, D. Biopeptides of milk: caseinophosphopeptides and mineral bioavailability. Reprod. Nutr. Dev., 2004, 44, 493-498.
    • (2004) Reprod. Nutr. Dev. , vol.44 , pp. 493-498
    • Bouhallab, S.1    Bougle, D.2
  • 143
    • 84894250407 scopus 로고    scopus 로고
    • Structural and functional characteristics of bovine milk protein glycosylation
    • O'Riordan, N.; Kane, M.; Joshi, L.; Hickey, R.M. Structural and functional characteristics of bovine milk protein glycosylation. Glycobiology, 2014, 24, 220-236.
    • (2014) Glycobiology , vol.24 , pp. 220-236
    • O'riordan, N.1    Kane, M.2    Joshi, L.3    Hickey, R.M.4
  • 144
    • 84873638834 scopus 로고    scopus 로고
    • Chemical and functional properties of glycomacropeptide (GMP) and its role in the detection of cheese whey adulteration in milk: A review
    • Neelima J; Sharma, R.; Rajput, Y.S.; Mann, B. Chemical and functional properties of glycomacropeptide (GMP) and its role in the detection of cheese whey adulteration in milk: a review. Dairy Sci. Technol., 2013, 93, 21-43.
    • (2013) Dairy Sci. Technol. , vol.93 , pp. 21-43
    • Neelima, J.1    Sharma, R.2    Rajput, Y.S.3    Mann, B.4
  • 145
    • 4944261401 scopus 로고    scopus 로고
    • Free and total GMP (Glycomacropeptide) contents of milk during bovine lactation
    • Furlanetti, A.M.; Prata, L.F. Free and total GMP (glycomacropeptide) contents of milk during bovine lactation. Food Sci. Technol. (Campinas), 2003, 23, 121-125.
    • (2003) Food Sci. Technol. (Campinas) , vol.23 , pp. 121-125
    • Furlanetti, A.M.1    Prata, L.F.2    Total, G.3
  • 146
    • 16344385662 scopus 로고    scopus 로고
    • Analysis of Oglycosylation site occupancy in bovine kappa-casein glycoforms separated by two-dimensional gel electrophoresis
    • Holland, J.W.; Deeth, H.C.; Alewood, P.F. Analysis of Oglycosylation site occupancy in bovine kappa-casein glycoforms separated by two-dimensional gel electrophoresis. Proteomics, 2005, 5, 990-1002.
    • (2005) Proteomics , vol.5 , pp. 990-1002
    • Holland, J.W.1    Deeth, H.C.2    Alewood, P.F.3
  • 147
    • 33744457010 scopus 로고    scopus 로고
    • Resolution and characterisation of multiple isoforms of bovine kappa-casein by 2-DE following a reversible cysteine-tagging enrichment strategy
    • Holland, J.W.; Deeth, H.C.; Alewood, P.F. Resolution and characterisation of multiple isoforms of bovine kappa-casein by 2-DE following a reversible cysteine-tagging enrichment strategy. Proteomics, 2006, 6, 3087-3095.
    • (2006) Proteomics , vol.6 , pp. 3087-3095
    • Holland, J.W.1    Deeth, H.C.2    Alewood, P.F.3
  • 150
    • 84906854634 scopus 로고    scopus 로고
    • The structural and functional signatures of proteins that undergo multiple events of post-translational modification
    • Pejaver, V.; Hsu, W.L.; Xin, F.; Dunker, A.K.; Uversky, V.N.; Radivojac, P. The structural and functional signatures of proteins that undergo multiple events of post-translational modification. Protein Sci., 2014, 23, 1077-1093.
    • (2014) Protein Sci. , vol.23 , pp. 1077-1093
    • Pejaver, V.1    Hsu, W.L.2    Xin, F.3    Dunker, A.K.4    Uversky, V.N.5    Radivojac, P.6
  • 151
    • 63049110383 scopus 로고    scopus 로고
    • Role of calcium phosphate nanoclusters in the control of calcification
    • Holt, C.; Sorensen, E.S.; Clegg, R.A. Role of calcium phosphate nanoclusters in the control of calcification. FEBS J., 2009, 276, 2308-2323.
    • (2009) FEBS J. , vol.276 , pp. 2308-2323
    • Holt, C.1    Sorensen, E.S.2    Clegg, R.A.3
  • 154
    • 84857129811 scopus 로고    scopus 로고
    • Comprehensive comparative assessment of in-silico predictors of disordered regions
    • Peng, Z.L.; Kurgan, L. Comprehensive comparative assessment of in-silico predictors of disordered regions. Curr. Protein Pept. Sci., 2012, 13, 6-18.
