메뉴 건너뛰기




Volumn , Issue , 2005, Pages 1-66

Hair structure, function, and physicochemical properties

Author keywords

[No Author keywords available]

Indexed keywords


EID: 80052627738     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (15)

References (302)
  • 1
    • 85056961451 scopus 로고    scopus 로고
    • www.tlhw.com.
  • 2
    • 27544506718 scopus 로고
    • Neue Erkenntnisse über der morphologischen Aufbau des menschlichen Haares
    • Randebrook RJ. Neue Erkenntnisse über der morphologischen Aufbau des menschlichen Haares. J Soc Cosmet Chem 1964; 15: 691-706.
    • (1964) J Soc Cosmet Chem , vol.15 , pp. 691-706
    • Randebrook, R.J.1
  • 3
    • 0007971397 scopus 로고
    • Differences between adult and children’s hair
    • Bogaty HJ. Differences between adult and children’s hair. J Soc Cosmet Chem 1969; 20: 159-171.
    • (1969) J Soc Cosmet Chem , vol.20 , pp. 159-171
    • Bogaty, H.J.1
  • 4
    • 0016503587 scopus 로고
    • Racial and other genetic variations in hair form
    • Rook A. Racial and other genetic variations in hair form. Brit J Dermat 1975; 92: 599-600.
    • (1975) Brit J Dermat , vol.92 , pp. 599-600
    • Rook, A.1
  • 5
    • 0021125271 scopus 로고
    • Variation in hair histological variables: Medulla and diameter
    • Das-Chaudhuri AB, Chopra VP. Variation in hair histological variables: medulla and diameter. Hum Hered 1984; 34: 217-221.
    • (1984) Hum Hered , vol.34 , pp. 217-221
    • Das-Chaudhuri, A.B.1    Chopra, V.P.2
  • 6
    • 0015908619 scopus 로고
    • Quantitative hair form variation in seven populations
    • Hrdy D. Quantitative hair form variation in seven populations. Am J Phys Anthrop 1973; 39: 7-18.
    • (1973) Am J Phys Anthrop , vol.39 , pp. 7-18
    • Hrdy, D.1
  • 7
    • 0038626426 scopus 로고
    • Caucasian hair, Negro hair and wool: Similarities and differences
    • Menkart J, Wolfram LJ, Mao I. Caucasian hair, Negro hair and wool: similarities and differences. J Soc Cosmet Chem 1966; 17: 769-787.
    • (1966) J Soc Cosmet Chem , vol.17 , pp. 769-787
    • Menkart, J.1    Wolfram, L.J.2    Mao, I.3
  • 9
    • 85047691602 scopus 로고
    • Human hair form-morphology revealed by light and scanning electron microscopy and computer aided threedimensional reconstruction
    • Lindelöf B, Forslind B, Hedblad MA, Kaveus U. Human hair form-morphology revealed by light and scanning electron microscopy and computer aided threedimensional reconstruction. Arch Dermatol 1988; 124: 1359-1363.
    • (1988) Arch Dermatol , vol.124 , pp. 1359-1363
    • Lindelöf, B.1    Forslind, B.2    Hedblad, M.A.3    Kaveus, U.4
  • 12
    • 0030636219 scopus 로고    scopus 로고
    • Morphology and histochemistry of human hair
    • Jolles P, Zahn H, Höcker H, eds, Basel: Birkhauser Verlag
    • Swift JA. Morphology and histochemistry of human hair. In: Jolles P, Zahn H, Höcker H, eds. Formation and Structure of Human Hair. Basel: Birkhauser Verlag, 1997: 149-175.
    • (1997) Formation and Structure of Human Hair , pp. 149-175
    • Swift, J.A.1
  • 13
    • 0038792629 scopus 로고    scopus 로고
    • Hair shape of curly hair
    • Bernard BA. Hair shape of curly hair. J Am Acad Dermatol 2003; 48/6S: 120S-126S.
    • (2003) J Am Acad Dermatol , vol.48 , Issue.6S , pp. 120S-126S
    • Bernard, B.A.1
  • 14
    • 76549151796 scopus 로고
    • Hair medulla variation with age in human males
    • Luell E, Archer VE. Hair medulla variation with age in human males. Am J Phys Anthrop 1992; 22: 107-110.
    • (1992) Am J Phys Anthrop , vol.22 , pp. 107-110
    • Luell, E.1    Archer, V.E.2
  • 15
    • 0002391121 scopus 로고    scopus 로고
    • Human hair cuticle: Biologically conspired to the owner’s advantage
    • Swift JA. Human hair cuticle: biologically conspired to the owner’s advantage. J Cosmet Sci 1999; 50: 23-47.
    • (1999) J Cosmet Sci , vol.50 , pp. 23-47
    • Swift, J.A.1
  • 16
    • 0027454811 scopus 로고
    • The modification of the surface diffusion barrier of wool
    • Negri AP, Cornell HJ, Rivett DE. The modification of the surface diffusion barrier of wool. J Soc Dyers Col 1993; 109: 296-300.
    • (1993) J Soc Dyers Col , vol.109 , pp. 296-300
    • Negri, A.P.1    Cornell, H.J.2    Rivett, D.E.3
  • 17
    • 0009500108 scopus 로고    scopus 로고
    • The cuticle controls bending stiffness of hair
    • Swift JA. The cuticle controls bending stiffness of hair. J Cosmet Sci 2000; 51: 37-38.
    • (2000) J Cosmet Sci , vol.51 , pp. 37-38
    • Swift, J.A.1
  • 18
    • 0027542578 scopus 로고
    • A model for the surface of keratin fibers
    • Negri AP, Cornell HJ, Rivett DE. A model for the surface of keratin fibers. Text Res J 1993; 63: 109-115.
    • (1993) Text Res J , vol.63 , pp. 109-115
    • Negri, A.P.1    Cornell, H.J.2    Rivett, D.E.3
  • 19
    • 0002978717 scopus 로고
    • The properties of wool and a new chemical method for detecting damaged wool
    • Allworden KZ. The properties of wool and a new chemical method for detecting damaged wool. Angew Chem 1916; 29: 77-78.
    • (1916) Angew Chem , vol.29 , pp. 77-78
    • Allworden, K.Z.1
  • 20
    • 0002113751 scopus 로고
    • The cell membrane complex and its influence on the properties of the wool fibre
    • Leeder JD. The cell membrane complex and its influence on the properties of the wool fibre. Wool Sci Rev 1986; 63: 3-35.
    • (1986) Wool Sci Rev , vol.63 , pp. 3-35
    • Leeder, J.D.1
  • 21
    • 0026710233 scopus 로고
    • A comparative study of covalently-bound fatty acids in keratinized tissues
    • Peet DJ, Wettenhall EH, Rivett DE, Allen AK. A comparative study of covalently-bound fatty acids in keratinized tissues. Comp Biochem Physiol 1992; 102B: 363-366.
    • (1992) Comp Biochem Physiol , vol.102B , pp. 363-366
    • Peet, D.J.1    Wettenhall, E.H.2    Rivett, D.E.3    Allen, A.K.4
  • 22
    • 0031423604 scopus 로고    scopus 로고
    • The role of 18-methyleicosanoic acid in the structure and formation of mammalian hair fibres
    • Jones LN, Rivett DE. The role of 18-methyleicosanoic acid in the structure and formation of mammalian hair fibres. Micron 1997; 28: 469-485.
    • (1997) Micron , vol.28 , pp. 469-485
    • Jones, L.N.1    Rivett, D.E.2
  • 23
    • 84965534110 scopus 로고
    • Covalently linked fatty acids at the surface of wool: Part of the cuticle cell envelope
    • Zahn H, Messinger H, Höcker H. Covalently linked fatty acids at the surface of wool: part of the cuticle cell envelope. Text Res J 1994; 64: 554-555.
    • (1994) Text Res J , vol.64 , pp. 554-555
    • Zahn, H.1    Messinger, H.2    Höcker, H.3
  • 25
    • 84965911485 scopus 로고
    • Degradation of human hair by papain
    • Swift JA, Holmes AW. Degradation of human hair by papain. Text Res J 1965; 35: 1014-1019.
    • (1965) Text Res J , vol.35 , pp. 1014-1019
    • Swift, J.A.1    Holmes, A.W.2
  • 26
    • 0003371293 scopus 로고
    • The chemistry of human hair cuticle, part III: The isolation and amino acid analysis of various subfractions of the cuticle obtained by pronase and trypsin digestion
    • Swift JA, Bews BJ. The chemistry of human hair cuticle, part III: the isolation and amino acid analysis of various subfractions of the cuticle obtained by pronase and trypsin digestion. J Soc Cosmet Chem 1976; 27: 289-300.
    • (1976) J Soc Cosmet Chem , vol.27 , pp. 289-300
    • Swift, J.A.1    Bews, B.J.2
  • 27
    • 0030636267 scopus 로고    scopus 로고
    • The role of keratin proteins and their genes in the growth, structure and properties of hair
    • Jolles P, Zahn H, Höcker H, eds, Basel: Birkhauser Verlag
    • Powell B, Rogers GE. The role of keratin proteins and their genes in the growth, structure and properties of hair. In: Jolles P, Zahn H, Höcker H, eds. Formation and Structure of Human Hair. Basel: Birkhauser Verlag, 1997: 59-148.
    • (1997) Formation and Structure of Human Hair , pp. 59-148
    • Powell, B.1    Rogers, G.E.2
  • 29
    • 0035459476 scopus 로고    scopus 로고
    • Elucidating penetration pathways into the hair fiber using novel microscopic techniques
    • Gummer CL. Elucidating penetration pathways into the hair fiber using novel microscopic techniques. J Cosmet Sci 2001; 52: 265-280.
    • (2001) J Cosmet Sci , vol.52 , pp. 265-280
    • Gummer, C.L.1
  • 30
    • 85016006962 scopus 로고    scopus 로고
    • Ultrastructure and micromechanical properties of vertebrate keratin fibers: Multimodal atomic force microscope imaging
    • Parbhu AN, Almqvist N, Bryson WG, Lal R. Ultrastructure and micromechanical properties of vertebrate keratin fibers: multimodal atomic force microscope imaging. Mol Biol Cell 1998; 9: 105A.
    • (1998) Mol Biol Cell , vol.9 , pp. 105
    • Parbhu, A.N.1    Almqvist, N.2    Bryson, W.G.3    Lal, R.4
  • 31
    • 0033533380 scopus 로고    scopus 로고
    • Disulfide bonds in the outer layer of keratin fibers confer higher mechanical rigidity: Correlative nano-indentation and elasticity measurement with an AFM
    • Parbhu AN, Bryson WG, Lal R. Disulfide bonds in the outer layer of keratin fibers confer higher mechanical rigidity: correlative nano-indentation and elasticity measurement with an AFM. Biochem 1999; 38: 11755-11761.