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 6-18
    • Peng, Z.L.1    Kurgan, L.2
  • 155
    • 84893003756 scopus 로고    scopus 로고
    • Accurate prediction of disorder in protein chains with a comprehensive and empirically designed consensus
    • Fan, X.; Kurgan, L. Accurate prediction of disorder in protein chains with a comprehensive and empirically designed consensus. J. Biomol. Struct. Dyn., 2014, 32, 448-464.
    • (2014) J. Biomol. Struct. Dyn. , vol.32 , pp. 448-464
    • Fan, X.1    Kurgan, L.2
  • 158
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztanyi, Z.; Csizmok, V.; Tompa, P.; Simon, I. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics, 2005, 21, 3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 160
    • 84865129593 scopus 로고    scopus 로고
    • MobiDB: A comprehensive database of intrinsic protein disorder annotations
    • Di Domenico, T.; Walsh, I.; Martin, A.J.; Tosatto, S.C. MobiDB: a comprehensive database of intrinsic protein disorder annotations. Bioinformatics, 2012, 28, 2080-2081.
    • (2012) Bioinformatics , vol.28 , pp. 2080-2081
    • Di Domenico, T.1    Walsh, I.2    Martin, A.J.3    Tosatto, S.C.4
  • 161
    • 84946098212 scopus 로고    scopus 로고
    • MobiDB 2.0: An improved database of intrinsically disordered and mobile proteins
    • Potenza, E.; Domenico, T.D.; Walsh, I.; Tosatto, S.C. MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins. Nucleic Acids Res., 2015.
    • (2015) Nucleic Acids Res.
    • Potenza, E.1    Domenico, T.D.2    Walsh, I.3    Tosatto, S.C.4
  • 162
  • 164
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • Linding, R.; Russell, R.B.; Neduva, V.; Gibson, T.J. GlobPlot: exploring protein sequences for globularity and disorder. Nucleic Acids Res., 2003, 31, 3701-3708.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 165
    • 30344485673 scopus 로고    scopus 로고
    • Exploiting heterogeneous sequence properties improves prediction of protein disorder
    • Obradovic, Z.; Peng, K.; Vucetic, S.; Radivojac, P.; Dunker, A.K. Exploiting heterogeneous sequence properties improves prediction of protein disorder. Proteins, 2005, 61(Suppl 7), 176-182.
    • (2005) Proteins , vol.61 , pp. 176-182
    • Obradovic, Z.1    Peng, K.2    Vucetic, S.3    Radivojac, P.4    Dunker, A.K.5
  • 167
    • 20744437001 scopus 로고    scopus 로고
    • RONN: The bio-basis function neural network technique applied to the detection of natively disordered regions in proteins
    • Yang, Z.R.; Thomson, R.; McNeil, P.; Esnouf, R.M. RONN: the bio-basis function neural network technique applied to the detection of natively disordered regions in proteins. Bioinformatics, 2005, 21, 3369-3376.
    • (2005) Bioinformatics , vol.21 , pp. 3369-3376
    • Yang, Z.R.1    Thomson, R.2    McNeil, P.3    Esnouf, R.M.4
  • 170
    • 67349162535 scopus 로고    scopus 로고
    • CDF it all: Consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions
    • Xue, B.; Oldfield, C.J.; Dunker, A.K.; Uversky, V.N. CDF it all: consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions. FEBS Lett., 2009, 583, 1469-1474.
    • (2009) FEBS Lett. , vol.583 , pp. 1469-1474
    • Xue, B.1    Oldfield, C.J.2    Dunker, A.K.3    Uversky, V.N.4
  • 171
    • 41049091705 scopus 로고    scopus 로고
    • Intrinsic disorder in pathogenic and non-pathogenic microbes: Discovering and analyzing the unfoldomes of earlybranching eukaryotes
    • Mohan, A.; Sullivan, W.J. Jr.; Radivojac, P.; Dunker, A.K.; Uversky, V.N. Intrinsic disorder in pathogenic and non-pathogenic microbes: discovering and analyzing the unfoldomes of earlybranching eukaryotes. Mol. Biosyst., 2008, 4, 328-340.