    • (1999) Biochem , vol.38 , pp. 11755-11761
    • Parbhu, A.N.1    Bryson, W.G.2    Lal, R.3
  • 32
    • 0029102924 scopus 로고
    • Atomic force microscopy of human hair cuticles: A microscopic study of environmental effects on hair morphology
    • O’Connor SD, Komisarek KD, Baldeschwieler JD. Atomic force microscopy of human hair cuticles: a microscopic study of environmental effects on hair morphology. J Invest Dermatol 1995; 105: 96-99.
    • (1995) J Invest Dermatol , vol.105 , pp. 96-99
    • O’Connor, S.D.1    Komisarek, K.D.2    Baldeschwieler, J.D.3
  • 34
    • 84964140873 scopus 로고
    • The heterogeneity of the keratin fibers
    • Mercer EH. The heterogeneity of the keratin fibers. Text Res J 1953; 23: 388-397.
    • (1953) Text Res J , vol.23 , pp. 388-397
    • Mercer, E.H.1
  • 35
    • 0000846873 scopus 로고
    • Composition of the cortex of sound and tender wools
    • Orwin DFG, Woods JL. Composition of the cortex of sound and tender wools. J Text Inst 1980; 71: 315-317.
    • (1980) J Text Inst , vol.71 , pp. 315-317
    • Orwin, D.F.G.1    Woods, J.L.2
  • 36
    • 0002725345 scopus 로고
    • Morphology and fine structure of hair
    • Orfanos C, Montagna W, Stuttgen G, eds, Berlin: Springer-Verlag
    • Kassenbeck P. Morphology and fine structure of hair. In: Orfanos C, Montagna W, Stuttgen G, eds. Hair Research. Berlin: Springer-Verlag, 1981: 52-63.
    • (1981) Hair Research , pp. 52-63
    • Kassenbeck, P.1
  • 37
    • 0036744353 scopus 로고    scopus 로고
    • The high sulphur proteins of wool: Towards an understanding of sheep breed diversity
    • Flanagan LM, Plowman JE, Bryson WG. The high sulphur proteins of wool: towards an understanding of sheep breed diversity. Proteomics 2002; 2: 1240-1246.
    • (2002) Proteomics , vol.2 , pp. 1240-1246
    • Flanagan, L.M.1    Plowman, J.E.2    Bryson, W.G.3
  • 41
    • 0032407581 scopus 로고    scopus 로고
    • Organization of microfibrils in keratin fibers studied by X-ray scattering modelling using the paracrystal concept
    • Briki F, Busson B, Doucet J. Organization of microfibrils in keratin fibers studied by X-ray scattering modelling using the paracrystal concept. Biochim Biophys Acta 1998; 1429: 57-68.
    • (1998) Biochim Biophys Acta , vol.1429 , pp. 57-68
    • Briki, F.1    Busson, B.2    Doucet, J.3
  • 42
    • 0017977093 scopus 로고
    • An electron microscope study of fibril: Matrix arrangements in high- and low-crimp wool fibres
    • Kaplin IJ, Whiteley KJ. An electron microscope study of fibril: matrix arrangements in high- and low-crimp wool fibres. Aust J Biol Sci 1978; 31: 231-240.
    • (1978) Aust J Biol Sci , vol.31 , pp. 231-240
    • Kaplin, I.J.1    Whiteley, K.J.2
  • 43
    • 84894463726 scopus 로고
    • The structure of keratin macrofibrils, part I: Keratins of high sulphur content
    • Tokyo
    • Kaplin LJ, Whiteley KJ. The structure of keratin macrofibrils, part I: keratins of high sulphur content. Proc 7th Int Wool Text Res Conf I, Tokyo 1985; 95-104.
    • (1985) Proc 7th Int Wool Text Res Conf I , pp. 95-104
    • Kaplin, L.J.1    Whiteley, K.J.2
  • 45
    • 2342556719 scopus 로고
    • Some problems in the X-ray analysis of the structure of animal hairs and other protein fibres
    • Astbury WT. Some problems in the X-ray analysis of the structure of animal hairs and other protein fibres. Trans Faraday Soc 1933; 29: 193-211.
    • (1933) Trans Faraday Soc , vol.29 , pp. 193-211
    • Astbury, W.T.1
  • 47
    • 76549252207 scopus 로고
    • The structure of proteins: Two hydrogen-bonded helical configurations of the polypeptide chain
    • Pauling L, Corey RB, Branson HR. The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain. Proc Natl Acad Sci 1951; 37: 205-211.
    • (1951) Proc Natl Acad Sci , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 48
    • 0032772539 scopus 로고    scopus 로고
    • Side-chains configurations in coiled coils reveled by the 5.15A meridional reflection on hard alpha-keratin X-ray diffraction patterns
    • Busson B, Briki F, Doucet J. Side-chains configurations in coiled coils reveled by the 5.15A meridional reflection on hard alpha-keratin X-ray diffraction patterns. J Struct Biol 1999; 125: 1-10.
    • (1999) J Struct Biol , vol.125 , pp. 1-10
    • Busson, B.1    Briki, F.2    Doucet, J.3
  • 49
    • 0032853296 scopus 로고    scopus 로고
    • Modeling alpha-helical coiled coils: Analytic relations between parameters
    • Busson B, Doucet J. Modeling alpha-helical coiled coils: analytic relations between parameters. J Struct Biol 1999; 127: 16-21.
    • (1999) J Struct Biol , vol.127 , pp. 16-21
    • Busson, B.1    Doucet, J.2
  • 50
    • 0000920828 scopus 로고
    • The packing of alpha-helices: Simple coiled-coil
    • Crick FHC. The packing of alpha-helices: simple coiled-coil. Acta Cryst 1953; 6: 689-697.
    • (1953) Acta Cryst , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 52
    • 0018085943 scopus 로고
    • Suberimidate crosslinking shows that a rod-shaped, low cystine, high helix protein prepared by limited proteolysis of reduced wool has four protein chains
    • Ahmadi B, Speakman PT. Suberimidate crosslinking shows that a rod-shaped, low cystine, high helix protein prepared by limited proteolysis of reduced wool has four protein chains. FEBS Lett 1978; 94: 365-367.
    • (1978) FEBS Lett , vol.94 , pp. 365-367
    • Ahmadi, B.1    Speakman, P.T.2
  • 53
    • 0027160195 scopus 로고
    • Keratin intermediate filament structure: Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly
    • Steinert PM, Markov L, Fraser RDB, Parry DAD. Keratin intermediate filament structure: crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly. J Mol Biol 1993; 230: 436-452.
    • (1993) J Mol Biol , vol.230 , pp. 436-452
    • Steinert, P.M.1    Markov, L.2    Fraser, R.D.B.3    Parry, D.A.D.4
  • 54
    • 0017200485 scopus 로고
    • Structure of the alpha- keratin microfibril
    • Fraser RDB, MacRae TP, Suzuki E. Structure of the alpha- keratin microfibril. J Mol Biol 1976; 108: 435-452.
    • (1976) J Mol Biol , vol.108 , pp. 435-452
    • Fraser, R.D.B.1    MacRae, T.P.2    Suzuki, E.3
  • 55
    • 0020776621 scopus 로고
    • The structure of the alpha-keratin microfibril
    • Fraser RDB, MacRae TP. The structure of the alpha-keratin microfibril. Biosci Rep 1983; 3: 517-525.
    • (1983) Biosci Rep , vol.3 , pp. 517-525
    • Fraser, R.D.B.1    MacRae, T.P.2
  • 56
    • 0021931209 scopus 로고
    • Intermediate filament structure
    • Fraser RDB, MacRae TP. Intermediate filament structure. Biosci Rep 1985; 5: 573-579.
    • (1985) Biosci Rep , vol.5 , pp. 573-579
    • Fraser, R.D.B.1    MacRae, T.P.2
  • 58
    • 0029902659 scopus 로고    scopus 로고
    • Hard alpha-keratin intermediate filaments: An alternative interpretation of the low-angle equatorial X-ray diffraction pattern, and the axial disposition of putative disulphide bonds in the intra- and inter-protofilamentous networks
    • Parry DAD. Hard alpha-keratin intermediate filaments: an alternative interpretation of the low-angle equatorial X-ray diffraction pattern, and the axial disposition of putative disulphide bonds in the intra- and inter-protofilamentous networks. Int J Biol Macromol 1996; 19: 45-50.
    • (1996) Int J Biol Macromol , vol.19 , pp. 45-50
    • Parry, D.A.D.1
  • 59
    • 0035914358 scopus 로고    scopus 로고
    • Subfilamentous protofibril structures in fibrous proteins
    • Parry DAD, Marekov LN, Steinert PM. Subfilamentous protofibril structures in fibrous proteins. J Biol Chem 2001; 276: 39253-39258.
    • (2001) J Biol Chem , vol.276 , pp. 39253-39258
    • Parry, D.A.D.1    Marekov, L.N.2    Steinert, P.M.3
  • 63
    • 84970608630 scopus 로고
    • The isolation and properties of some soluble proteins from wool, part IX: The proteins in wools of increased sulphur content
    • Gillespie JM. The isolation and properties of some soluble proteins from wool, part IX: The proteins in wools of increased sulphur content. Aust J Biol Sci 1964; 17: 548-560.
    • (1964) Aust J Biol Sci , vol.17 , pp. 548-560
    • Gillespie, J.M.1
  • 64
    • 0028410921 scopus 로고
    • A model for the mechanical properties of the alpha-keratin cortex
    • Feughelman M. A model for the mechanical properties of the alpha-keratin cortex. Text Res J 1994; 64: 236-239.
    • (1994) Text Res J , vol.64 , pp. 236-239
    • Feughelman, M.1
  • 65
    • 0018637473 scopus 로고
    • Repeating patterns of amino acid residues in the sequences of some high sulphur proteins from alpha-keratin
    • Parry DAD, Fraser RTB, MacRae TP. Repeating patterns of amino acid residues in the sequences of some high sulphur proteins from alpha-keratin. Int J Biol Macromol 1979; 1: 17-22.
    • (1979) Int J Biol Macromol , vol.1 , pp. 17-22
    • Parry, D.A.D.1    Fraser, R.T.B.2    MacRae, T.P.3
  • 66
    • 0026807962 scopus 로고
    • Diffusion of dyes in natural fibres
    • Brady PR. Diffusion of dyes in natural fibres. Rev Prog Coloration 1992; 22: 58-78.