    • (2008) Mol. Biosyst. , vol.4 , pp. 328-340
    • Mohan, A.1    Sullivan, W.J.2    Radivojac, P.3    Dunker, A.K.4    Uversky, V.N.5
  • 173
    • 0036402827 scopus 로고    scopus 로고
    • Identification and functions of usefully disordered proteins
    • Dunker, A.K.; Brown, C.J.; Obradovic, Z. Identification and functions of usefully disordered proteins. Adv. Protein Chem., 2002, 62, 25-49.
    • (2002) Adv. Protein Chem. , vol.62 , pp. 25-49
    • Dunker, A.K.1    Brown, C.J.2    Obradovic, Z.3
  • 174
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. Intrinsically unstructured proteins. Trends Biochem. Sci., 2002, 27, 527-533.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 175
    • 24944511034 scopus 로고    scopus 로고
    • Handbook of Protein Folding, Buchner, J.; Kiefhaber, T. Editors. 2005, Wiley-VCH, Verlag GmbH & Co., Weinheim, Germany
    • Daughdrill, G.W.; Pielak, G.J.; Uversky, V.N.; Cortese, M.S.; Dunker, A.K. Natively disordered proteins, in Handbook of Protein Folding, Buchner, J.; Kiefhaber, T. Editors. 2005, Wiley-VCH, Verlag GmbH & Co.: Weinheim, Germany. p. 271-353.
    • Natively Disordered Proteins , pp. 271-353
    • Daughdrill, G.W.1    Pielak, G.J.2    Uversky, V.N.3    Cortese, M.S.4    Dunker, A.K.5
  • 176
    • 24944546549 scopus 로고    scopus 로고
    • Coupled folding and binding with alpha-helixforming molecular recognition elements
    • Oldfield, C.J.; Cheng, Y.; Cortese, M.S.; Romero, P.; Uversky, V.N.; Dunker, A.K. Coupled folding and binding with alpha-helixforming molecular recognition elements. Biochemistry, 2005, 44, 12454-12470.
    • (2005) Biochemistry , vol.44 , pp. 12454-12470
    • Oldfield, C.J.1    Cheng, Y.2    Cortese, M.S.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 177
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky, V.N.; Oldfield, C.J.; Dunker, A.K. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit., 2005, 18, 343-384.
    • (2005) J. Mol. Recognit. , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 179
    • 40949105259 scopus 로고    scopus 로고
    • Signal transduction via unstructured protein conduits
    • Dunker, A.K.; Uversky, V.N. Signal transduction via unstructured protein conduits. Nat. Chem. Biol., 2008, 4, 229-230.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 229-230
    • Dunker, A.K.1    Uversky, V.N.2
  • 180
    • 79951905332 scopus 로고    scopus 로고
    • Multitude of binding modes attainable by intrinsically disordered proteins: A portrait gallery of disorder-based complexes
    • Uversky, V.N. Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes. Chem. Soc. Rev., 2011, 40, 1623-1634.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 1623-1634
    • Uversky, V.N.1
  • 181
    • 84859712819 scopus 로고    scopus 로고
    • Disordered competitive recruiter: Fast and foldable
    • Uversky, V.N. Disordered competitive recruiter: fast and foldable. J. Mol. Biol., 2012, 418, 267-268.
    • (2012) J. Mol. Biol. , vol.418 , pp. 267-268
    • Uversky, V.N.1
  • 182
    • 84878627017 scopus 로고    scopus 로고
    • Intrinsic Disorder-based Protein Interactions and their Modulators
    • Uversky, V.N. Intrinsic Disorder-based Protein Interactions and their Modulators. Curr. Pharm. Des., 2013, 19, 4191-4213.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 4191-4213
    • Uversky, V.N.1
  • 183
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H.J.; Wright, P.E. Coupling of folding and binding for unstructured proteins. Curr. Opin. Struct. Biol., 2002, 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 184
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J.; Wright, P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol., 2005, 6, 197-208.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 185
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Reassessing the protein structure-function paradigm
    • Wright, P.E.; Dyson, H.J. Intrinsically unstructured proteins: reassessing the protein structure-function paradigm. J. Mol. Biol., 1999, 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 188
    • 36749037699 scopus 로고    scopus 로고
    • Mining alpha-helix-forming molecular recognition features with cross species sequence alignments
    • Cheng, Y.; Oldfield, C.J.; Meng, J.; Romero, P.; Uversky, V.N.; Dunker, A.K. Mining alpha-helix-forming molecular recognition features with cross species sequence alignments. Biochemistry, 2007, 46, 13468-13477.