    • (1992) Rev Prog Coloration , vol.22 , pp. 58-78
    • Brady, P.R.1
  • 68
    • 0015775881 scopus 로고
    • The structure and chemistry of keratin fibers
    • Bradbury JH. The structure and chemistry of keratin fibers. Adv Prot Chem 1973; 27: 111-211.
    • (1973) Adv Prot Chem , vol.27 , pp. 111-211
    • Bradbury, J.H.1
  • 69
    • 2342612556 scopus 로고
    • The contribution of the resistant cell membranes to the properties of keratinized tissues
    • Mercer EH. The contribution of the resistant cell membranes to the properties of keratinized tissues. J Soc Cosmet Chem 1965; 16: 507-514.
    • (1965) J Soc Cosmet Chem , vol.16 , pp. 507-514
    • Mercer, E.H.1
  • 71
    • 77049150915 scopus 로고
    • The analysis of hair keratin I. Application of microbiological techniques to hydrolysates of human hair
    • Lang J, Lucas C. The analysis of hair keratin I. Application of microbiological techniques to hydrolysates of human hair. Biochem J 1952; 52: 84-87.
    • (1952) Biochem J , vol.52 , pp. 84-87
    • Lang, J.1    Lucas, C.2
  • 72
    • 0344503757 scopus 로고
    • Amino acid composition of human hair
    • Robbins CR, Kelly CH. Amino acid composition of human hair. Text Res J 1970; 40: 891-896.
    • (1970) Text Res J , vol.40 , pp. 891-896
    • Robbins, C.R.1    Kelly, C.H.2
  • 73
    • 0029136789 scopus 로고
    • Applying principal components analysis to the amino acid composition of keratin materials
    • Wortmann FJ, Wortmann G, Zahn H. Applying principal components analysis to the amino acid composition of keratin materials. Text Res J 1995; 65: 669-675.
    • (1995) Text Res J , vol.65 , pp. 669-675
    • Wortmann, F.J.1    Wortmann, G.2    Zahn, H.3
  • 74
    • 50449141761 scopus 로고
    • Preparation of an electrophoretically homogenous keratin derivative from wool
    • Gillespie JM, Lennox FG. Preparation of an electrophoretically homogenous keratin derivative from wool. Biochim Biophys Acta 1953; 12: 481-482.
    • (1953) Biochim Biophys Acta , vol.12 , pp. 481-482
    • Gillespie, J.M.1    Lennox, F.G.2
  • 75
    • 5344259399 scopus 로고
    • Structure of wool fibres: Isolation of an alpha and beta protein in wool
    • Alexander P, Earland C. Structure of wool fibres: isolation of an alpha and beta protein in wool. Nature 1950; 166: 396-397.
    • (1950) Nature , vol.166 , pp. 396-397
    • Alexander, P.1    Earland, C.2
  • 76
    • 70350179268 scopus 로고
    • Non-covalent bonding in keratins: The effect of esterification and acylation on the properties of wool
    • Wolfram LJ, Milligan B. Non-covalent bonding in keratins: the effect of esterification and acylation on the properties of wool. Proc 5th Int Wool Text Res Conf (Aachen) III 1975; 242-252.
    • (1975) Proc 5th Int Wool Text Res Conf (Aachen) , vol.3 , pp. 242-252
    • Wolfram, L.J.1    Milligan, B.2
  • 77
    • 0003898444 scopus 로고
    • Montagna W, Lobitz WC, eds, Lake Arrolohead: Academic Press
    • Rogers GE. In: Montagna W, Lobitz WC, eds. The Epidermis. Lake Arrolohead: Academic Press, 1964.
    • (1964) The Epidermis
    • Rogers, G.E.1
  • 78
    • 11144324103 scopus 로고
    • Separation of chemically unmodified histological components of keratin fibres and analysis of cuticles
    • Bradbury JH, Chapman GV, Hambly AN, King NLR. Separation of chemically unmodified histological components of keratin fibres and analysis of cuticles. Nature 1966; 210: 1333-1334.
    • (1966) Nature , vol.210 , pp. 1333-1334
    • Bradbury, J.H.1    Chapman, G.V.2    Hambly, A.N.3    King, N.L.R.4
  • 79
    • 0018320296 scopus 로고
    • Minimum depth electron probe X-ray microanalysis as a means for determining the sulphur content of the human hair surface
    • Swift JA. Minimum depth electron probe X-ray microanalysis as a means for determining the sulphur content of the human hair surface. Scanning 1979; 2: 83-88.
    • (1979) Scanning , vol.2 , pp. 83-88
    • Swift, J.A.1
  • 80
    • 0000262018 scopus 로고
    • The dependence of the conformations of synthetic polypeptides on amino acid composition
    • Blout ER. The dependence of the conformations of synthetic polypeptides on amino acid composition. J Am Chem Soc 1960; 82: 3787-3789.
    • (1960) J Am Chem Soc , vol.82 , pp. 3787-3789
    • Blout, E.R.1
  • 81
    • 0025678972 scopus 로고
    • Structure and expression of genes for a class of cysteine-rich proteins of the cuticle layers of differentiating wool and hair follicles
    • Mackinnon PJ, Powell BC, Rogers GE. Structure and expression of genes for a class of cysteine-rich proteins of the cuticle layers of differentiating wool and hair follicles. J Cell Biol 1990; 111: 2587-2600.
    • (1990) J Cell Biol , vol.111 , pp. 2587-2600
    • Mackinnon, P.J.1    Powell, B.C.2    Rogers, G.E.3
  • 82
    • 0028080223 scopus 로고
    • Differential expression of genes encoding a cysteine-rich keratin family in the hair cuticle
    • Jenkins BJ, Powell BC. Differential expression of genes encoding a cysteine-rich keratin family in the hair cuticle. J Invest Dermatol 1994; 103: 310-317.
    • (1994) J Invest Dermatol , vol.103 , pp. 310-317
    • Jenkins, B.J.1    Powell, B.C.2
  • 83
    • 2242419081 scopus 로고    scopus 로고
    • Characterization of a first domain of human high glycine-tyrosine and high sulfur keratin-associated protein (KAP) genes on chromosome 21q22.1
    • Rogers MA, Langbein L, Winter H, Ehmann C, Praetzel S, Schweizer J. Characterization of a first domain of human high glycine-tyrosine and high sulfur keratin-associated protein (KAP) genes on chromosome 21q22.1. J Biol Chem 2002; 277: 48993-49002.
    • (2002) J Biol Chem , vol.277 , pp. 48993-49002
    • Rogers, M.A.1    Langbein, L.2    Winter, H.3    Ehmann, C.4    Praetzel, S.5    Schweizer, J.6
  • 85
    • 0035860762 scopus 로고    scopus 로고
    • The catalog of human hair keratins. II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and II keratins
    • Langbein L, Rogers MA, Winter H, Praetzel S, Schweizer J. The catalog of human hair keratins. II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and II keratins. J Biol Chem 2001; 276: 35123-35132.
    • (2001) J Biol Chem , vol.276 , pp. 35123-35132
    • Langbein, L.1    Rogers, M.A.2    Winter, H.3    Praetzel, S.4    Schweizer, J.5
  • 86
    • 0001675158 scopus 로고
    • The chemistry of human hair cuticle, part II: The isolation and amino acid analysis of the cell membranes and A-layer
    • Swift JA, Bews B. The chemistry of human hair cuticle, part II: the isolation and amino acid analysis of the cell membranes and A-layer. J Soc Cosmet Chem 1974; 25: 355-366.
    • (1974) J Soc Cosmet Chem , vol.25 , pp. 355-366
    • Swift, J.A.1    Bews, B.2
  • 87
    • 0025756640 scopus 로고
    • The presence of glycoproteins in the cell membrane complex of a variety of keratin fibres
    • Allen AK, Ellis J, Rivett DE. The presence of glycoproteins in the cell membrane complex of a variety of keratin fibres. Biochim Biophys Acta 1991; 1074: 331-333.
    • (1991) Biochim Biophys Acta , vol.1074 , pp. 331-333
    • Allen, A.K.1    Ellis, J.2    Rivett, D.E.3
  • 88
    • 0025246752 scopus 로고
    • Amounts of fibrous proteins and matrix substances in hairs of different races
    • Dekio S, Jidoi J. Amounts of fibrous proteins and matrix substances in hairs of different races. J Dermatol 1990; 17: 62-64.
    • (1990) J Dermatol , vol.17 , pp. 62-64
    • Dekio, S.1    Jidoi, J.2
  • 89
    • 0020082850 scopus 로고
    • Related amino acid sequences in neurofilaments and non-neural intermediate filaments
    • Geisler N, Plessman U, Weber K. Related amino acid sequences in neurofilaments and non-neural intermediate filaments. Nature 1982; 296: 448-450.
    • (1982) Nature , vol.296 , pp. 448-450
    • Geisler, N.1    Plessman, U.2    Weber, K.3
  • 90
    • 0020536539 scopus 로고
    • Structural homology between hard alphakeratin and the intermediate filament proteins desmin and vimentin
    • Dowling LM, Parry DAD, Sparrow LG. Structural homology between hard alphakeratin and the intermediate filament proteins desmin and vimentin. Biosci Rep 1983; 3: 73-78.
    • (1983) Biosci Rep , vol.3 , pp. 73-78
    • Dowling, L.M.1    Parry, D.A.D.2    Sparrow, L.G.3
  • 91
    • 0020614212 scopus 로고
    • The cDNA sequence of a Type II cytoskeletal keratin reveals constant and variable structural domains among keratins
    • Hanukoglu I, Fuchs E. The cDNA sequence of a Type II cytoskeletal keratin reveals constant and variable structural domains among keratins. Cell 1983; 33: 915-924.
    • (1983) Cell , vol.33 , pp. 915-924
    • Hanukoglu, I.1    Fuchs, E.2
  • 92
    • 33749357063 scopus 로고
    • Intermediate filament structure: 3. Analysis of sequence homologies
    • Conway JF, Parry DAD. Intermediate filament structure: 3. Analysis of sequence homologies. Int J Biol Macromol 1988; 10: 79-98.
    • (1988) Int J Biol Macromol , vol.10 , pp. 79-98
    • Conway, J.F.1    Parry, D.A.D.2
  • 94
    • 0031657562 scopus 로고    scopus 로고
    • Hard alpha-keratin intermediate filament chains: Substructure of the N- and C-terminal domains and the predicted structure and function of the C-terminal domains of type I and type II chains
    • Parry DAD, North ACT. Hard alpha-keratin intermediate filament chains: substructure of the N- and C-terminal domains and the predicted structure and function of the C-terminal domains of type I and type II chains. J Struc Biol 1998; 122: 67-75.