    • (2007) Biochemistry , vol.46 , pp. 13468-13477
    • Cheng, Y.1    Oldfield, C.J.2    Meng, J.3    Romero, P.4    Uversky, V.N.5    Dunker, A.K.6
  • 189
    • 67049119327 scopus 로고    scopus 로고
    • Prediction of protein binding regions in disordered proteins
    • Meszaros, B.; Simon, I.; Dosztanyi, Z. Prediction of protein binding regions in disordered proteins. PLoS Comput. Biol., 2009, 5, e1000376.
    • (2009) Plos Comput. Biol. , pp. 5
    • Meszaros, B.1    Simon, I.2    Dosztanyi, Z.3
  • 190
    • 70349996473 scopus 로고    scopus 로고
    • ANCHOR: Web server for predicting protein binding regions in disordered proteins
    • Dosztanyi, Z.; Meszaros, B.; Simon, I. ANCHOR: web server for predicting protein binding regions in disordered proteins. Bioinformatics, 2009, 25, 2745-2746.
    • (2009) Bioinformatics , vol.25 , pp. 2745-2746
    • Dosztanyi, Z.1    Meszaros, B.2    Simon, I.3
  • 191
    • 14844342815 scopus 로고    scopus 로고
    • The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins
    • Dosztanyi, Z.; Csizmok, V.; Tompa, P.; Simon, I. The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. J. Mol. Biol., 2005, 347, 827-839.
    • (2005) J. Mol. Biol. , vol.347 , pp. 827-839
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 193
    • 1642512502 scopus 로고    scopus 로고
    • The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner
    • Bourhis, J.M.; Johansson, K.; Receveur-Brechot, V.; Oldfield, C.J.; Dunker, K.A.; Canard, B.; Longhi, S. The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner. Virus Res., 2004, 99, 157-167.
    • (2004) Virus Res. , vol.99 , pp. 157-167
    • Bourhis, J.M.1    Johansson, K.2    Receveur-Brechot, V.3    Oldfield, C.J.4    Dunker, K.A.5    Canard, B.6    Longhi, S.7
  • 196
    • 34547588389 scopus 로고    scopus 로고
    • PrDOS: Prediction of disordered protein regions from amino acid sequence
    • Ishida, T.; Kinoshita, K. PrDOS: prediction of disordered protein regions from amino acid sequence. Nucleic Acids Res., 2007, 35, W460-464.
    • (2007) Nucleic Acids Res. , vol.35 , pp. W460-W464
    • Ishida, T.1    Kinoshita, K.2
  • 200
    • 33645214608 scopus 로고    scopus 로고
    • Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks
    • Patil, A.; Nakamura, H. Disordered domains and high surface charge confer hubs with the ability to interact with multiple proteins in interaction networks. FEBS Lett., 2006, 580, 2041-2045.
    • (2006) FEBS Lett. , vol.580 , pp. 2041-2045
    • Patil, A.1    Nakamura, H.2
  • 202
    • 33745686603 scopus 로고    scopus 로고
    • What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae?
    • Ekman, D.; Light, S.; Bjorklund, A.K.; Elofsson, A. What properties characterize the hub proteins of the protein-protein interaction network of Saccharomyces cerevisiae? Genome Biol., 2006, 7, R45.
    • (2006) Genome Biol. , vol.7 , pp. R45
    • Ekman, D.1    Light, S.2    Bjorklund, A.K.3    Elofsson, A.4
  • 203
    • 33750999318 scopus 로고    scopus 로고
    • Disorder and sequence repeats in hub proteins and their implications for network evolution
    • Dosztanyi, Z.; Chen, J.; Dunker, A.K.; Simon, I.; Tompa, P. Disorder and sequence repeats in hub proteins and their implications for network evolution. J. Proteome Res., 2006, 5, 2985-2995.
    • (2006) J. Proteome Res. , vol.5 , pp. 2985-2995
    • Dosztanyi, Z.1    Chen, J.2    Dunker, A.K.3    Simon, I.4    Tompa, P.5
  • 204
    • 30144437939 scopus 로고    scopus 로고
    • Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes
    • Singh, G.P.; Ganapathi, M.; Sandhu, K.S.; Dash, D. Intrinsic unstructuredness and abundance of PEST motifs in eukaryotic proteomes. Proteins, 2006, 62, 309-315.
    • (2006) Proteins , vol.62 , pp. 309-315
    • Singh, G.P.1    Ganapathi, M.2    Sandhu, K.S.3    Dash, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.