    • (1998) J Struc Biol , vol.122 , pp. 67-75
    • Parry, D.A.D.1    North, A.C.T.2
  • 95
    • 0024209619 scopus 로고    scopus 로고
    • Hair low-sulfur protein composition does not differ electrophoretically among different races
    • Dekio S, Jidoi J. Hair low-sulfur protein composition does not differ electrophoretically among different races. J Dermatol 1998; 15: 393-396.
    • (1998) J Dermatol , vol.15 , pp. 393-396
    • Dekio, S.1    Jidoi, J.2
  • 96
    • 0035380463 scopus 로고    scopus 로고
    • Characterization of a cluster of human high/ultrahigh sulfur keratin-associated protein genes embedded in the type I keratin gene domain on chromosome 17q12-21
    • Rogers MA, Langbein L, Winter H, Ehmann C, Praetzel S, Korn B, Schweizer J. Characterization of a cluster of human high/ultrahigh sulfur keratin-associated protein genes embedded in the type I keratin gene domain on chromosome 17q12-21. J Biol Chem 2001; 276: 19440-19451.
    • (2001) J Biol Chem , vol.276 , pp. 19440-19451
    • Rogers, M.A.1    Langbein, L.2    Winter, H.3    Ehmann, C.4    Praetzel, S.5    Korn, B.6    Schweizer, J.7
  • 97
    • 0036175002 scopus 로고    scopus 로고
    • Ito M. hKAP1.6 hKAP1.7, two novel human high sulfur keratin-associated proteins are expressed in the hair follicle cortex
    • Shimomura Y, Aoki N, Rogers MA, Langbein L, Schweizer J. Ito M. hKAP1.6 hKAP1.7, two novel human high sulfur keratin-associated proteins are expressed in the hair follicle cortex. J Invest Dermatol 2002; 118: 226-231.
    • (2002) J Invest Dermatol , vol.118 , pp. 226-231
    • Shimomura, Y.1    Aoki, N.2    Rogers, M.A.3    Langbein, L.4    Schweizer, J.5
  • 99
    • 0034081365 scopus 로고    scopus 로고
    • Application of proteomics for determining protein markers for wool quality traits
    • Plowman JE, Bryson WG, Jordan TW. Application of proteomics for determining protein markers for wool quality traits. Electrophoresis 2000; 21: 1899-1906.
    • (2000) Electrophoresis , vol.21 , pp. 1899-1906
    • Plowman, J.E.1    Bryson, W.G.2    Jordan, T.W.3
  • 100
    • 0037160101 scopus 로고    scopus 로고
    • Polymorphisms in the human high sulfur hair keratin-associated protein 1, KAP1, gene family
    • Shimomura Y, Aoki N, Schweizer J, Langbein L, Rogers MA, Winter H, Ito M. Polymorphisms in the human high sulfur hair keratin-associated protein 1, KAP1, gene family. J Biol Chem 2002; 277: 45493-45501.
    • (2002) J Biol Chem , vol.277 , pp. 45493-45501
    • Shimomura, Y.1    Aoki, N.2    Schweizer, J.3    Langbein, L.4    Rogers, M.A.5    Winter, H.6    Ito, M.7
  • 101
    • 0000907653 scopus 로고
    • Hair lipids-the extraction of fatty materials from hair clippings
    • Curry KV, Golding S. Hair lipids-the extraction of fatty materials from hair clippings. J Soc Cosmet Chem 1971; 22: 681-699.
    • (1971) J Soc Cosmet Chem , vol.22 , pp. 681-699
    • Curry, K.V.1    Golding, S.2
  • 102
    • 0018563347 scopus 로고
    • The extraction, quantification and nature of hair lipid
    • Shaw DA. The extraction, quantification and nature of hair lipid. Int J Cosmet Sci 1979; 1: 291-302.
    • (1979) Int J Cosmet Sci , vol.1 , pp. 291-302
    • Shaw, D.A.1
  • 103
    • 84986409357 scopus 로고
    • Evolution in the composition of human skin surface lipids during their accumulation on scalp and hair
    • Bore P, Goetz N, Gataud P, Tourenq P. Evolution in the composition of human skin surface lipids during their accumulation on scalp and hair. Int J Cosmet Sci 1982; 4: 39-52.
    • (1982) Int J Cosmet Sci , vol.4 , pp. 39-52
    • Bore, P.1    Goetz, N.2    Gataud, P.3    Tourenq, P.4
  • 104
    • 0005893704 scopus 로고
    • Detection and identification of volatile compounds evolved from human hair and scalp using headspace gas chromatography
    • Goetz N, Kaba G, Good D, Hussler G, Bore P. Detection and identification of volatile compounds evolved from human hair and scalp using headspace gas chromatography. J Soc Cosmet Chem 1988; 39: 1-13.
    • (1988) J Soc Cosmet Chem , vol.39 , pp. 1-13
    • Goetz, N.1    Kaba, G.2    Good, D.3    Hussler, G.4    Bore, P.5
  • 106
    • 0039089737 scopus 로고
    • Characterization of internal lipids from wool
    • Schwan A, Herrling J, Zahn H. Characterization of internal lipids from wool. Colloid Polymer Sci 1986; 264: 171-175.
    • (1986) Colloid Polymer Sci , vol.264 , pp. 171-175
    • Schwan, A.1    Herrling, J.2    Zahn, H.3
  • 113
    • 0000043260 scopus 로고    scopus 로고
    • Drug distribution in human hair by infrared microscopy
    • Kalasinsky KS. Drug distribution in human hair by infrared microscopy. Cell Mol Biol 1998; 44: 81-87.
    • (1998) Cell Mol Biol , vol.44 , pp. 81-87
    • Kalasinsky, K.S.1
  • 114
    • 0020665625 scopus 로고
    • Regional differences in hair zinc concentrations: A possible effect of water hardness
    • Gibson RS, Anderson BM, Scythes CA. Regional differences in hair zinc concentrations: a possible effect of water hardness. Am J Clin Nutr 1983; 37: 37-42.
    • (1983) Am J Clin Nutr , vol.37 , pp. 37-42
    • Gibson, R.S.1    Anderson, B.M.2    Scythes, C.A.3
  • 115
    • 0018827507 scopus 로고
    • Interrelationships of blood and hair mercury concentrations in a North American population exposed to methylmercury
    • Phelps RW, Clarkson TW, Kershaw TG, Wheatley B. Interrelationships of blood and hair mercury concentrations in a North American population exposed to methylmercury. Arch Environ Health 1980; 35: 161-168.
    • (1980) Arch Environ Health , vol.35 , pp. 161-168
    • Phelps, R.W.1    Clarkson, T.W.2    Kershaw, T.G.3    Wheatley, B.4
  • 116
    • 0024404632 scopus 로고
    • Hair analysis for drugs of abuse
    • Baumgartner W. Hair analysis for drugs of abuse. J Forensic Sci 1989; 34: 1433-1453.
    • (1989) J Forensic Sci , vol.34 , pp. 1433-1453
    • Baumgartner, W.1
  • 117
    • 0033962028 scopus 로고    scopus 로고
    • Is there a place for hair analysis in doping controls?
    • Rivier L. Is there a place for hair analysis in doping controls? Forensic Sci Int 2000; 107: 309-323.
    • (2000) Forensic Sci Int , vol.107 , pp. 309-323
    • Rivier, L.1
  • 118
    • 0033976412 scopus 로고    scopus 로고
    • Potential problems with the interpretation of hair analysis results
    • Wennig R. Potential problems with the interpretation of hair analysis results. Forensic Sci Int 2000; 107: 5-12.
    • (2000) Forensic Sci Int , vol.107 , pp. 5-12
    • Wennig, R.1
  • 119
    • 0038762085 scopus 로고
    • Hysteresis phenomena in the absorption of water by human hair
    • Chamberlain N, Speakman JB. Hysteresis phenomena in the absorption of water by human hair. J Electrochem 1931; 37: 374-375.
    • (1931) J Electrochem , vol.37 , pp. 374-375
    • Chamberlain, N.1    Speakman, J.B.2
  • 120
    • 84964172854 scopus 로고
    • An experimental and theoretical study of the adsorption and swelling isotherms of human hair in water vapor
    • White HJ, Stam PB. An experimental and theoretical study of the adsorption and swelling isotherms of human hair in water vapor. Text Res J 1949; 19: 136.
    • (1949) Text Res J , vol.19 , pp. 136
    • White, H.J.1    Stam, P.B.2
  • 121
    • 85056963836 scopus 로고    scopus 로고
    • Waiter there’s a hair in my hygrometer
    • Carlson S. Waiter there’s a hair in my hygrometer. Scientific American 1998; 6: 74-75.
    • (1998) Scientific American , vol.6 , pp. 74-75
    • Carlson, S.1
  • 122
    • 0343989876 scopus 로고
    • Nuclear magnetic resonance investigation of the state of water in human hair
    • Clifford J, Sheard B. Nuclear magnetic resonance investigation of the state of water in human hair. Biopolymers 1966; 4: 1057-1065.
    • (1966) Biopolymers , vol.4 , pp. 1057-1065
    • Clifford, J.1    Sheard, B.2
  • 123
    • 34250476447 scopus 로고
    • A NMR study of the anisotropy of water absorbed by keratin
    • Lynch LJ, Haly AR. A NMR study of the anisotropy of water absorbed by keratin. Kolloid zz Polym 1970; 239: 581-586.
    • (1970) Kolloid zz Polym , vol.239 , pp. 581-586
    • Lynch, L.J.1    Haly, A.R.2
  • 124
    • 0006573036 scopus 로고
    • Nondestructive analysis of water structure and content in animal tissues by FT-NIR spectroscopy with light-fiber optics, part I: Human hair
    • Yukihiroozaki Miura T, Sakurai K, Matsunaga T. Nondestructive analysis of water structure and content in animal tissues by FT-NIR spectroscopy with light-fiber optics, part I: Human hair. Appl Spec 1992; 46: 875-878.
    • (1992) Appl Spec , vol.46 , pp. 875-878
    • Yukihiroozaki Miura, T.1    Sakurai, K.2    Matsunaga, T.3
  • 125
    • 0023288930 scopus 로고
    • States of water sorbed on wool as studied by differential scanning calorimetry
    • Ito H, Miyamoto T, Inagaki H, Sakabe H. States of water sorbed on wool as studied by differential scanning calorimetry. Text Res J 1987; 57: 66-72.
    • (1987) Text Res J , vol.57 , pp. 66-72
    • Ito, H.1    Miyamoto, T.2    Inagaki, H.3    Sakabe, H.4
  • 126
    • 0019841713 scopus 로고
    • Free water in hair keratin? A depolarization thermalcurrent study
    • Leveque JL, Garson JC, Pissis P. Free water in hair keratin? a depolarization thermalcurrent study. Biopolym 1980; 20: 2649-2656.
    • (1980) Biopolym , vol.20 , pp. 2649-2656
    • Leveque, J.L.1    Garson, J.C.2    Pissis, P.3
  • 127
    • 0024759045 scopus 로고
    • Water in keratin-piezoelectric, dielectric and elastic experiments
    • Maeda H. Water in keratin-piezoelectric, dielectric and elastic experiments. Biophys J 1989; 56: 861-868.
    • (1989) Biophys J , vol.56 , pp. 861-868
    • Maeda, H.1
  • 128
    • 0014778590 scopus 로고
    • Analysis of sorption isotherms of non-homogeneous sorbents
    • D’Arcy RL, Watt IC. Analysis of sorption isotherms of non-homogeneous sorbents. Trans Faraday Soc 1970; 66: 1236-1245.
    • (1970) Trans Faraday Soc , vol.66 , pp. 1236-1245
    • D’Arcy, R.L.1    Watt, I.C.2
  • 129
    • 84951416631 scopus 로고
    • Sorption of water vapor by keratin
    • Watt IC. Sorption of water vapor by keratin. J Macromol Sci Chem 1980; C18: 169-245.
    • (1980) J Macromol Sci Chem , vol.C18 , pp. 169-245
    • Watt, I.C.1
  • 130
    • 85004485809 scopus 로고
    • Fundamental studies on the interaction between moisture and textiles, part X: Moisture sorption properties of wool and hair fibers
    • Horikita M, Fukuda M, Takaoka A, Kawai H. Fundamental studies on the interaction between moisture and textiles, part X: moisture sorption properties of wool and hair fibers. Sen’i Gakkaishi 1989; 45: 367-381.
    • (1989) Sen’i Gakkaishi , vol.45 , pp. 367-381
    • Horikita, M.1    Fukuda, M.2    Takaoka, A.3    Kawai, H.4
  • 131
    • 84933733147 scopus 로고
    • The nature of water absorbed by the protein keratin
    • Algie JE. The nature of water absorbed by the protein keratin. J Text Inst 1971; 62: 696-699.
    • (1971) J Text Inst , vol.62 , pp. 696-699
    • Algie, J.E.1
  • 132
    • 0017947666 scopus 로고
    • Diffusion characteristics of water vapor in some keratins
    • El-Shimi AF, Princen HM. Diffusion characteristics of water vapor in some keratins. Colloid Polym Sci 1978; 256: 209-217.
    • (1978) Colloid Polym Sci , vol.256 , pp. 209-217
    • El-Shimi, A.F.1    Princen, H.M.2
  • 133
    • 49249140136 scopus 로고
    • An investigation of the freezing of water associated with wool keratin by NMR methods
    • Lynch LJ, Webster DS. An investigation of the freezing of water associated with wool keratin by NMR methods. J Colloid Interf Sci 1979; 69: 238-246.
    • (1979) J Colloid Interf Sci , vol.69 , pp. 238-246
    • Lynch, L.J.1    Webster, D.S.2
  • 134
    • 84964152156 scopus 로고
    • The swelling of human hair in water and water vapor
    • Stam R. The swelling of human hair in water and water vapor. Text Res J 1952; 22: 448-465.
    • (1952) Text Res J , vol.22 , pp. 448-465
    • Stam, R.1
  • 136
    • 0036217572 scopus 로고    scopus 로고
    • A new deformation model for hard alpha-keratin fibers at the nanometer scale: Implications for hard alpha-keratin intermediate filament mechanical properties
    • Kreplak L, Franbourg A, Briki F, Leroy F, Dalle D, Doucet J. A new deformation model for hard alpha-keratin fibers at the nanometer scale: implications for hard alpha-keratin intermediate filament mechanical properties. Biophys J 2002; 82: 2265-2274.
    • (2002) Biophys J , vol.82 , pp. 2265-2274
    • Kreplak, L.1    Franbourg, A.2    Briki, F.3    Leroy, F.4    Dalle, D.5    Doucet, J.6
  • 137
    • 85024467667 scopus 로고
    • Sorption behavior and thermal stability of the microfibril-matrix-complex of alpha-keratins
    • Tokyo
    • Spei M. Sorption behavior and thermal stability of the microfibril-matrix-complex of alpha-keratins. Proc 7th Int Wool Text Res Conf I, 312-318 Tokyo (1985).
    • (1985) Proc 7th Int Wool Text Res Conf , vol.1 , pp. 312-318
    • Spei, M.1
  • 140
    • 0035844696 scopus 로고    scopus 로고
    • Investigation of human hair cuticle structure by microdiffraction: Direct observation of cell membrane complex swelling
    • Kreplak L, Merigoux C, Briki F, Flot D, Doucet J. Investigation of human hair cuticle structure by microdiffraction: direct observation of cell membrane complex swelling. Biochim Biophys Acta 2001; 1547: 268-274.
    • (2001) Biochim Biophys Acta , vol.1547 , pp. 268-274
    • Kreplak, L.1    Merigoux, C.2    Briki, F.3    Flot, D.4    Doucet, J.5
  • 142
    • 0007956329 scopus 로고
    • The behaviour of hair at low pH values
    • Breuer MM, Pritchard D. The behaviour of hair at low pH values. J Soc Cosmet Chem 1967; 18: 643-650.
    • (1967) J Soc Cosmet Chem , vol.18 , pp. 643-650
    • Breuer, M.M.1    Pritchard, D.2
  • 143
    • 0040314034 scopus 로고
    • A study of the swelling of hair in mixed aqueous solvents
    • Valko E, Barnett GJ. A study of the swelling of hair in mixed aqueous solvents. J Soc Cosmet Chem 1952; 3: 108-117.
    • (1952) J Soc Cosmet Chem , vol.3 , pp. 108-117
    • Valko, E.1    Barnett, G.J.2
  • 144
    • 84955117746 scopus 로고
    • The swelling of hair a viscose rayon monofil in aqueous solutions
    • Barnard W, White H. The swelling of hair a viscose rayon monofil in aqueous solutions. Text Res J 1954; 24: 695-704.
    • (1954) Text Res J , vol.24 , pp. 695-704
    • Barnard, W.1    White, H.2
  • 145
    • 79954556513 scopus 로고
    • The nature of melanins
    • Jarrett A, ed, London: Academic
    • Riley PA. The nature of melanins. In: Jarrett A, ed. The Physiology and Pathophysiology of Skin. vol. 3, London: Academic 1974: 1102.
    • (1974) The Physiology and Pathophysiology of Skin , vol.3 , pp. 1102
    • Riley, P.A.1
  • 146
    • 84866986924 scopus 로고
    • A contribution to understanding the nature of hair color
    • Albrecht L, Kurtz SK, Wolfram LJ. A contribution to understanding the nature of hair color. J Soc Cosmet Chem 1988; 39: 396.
    • (1988) J Soc Cosmet Chem , vol.39 , pp. 396
    • Albrecht, L.1    Kurtz, S.K.2    Wolfram, L.J.3
  • 148
    • 0002669405 scopus 로고
    • Biochemistry and physiology of melanin
    • Levine N, ed, New York: CRC Press
    • Ito S. Biochemistry and physiology of melanin. In: Levine N, ed. Pigmentation and Pigmentary Disorders. New York: CRC Press, 1993: 33-59.
    • (1993) Pigmentation and Pigmentary Disorders , pp. 33-59
    • Ito, S.1
  • 149
    • 0014385243 scopus 로고
    • Die Feinstruktur des menschlichen Haares, III. Das Haarpigment
    • Orfanos C, Ruska H. Die Feinstruktur des menschlichen Haares, III. Das Haarpigment. Arch Klin Exp Dermatol 1968; 231: 279.
    • (1968) Arch Klin Exp Dermatol , vol.231 , pp. 279
    • Orfanos, C.1    Ruska, H.2
  • 150
    • 0035283130 scopus 로고    scopus 로고
    • Relationship of melanin degradation products to actual melanin content: Application to human hair
    • Borges CR, Roberts JC, Wilkins DG, Rollins DE. Relationship of melanin degradation products to actual melanin content: application to human hair. Anal Biochem 2001; 290: 116-125.
    • (2001) Anal Biochem , vol.290 , pp. 116-125
    • Borges, C.R.1    Roberts, J.C.2    Wilkins, D.G.3    Rollins, D.E.4
  • 151
    • 0021232445 scopus 로고
    • Feinbau und Chemie des Haares. II
    • Zahn H. Feinbau und Chemie des Haares. II. Parfum Kosmet 1984; 65: 585-594.
    • (1984) Parfum Kosmet , vol.65 , pp. 585-594
    • Zahn, H.1
  • 152
    • 0027217082 scopus 로고
    • Hair melanins and hair color: Ultrastructural and biochemical aspects
    • Ortonne JP, Prota G. Hair melanins and hair color: ultrastructural and biochemical aspects. J Invest Dermatol 1993; 101: 82s-89s.
    • (1993) J Invest Dermatol , vol.101 , pp. 82s-89s
    • Ortonne, J.P.1    Prota, G.2
  • 153
    • 0002283125 scopus 로고
    • Photophysics and photochemistry of melanin
    • Zeise L, Chedekel MR, Fitzpatrick TB, eds, Overland Park, KS: Valdenmar Publishing Company
    • Chedekel MR. Photophysics and photochemistry of melanin. In: Zeise L, Chedekel MR, Fitzpatrick TB, eds. Melanin: Its Role in Human Photoprotection. Vol. 11. Overland Park, KS: Valdenmar Publishing Company, 1995: 11-23.
    • (1995) Melanin: Its Role in Human Photoprotection , vol.11 , pp. 11-23
    • Chedekel, M.R.1
  • 155
    • 0031940949 scopus 로고    scopus 로고
    • Pheomelanin vs.eumelanin as a chemical indicator of UV susceptibility in red haired subjects: A pilot study
    • Vincensi MR, d’Ischia M, Napolitano A. Pheomelanin vs.eumelanin as a chemical indicator of UV susceptibility in red haired subjects: a pilot study. Melanoma Res 1998; 8: 53-58.
    • (1998) Melanoma Res , vol.8 , pp. 53-58
    • Vincensi, M.R.1    d’Ischia, M.2    Napolitano, A.3
  • 157
    • 0002428814 scopus 로고
    • Weathering of hair
    • Tolgyesi E. Weathering of hair. Cosmet Toiletries 1983; 98(10): 29-33.
    • (1983) Cosmet Toiletries , vol.98 , Issue.10 , pp. 29-33
    • Tolgyesi, E.1
  • 159
    • 0042701819 scopus 로고
    • Isolation of melanin pigments from human hair
    • Arnaud JC, Boré P. Isolation of melanin pigments from human hair. J Soc Cosmet Chem 1981; 32: 137-152.
    • (1981) J Soc Cosmet Chem , vol.32 , pp. 137-152
    • Arnaud, J.C.1    Boré, P.2
  • 161
    • 0001270545 scopus 로고
    • Chemical- and photo-bleaching of brown and red hair
    • Wolfram LJ, Albrecht L. Chemical- and photo-bleaching of brown and red hair. J Soc Cosmet Chem 1987; 82: 179-191.
    • (1987) J Soc Cosmet Chem , vol.82 , pp. 179-191
    • Wolfram, L.J.1    Albrecht, L.2
  • 162
    • 0020676663 scopus 로고
    • A comparative study of the physical and chemical properties of melanins isolated from human black and red hair
    • Menon IA, Persad S, Haberman HF, Kurian CJ. A comparative study of the physical and chemical properties of melanins isolated from human black and red hair. J lnvest Dermatol 1983; 80(3): 202-206.
    • (1983) J lnvest Dermatol , vol.80 , Issue.3 , pp. 202-206
    • Menon, I.A.1    Persad, S.2    Haberman, H.F.3    Kurian, C.J.4
  • 163
    • 0013769875 scopus 로고
    • Structure of melanins and melanogenesis. IV. On some natural melanins
    • Nicolaus RA, Piatelli M, Fattorusso E. Structure of melanins and melanogenesis. IV. On some natural melanins. Tetrahedron 1964; 20: 1163.
    • (1964) Tetrahedron , vol.20 , pp. 1163
    • Nicolaus, R.A.1    Piatelli, M.2    Fattorusso, E.3
  • 165
    • 1842396465 scopus 로고
    • Some problems of tyrosine metabolism
    • Raper HS. Some problems of tyrosine metabolism. J Chem Soc 1938: 125-130.
    • (1938) J Chem Soc , pp. 125-130
    • Raper, H.S.1
  • 166
    • 77049203277 scopus 로고
    • Comparative biochemistry of phenoloxidase complexes
    • Mason HS. Comparative biochemistry of phenoloxidase complexes. Adv Enzymol 1955; 14: 105-184.
    • (1955) Adv Enzymol , vol.14 , pp. 105-184
    • Mason, H.S.1
  • 168
    • 0017388583 scopus 로고
    • A facile one-step synthesis of cysteinyl dopas using mushroom tyrosinase
    • Ito G, Prota G. A facile one-step synthesis of cysteinyl dopas using mushroom tyrosinase. Experientia 1977; 33: 1118-1119.
    • (1977) Experientia , vol.33 , pp. 1118-1119
    • Ito, G.1    Prota, G.2
  • 171
    • 0002281576 scopus 로고    scopus 로고
    • The chemistry of melanins and related metabolites
    • Nordlung JJ, Boissy RE, Hearing VJ, et al., eds, New York: Oxford University Press
    • Prota G, d’Ischia M, Napolitano A. The chemistry of melanins and related metabolites. In: Nordlung JJ, Boissy RE, Hearing VJ, et al., eds. The Pigmentary System: Physiology and Pathophysiology. New York: Oxford University Press, 1998: 307-332.
    • (1998) The Pigmentary System: Physiology and Pathophysiology , pp. 307-332
    • Prota, G.1    d’Ischia, M.2    Napolitano, A.3
  • 174
    • 8544259014 scopus 로고
    • Prediction of hair assembly characteristics from single fiber properties
    • Robbins CR, Scott GV. Prediction of hair assembly characteristics from single fiber properties. J Soc Cosmet Chem 1978; 29: 783-792.
    • (1978) J Soc Cosmet Chem , vol.29 , pp. 783-792
    • Robbins, C.R.1    Scott, G.V.2
  • 175
    • 1842771268 scopus 로고
    • Prediction of hair assembly characteristics from single-fiber properties, Part II: The relationship of fiber curvature, friction, stiffness and diameter to combing behavior
    • Robbins CR, Reich C. Prediction of hair assembly characteristics from single-fiber properties, Part II: the relationship of fiber curvature, friction, stiffness and diameter to combing behavior. J Soc Cosmet Chem 1986; 37: 141-158.
    • (1986) J Soc Cosmet Chem , vol.37 , pp. 141-158
    • Robbins, C.R.1    Reich, C.2
  • 176
    • 75649109792 scopus 로고
    • The plasticity of wool
    • Speakman JB. The plasticity of wool. Proc Roy Soc B 1928; 103: 377-396.
    • (1928) Proc Roy Soc B , vol.103 , pp. 377-396
    • Speakman, J.B.1
  • 177
    • 0006869799 scopus 로고
    • The rigidity of wool and its change with adsorption of water vapour
    • Speakman JB. The rigidity of wool and its change with adsorption of water vapour. Trans Faraday Soc 1929; 25: 93-103.
    • (1929) Trans Faraday Soc , vol.25 , pp. 93-103
    • Speakman, J.B.1
  • 178
    • 84871520083 scopus 로고
    • Adsorption of water by wool. Adsorption of water by wool
    • Speakman JB, Adsorption of water by wool. Adsorption of water by wool. J Soc Chem Ind 1930; 49: 209T-213T.
    • (1930) J Soc Chem Ind , vol.49 , pp. 209T-213T
    • Speakman, J.B.1
  • 179
    • 0001180907 scopus 로고
    • Temperature dependence of the mechanical properties of human hair in relation to structure
    • Rebenfeld L, Weigmann HD, Dansizer CJ. Temperature dependence of the mechanical properties of human hair in relation to structure. J Soc Cosmet Chem 1966; 17: 525-538.
    • (1966) J Soc Cosmet Chem , vol.17 , pp. 525-538
    • Rebenfeld, L.1    Weigmann, H.D.2    Dansizer, C.J.3
  • 180
    • 85056959340 scopus 로고
    • Mechanical properties of keratins
    • Pretoria
    • Bendit EG. Mechanical properties of keratins. Proc 6th Int Wool Text Res Conf 6(2), 43-66 Pretoria (1980).
    • (1980) Proc 6th Int Wool Text Res Conf , vol.6 , Issue.2 , pp. 43-66
    • Bendit, E.G.1
  • 181
    • 0019138788 scopus 로고
    • There is no hookean region in the stress-strain curve of keratin (or other viscoelastic polymers)
    • Bendit EG. There is no hookean region in the stress-strain curve of keratin (or other viscoelastic polymers). J Macromol Sci Phys 1980; B17(1): 129-140.
    • (1980) J Macromol Sci Phys , vol.B17 , Issue.1 , pp. 129-140
    • Bendit, E.G.1
  • 182
    • 0000365266 scopus 로고
    • A quantitative X-ray diffraction study of the alpha-beta transformation in wool keratin
    • Bendit EG. A quantitative X-ray diffraction study of the alpha-beta transformation in wool keratin. Text Res J 1960; 30(8): 547-555.
    • (1960) Text Res J , vol.30 , Issue.8 , pp. 547-555
    • Bendit, E.G.1
  • 183
    • 84966156466 scopus 로고
    • Cooperative unfolding of alpha-keratin
    • Feughelman M. Cooperative unfolding of alpha-keratin. J Appl Polym Sci 1966; 10: 1937-1947.
    • (1966) J Appl Polym Sci , vol.10 , pp. 1937-1947
    • Feughelman, M.1
  • 184
    • 85056975824 scopus 로고
    • The mechanical properties of wool keratin
    • Feughelman M. The mechanical properties of wool keratin. Royal Austral Chem Inst 1968; 35(5): 2-3.
    • (1968) Royal Austral Chem Inst , vol.35 , Issue.5 , pp. 2-3
    • Feughelman, M.1
  • 185
    • 0000160559 scopus 로고
    • The alpha-beta transformation in keratin
    • Bendit EG. The alpha-beta transformation in keratin. Nature 1957; 4558: 535.
    • (1957) Nature , vol.4558 , pp. 535
    • Bendit, E.G.1
  • 186
    • 84965853424 scopus 로고
    • The stress-strain characteristics of animal fibers after reduction and alkylation
    • Crewther WG. The stress-strain characteristics of animal fibers after reduction and alkylation. Text Res J 1965; 35(10): 867-877.
    • (1965) Text Res J , vol.35 , Issue.10 , pp. 867-877
    • Crewther, W.G.1
  • 187
    • 0001514744 scopus 로고    scopus 로고
    • DSC studies of the melting behaviour of alpha form crystallites in wool keratin
    • Cao J, Joko K, Cook JR. DSC studies of the melting behaviour of alpha form crystallites in wool keratin. Text Res J 1997; 67(2): 117-123.
    • (1997) Text Res J , vol.67 , Issue.2 , pp. 117-123
    • Cao, J.1    Joko, K.2    Cook, J.R.3
  • 188
    • 0037051763 scopus 로고    scopus 로고
    • Is the alpha-beta transition of keratin a transition of alpha-helices to betapleated sheets? Part II: Synchrotron investigation for stretched single specimens
    • Cao J. Is the alpha-beta transition of keratin a transition of alpha-helices to betapleated sheets? Part II: Synchrotron investigation for stretched single specimens. J Mol Structure 2002; 607: 69-75.
    • (2002) J Mol Structure , vol.607 , pp. 69-75
    • Cao, J.1
  • 189
    • 0034633562 scopus 로고    scopus 로고
    • Is the alpha-beta transition of keratin a transition of alpha-helices to betapleated sheets? Part I: In situ XRD studies
    • Cao J. Is the alpha-beta transition of keratin a transition of alpha-helices to betapleated sheets? Part I: In situ XRD studies. J Mol Structure 2000; 553: 101-107.
    • (2000) J Mol Structure , vol.553 , pp. 101-107
    • Cao, J.1
  • 190
    • 0035052403 scopus 로고    scopus 로고
    • Unravelling double stranded alpha-helical coiled coils. An X-ray diffraction study on hard alpha-keratin fibres
    • Kreplak L, Doucet J, Briki F. Unravelling double stranded alpha-helical coiled coils. An X-ray diffraction study on hard alpha-keratin fibres. Biopolymers 2001; 58(5): 526-533.
    • (2001) Biopolymers , vol.58 , Issue.5 , pp. 526-533
    • Kreplak, L.1    Doucet, J.2    Briki, F.3
  • 191
    • 0002290595 scopus 로고
    • Mechanical and fractographic behavior of negroid hair
    • Kamath YK, Hornby SB. Mechanical and fractographic behavior of negroid hair. J Soc Cosmet Chem 1984; 35: 21-43.
    • (1984) J Soc Cosmet Chem , vol.35 , pp. 21-43
    • Kamath, Y.K.1    Hornby, S.B.2
  • 194
    • 0011304931 scopus 로고
    • Effect of chemical and humectant treatments on the mechanical and fractographic behavior of negroid hair
    • Kamath YK, Hornsby SB, Weigmann HD. Effect of chemical and humectant treatments on the mechanical and fractographic behavior of negroid hair. J Soc Cosmet Chem 1985; 36(1): 39-52.
    • (1985) J Soc Cosmet Chem , vol.36 , Issue.1 , pp. 39-52
    • Kamath, Y.K.1    Hornsby, S.B.2    Weigmann, H.D.3
  • 197
    • 0014590673 scopus 로고
    • A convenient method for measuring fiber stiffness
    • Scott GV, Robbins CR. A convenient method for measuring fiber stiffness. Text Res J 1969; 39: 975-976.
    • (1969) Text Res J , vol.39 , pp. 975-976
    • Scott, G.V.1    Robbins, C.R.2
  • 199
    • 0019175502 scopus 로고
    • Les propriétés vibratoires transversales des fibres de kératine. Influence de l’eau et d’autres agents
    • Garson JC, Vidalis M, Roussopoulos P, Levêque JL. Les propriétés vibratoires transversales des fibres de kératine. Influence de l’eau et d’autres agents. Int J Cosmet Sci 1980; 2: 231-241.
    • (1980) Int J Cosmet Sci , vol.2 , pp. 231-241
    • Garson, J.C.1    Vidalis, M.2    Roussopoulos, P.3    Levêque, J.L.4
  • 200
    • 0012975224 scopus 로고
    • Torsional behavior of human hair
    • Wolfram LJ, Albrecht L. Torsional behavior of human hair. J Soc Cosmet Chem 1985; 36(1): 87-99.
    • (1985) J Soc Cosmet Chem , vol.36 , Issue.1 , pp. 87-99
    • Wolfram, L.J.1    Albrecht, L.2
  • 201
    • 84970278526 scopus 로고
    • An apparatus for measuring bending and torsional stress-strain-time relations of single fibers
    • Chapman BM. An apparatus for measuring bending and torsional stress-strain-time relations of single fibers. Text Res J 1971; 41: 705-707.
    • (1971) Text Res J , vol.41 , pp. 705-707
    • Chapman, B.M.1
  • 202
    • 84945779683 scopus 로고
    • On polymeric materials containing fibrils with a phase transition. II. The mechanical consequence of matrix shear
    • Chapman BM, Hearle JWS. On polymeric materials containing fibrils with a phase transition. II. The mechanical consequence of matrix shear. J Macromol Sci Phys 1968; B2(4): 697-741.
    • (1968) J Macromol Sci Phys , vol.B2 , Issue.4 , pp. 697-741
    • Chapman, B.M.1    Hearle, J.W.S.2
  • 203
    • 0015682516 scopus 로고
    • The effect of hydrophobic interactions on the torsional setting and smooth-drying properties of wool
    • Feldtman HD, Fleischfresser BE. The effect of hydrophobic interactions on the torsional setting and smooth-drying properties of wool. J Text Inst 1973; 64(11): 624-630.
    • (1973) J Text Inst , vol.64 , Issue.11 , pp. 624-630
    • Feldtman, H.D.1    Fleischfresser, B.E.2
  • 204
    • 84964188022 scopus 로고
    • The torsional properties of single wool fibers, part I: Torque- twist relationships and torsional relaxation in wet and dry fibers
    • Mitchell TW, Feughelman M. The torsional properties of single wool fibers, part I: torque- twist relationships and torsional relaxation in wet and dry fibers. Text Res J 1960; 30: 662-667.
    • (1960) Text Res J , vol.30 , pp. 662-667
    • Mitchell, T.W.1    Feughelman, M.2
  • 205
    • 84964169105 scopus 로고
    • Torsional properties of chemically modified wool fibers
    • Feughelman M, Watt IC. Torsional properties of chemically modified wool fibers. Text Res J 1966; 36: 849-850.
    • (1966) Text Res J , vol.36 , pp. 849-850
    • Feughelman, M.1    Watt, I.C.2
  • 206
    • 0018018363 scopus 로고
    • The microfibril-matrix relationships in the mechanical properties of keratin fibers, part I: The torsional properties of melted and permanently set keratin fibers
    • Feughelman M. The microfibril-matrix relationships in the mechanical properties of keratin fibers, part I: the torsional properties of melted and permanently set keratin fibers. Text Res J 1978; 48: 518-522.
    • (1978) Text Res J , vol.48 , pp. 518-522
    • Feughelman, M.1
  • 207
    • 84965916774 scopus 로고
    • The torsional properties of single wool fibers. Part II
    • Feughelman M, Mitchell TW. The torsional properties of single wool fibers. Part II. Text Res J 1961: 455-459.
    • (1961) Text Res J , pp. 455-459
    • Feughelman, M.1    Mitchell, T.W.2
  • 208
    • 0014477187 scopus 로고
    • The torsional properties of normal and sulfur-enriched wool fibers, Part II: Modulus of rigidity and torsional relaxation of fibers in water at temperatures between 20°C and 85°C
    • Armstrong LD, Feughelman M. The torsional properties of normal and sulfur-enriched wool fibers, Part II: modulus of rigidity and torsional relaxation of fibers in water at temperatures between 20°C and 85°C. Text Res J 1969; 39: 267-272.
    • (1969) Text Res J , vol.39 , pp. 267-272
    • Armstrong, L.D.1    Feughelman, M.2
  • 209
    • 84965953879 scopus 로고
    • The torsional properties of single wool fibers, part III: Disulfide reduced and permanently set wool fibers
    • Feughelman M, Mitchell TW. The torsional properties of single wool fibers, part III: disulfide reduced and permanently set wool fibers. Text Res J 1964; 34: 593-597.
    • (1964) Text Res J , vol.34 , pp. 593-597
    • Feughelman, M.1    Mitchell, T.W.2
  • 210
    • 0014476623 scopus 로고
    • The torsional properties of normal and sulfur-enriched wool fibers, part I: Modulus of rigidity and torsional relaxation of wet and dry fibers at 20°C
    • Armstrong LD, Feughelman M. The torsional properties of normal and sulfur-enriched wool fibers, part I: modulus of rigidity and torsional relaxation of wet and dry fibers at 20°C. Text Res J 1969; 39: 261-266.
    • (1969) Text Res J , vol.39 , pp. 261-266
    • Armstrong, L.D.1    Feughelman, M.2
  • 211
    • 10444263886 scopus 로고
    • Torsional properties of hair in relation to permanent waving and setting
    • Bogaty H. Torsional properties of hair in relation to permanent waving and setting. J Soc Cosmet Chem 1967; 18: 575-589.
    • (1967) J Soc Cosmet Chem , vol.18 , pp. 575-589
    • Bogaty, H.1
  • 212
    • 0023383732 scopus 로고
    • Effects of humidity, ageing, annealing and tensile loads on the torsional damping of wool fibers
    • Phillips DG. Effects of humidity, ageing, annealing and tensile loads on the torsional damping of wool fibers. Text Res J 1987; 57(7): 415-420.
    • (1987) Text Res J , vol.57 , Issue.7 , pp. 415-420
    • Phillips, D.G.1
  • 213
    • 84965400590 scopus 로고
    • Changes in the cross-linking of keratin fibers as revealed by stress-relaxation studies
    • Mottram FJ, Coad JR. Changes in the cross-linking of keratin fibers as revealed by stress-relaxation studies. Text Res J 1974; 44: 557-558.
    • (1974) Text Res J , vol.44 , pp. 557-558
    • Mottram, F.J.1    Coad, J.R.2
  • 214
    • 0022134001 scopus 로고
    • Thiol differences along keratin fibres-stress/strain and stress-relaxation behavior as a function of temperature and extension
    • Robinson MS, Rigby BJ. Thiol differences along keratin fibres-stress/strain and stress-relaxation behavior as a function of temperature and extension. Text Res J 1985; 55: 597-600.
    • (1985) Text Res J , vol.55 , pp. 597-600
    • Robinson, M.S.1    Rigby, B.J.2
  • 215
    • 25044466843 scopus 로고
    • The relaxation of stretched animal fibres-the relaxation of human hair
    • Wood GC. The relaxation of stretched animal fibres-the relaxation of human hair. J Text Inst 1954; 45: 462-471.
    • (1954) J Text Inst , vol.45 , pp. 462-471
    • Wood, G.C.1
  • 217
    • 34250517546 scopus 로고
    • The viscoelasticity and structure of fibrous proteins, II: Further dynamic measurements of keratin
    • Mason P. The viscoelasticity and structure of fibrous proteins, II: further dynamic measurements of keratin. Kolloid zz Polym 1967; 218: 46-52.
    • (1967) Kolloid zz Polym , vol.218 , pp. 46-52
    • Mason, P.1
  • 218
    • 0019346663 scopus 로고
    • Dynamic mechanical properties of keratin fibers during water absorption and desorption
    • Danilatos GD, Postle R. Dynamic mechanical properties of keratin fibers during water absorption and desorption. J Appl Polym Sci 1981; 26: 193-200.
    • (1981) J Appl Polym Sci , vol.26 , pp. 193-200
    • Danilatos, G.D.1    Postle, R.2
  • 219
    • 0017015411 scopus 로고
    • The internal dynamic mechanical loss in alpha-keratin fibers during moisture sorption
    • Danilatos GD, Feughelman M. The internal dynamic mechanical loss in alpha-keratin fibers during moisture sorption. Text Res J 1976; 46: 845-846.
    • (1976) Text Res J , vol.46 , pp. 845-846
    • Danilatos, G.D.1    Feughelman, M.2
  • 220
    • 0016061738 scopus 로고
    • Dynamic mechanical loss in keratin at low temperatures
    • Druhala M, Feughelman M. Dynamic mechanical loss in keratin at low temperatures. Colloid Polym Sci 1974; 252(5): 381-391.
    • (1974) Colloid Polym Sci , vol.252 , Issue.5 , pp. 381-391
    • Druhala, M.1    Feughelman, M.2
  • 221
    • 0018706897 scopus 로고
    • Dynamic mechanical properties of alpha keratin fibers during extension
    • Danilatos GD, Feughelman M. Dynamic mechanical properties of alpha keratin fibers during extension. J Macromol Sci Phys 1979; B19: 581-602.
    • (1979) J Macromol Sci Phys , vol.B19 , pp. 581-602
    • Danilatos, G.D.1    Feughelman, M.2
  • 222
    • 0020718768 scopus 로고
    • The time temperature dependence of the complex modulus of keratin fibers
    • Danilatos GD, Postle R. The time temperature dependence of the complex modulus of keratin fibers. J Appl Polym Sci 1983; 28: 1221-1224.
    • (1983) J Appl Polym Sci , vol.28 , pp. 1221-1224
    • Danilatos, G.D.1    Postle, R.2
  • 223
    • 0019653977 scopus 로고
    • Low-strain dynamic mechanical properties of keratin fibers during water absorption
    • Danilatos GD, Postle R. Low-strain dynamic mechanical properties of keratin fibers during water absorption. J Macromol Sci Phys 1981; B1(19): 153-165.
    • (1981) J Macromol Sci Phys , vol.B1 , Issue.19 , pp. 153-165
    • Danilatos, G.D.1    Postle, R.2
  • 225
    • 85027475975 scopus 로고
    • The effect of the sorption process on the dynamic rigidity modulus of the wool fiber
    • Mackay BH, Downes JG. The effect of the sorption process on the dynamic rigidity modulus of the wool fiber. J Appl Polym Sci 1959; 2(4): 32-38.
    • (1959) J Appl Polym Sci , vol.2 , Issue.4 , pp. 32-38
    • Mackay, B.H.1    Downes, J.G.2
  • 226
    • 0012969303 scopus 로고
    • Cuticle damage and tensile properties of human hair
    • Robbins CR, Crawford RJ. Cuticle damage and tensile properties of human hair. J Soc Cosmet Chem 1991; 42: 59-67.
    • (1991) J Soc Cosmet Chem , vol.42 , pp. 59-67
    • Robbins, C.R.1    Crawford, R.J.2
  • 227
    • 0038876979 scopus 로고    scopus 로고
    • Mechanism of tensile stress release in the keratin fiber cuticle: I
    • Ruetsch SB, Weigmann HD. Mechanism of tensile stress release in the keratin fiber cuticle: I. J Soc Cosmet Chem 1996; 47: 13-26.
    • (1996) J Soc Cosmet Chem , vol.47 , pp. 13-26
    • Ruetsch, S.B.1    Weigmann, H.D.2
  • 228
    • 0029589997 scopus 로고
    • Some simple theoretical considerations on the bending stiffness of human hair
    • Swift JA. Some simple theoretical considerations on the bending stiffness of human hair. Int J Cosmet Sci 1995; 17: 245-253.
    • (1995) Int J Cosmet Sci , vol.17 , pp. 245-253
    • Swift, J.A.1
  • 230
    • 0001748317 scopus 로고
    • Some mechanical properties of wool fibers in the hookean region from zero to 100% relative humidity
    • Feughelman M, Robinson MS. Some mechanical properties of wool fibers in the hookean region from zero to 100% relative humidity. Text Res J 1971; 41(6): 469-474.
    • (1971) Text Res J , vol.41 , Issue.6 , pp. 469-474
    • Feughelman, M.1    Robinson, M.S.2
  • 231
    • 34250468665 scopus 로고
    • Mechanical properties of keratin fibres between -196 and 20°C
    • Druhala M, Feughelman M. Mechanical properties of keratin fibres between -196 and 20°C. Kolloid zz Polym 1971; 248: 1032-1033.
    • (1971) Kolloid zz Polym , vol.248 , pp. 1032-1033
    • Druhala, M.1    Feughelman, M.2
  • 232
    • 0016567127 scopus 로고
    • Properties of wool fibers heated to temperature above 100 degrees
    • Watt IC. Properties of wool fibers heated to temperature above 100 degrees. Text Res J 1975; 45: 728-735.
    • (1975) Text Res J , vol.45 , pp. 728-735
    • Watt, I.C.1
  • 233
    • 83255165194 scopus 로고
    • Feughelman. The mechanical properties of wool fibers in water at temperatures above 100 degree
    • Mitchell TW, Feughelman. The mechanical properties of wool fibers in water at temperatures above 100 degree. Text Res J 1967; 37(8): 660-666.
    • (1967) Text Res J , vol.37 , Issue.8 , pp. 660-666
    • Mitchell, T.W.1
  • 234
    • 0014510758 scopus 로고
    • A review of the mechanical properties of keratin fibres
    • Chapman BM. A review of the mechanical properties of keratin fibres. J Text Inst 1969; 60: 181-207.
    • (1969) J Text Inst , vol.60 , pp. 181-207
    • Chapman, B.M.1
  • 235
    • 33947444019 scopus 로고
    • Elasticity of keratin fibers, part II: Influence of temperature
    • Bull HB. Elasticity of keratin fibers, part II: influence of temperature. Jaocs 1945; 67: 533-536.
    • (1945) Jaocs , vol.67 , pp. 533-536
    • Bull, H.B.1
  • 236
    • 0034029857 scopus 로고    scopus 로고
    • A critical review of the structural mechanics of wool and hair fibres
    • Hearle JWS. A critical review of the structural mechanics of wool and hair fibres. Int J Macromol 2000; 27: 123-138.
    • (2000) Int J Macromol , vol.27 , pp. 123-138
    • Hearle, J.W.S.1
  • 237
    • 84964165967 scopus 로고
    • A two-phase structure for keratin fibers
    • Feughelman M. A two-phase structure for keratin fibers. Text Res J 1959; 29: 223-228.
    • (1959) Text Res J , vol.29 , pp. 223-228
    • Feughelman, M.1
  • 238
    • 0027953051 scopus 로고
    • The stress/strain curve of alpha-keratin fibers and the structure of the intermediate filament
    • Wortmann FJ, Zahn H. The stress/strain curve of alpha-keratin fibers and the structure of the intermediate filament. Text Res J 1994; 64(12): 737-743.
    • (1994) Text Res J , vol.64 , Issue.12 , pp. 737-743
    • Wortmann, F.J.1    Zahn, H.2
  • 239
    • 84964153039 scopus 로고
    • A mechanical model for wool and other keratin fibers
    • Chapman BM. A mechanical model for wool and other keratin fibers. Text Res J 1969; 39: 1102-1109.
    • (1969) Text Res J , vol.39 , pp. 1102-1109
    • Chapman, B.M.1
  • 240
    • 0000365266 scopus 로고
    • A quantitative X-ray diffraction study of the alpha-beta transformation in wool keratin
    • Bendit EG. A quantitative X-ray diffraction study of the alpha-beta transformation in wool keratin. Text Res J 1960; 30(8): 547-555.
    • (1960) Text Res J , vol.30 , Issue.8 , pp. 547-555
    • Bendit, E.G.1
  • 241
    • 0001442128 scopus 로고
    • The mechanical properties of wool keratin and its molecular configuration
    • Feughelman M, Haly AR. The mechanical properties of wool keratin and its molecular configuration. Kolloid zz Polym 1960; 168: 107-115.
    • (1960) Kolloid zz Polym , vol.168 , pp. 107-115
    • Feughelman, M.1    Haly, A.R.2
  • 242
    • 8444228117 scopus 로고
    • A mechanical model for wool
    • Menefee E. A mechanical model for wool. Text Res J 1968; 38(12): 1149-1163.
    • (1968) Text Res J , vol.38 , Issue.12 , pp. 1149-1163
    • Menefee, E.1
  • 243
    • 8744247043 scopus 로고
    • Relations between structure and the mechanical properties of keratin fibers
    • Feughelman M. Relations between structure and the mechanical properties of keratin fibers. Appl Polym Symp 1971; 18(2): 757-774.
    • (1971) Appl Polym Symp , vol.18 , Issue.2 , pp. 757-774
    • Feughelman, M.1
  • 244
    • 84910232276 scopus 로고
    • Relation of keratin structure to its mechanical behavior
    • Menefee E. Relation of keratin structure to its mechanical behavior. Appl Polym Symp 1971; 18: 809-821.
    • (1971) Appl Polym Symp , vol.18 , pp. 809-821
    • Menefee, E.1
  • 245
    • 0008162524 scopus 로고
    • A unified structural theory for wool keratin
    • Skertchly ARB. A unified structural theory for wool keratin. Nature 1964; 202: 161-164.
    • (1964) Nature , vol.202 , pp. 161-164
    • Skertchly, A.R.B.1
  • 246
    • 0015288199 scopus 로고
    • The effects of disaggregating agents on the stress-strain relationship for wool fibers
    • Crewther WG. The effects of disaggregating agents on the stress-strain relationship for wool fibers. Text Res J 1972; 42(2): 77-85.
    • (1972) Text Res J , vol.42 , Issue.2 , pp. 77-85
    • Crewther, W.G.1
  • 247
    • 84948636557 scopus 로고
    • The stress relaxation and set of wool fibers with particular reference to their structure and mechanical properties
    • Munakata H. The stress relaxation and set of wool fibers with particular reference to their structure and mechanical properties. Text Res J 1964; 3: 97-109.
    • (1964) Text Res J , vol.3 , pp. 97-109
    • Munakata, H.1
  • 248
    • 0000036273 scopus 로고
    • A note on the role of the microfibrils in the mechanical properties of alpha-keratins
    • Feughelman M. A note on the role of the microfibrils in the mechanical properties of alpha-keratins. J Macromol Sci Phys 1979; B16(1): 155-162.
    • (1979) J Macromol Sci Phys , vol.B16 , Issue.1 , pp. 155-162
    • Feughelman, M.1
  • 249
    • 0343667664 scopus 로고
    • On polymeric materials containing fibrils with a phase transition, part I: General discussion of mechanics applied particularly to wools fibers
    • Chapman BM, Hearle JWS. On polymeric materials containing fibrils with a phase transition, part I: General discussion of mechanics applied particularly to wools fibers. J Macromol Sci Phys 1968; B2(4): 663-695.
    • (1968) J Macromol Sci Phys , vol.B2 , Issue.4 , pp. 663-695
    • Chapman, B.M.1    Hearle, J.W.S.2
  • 250
    • 84946250829 scopus 로고
    • On polymeric materials containing fibrils with a phase transition, part IV: Comparison model predictions with behaviour of wool fibers
    • Chapman BM, Hearle JWS. On polymeric materials containing fibrils with a phase transition, part IV: Comparison model predictions with behaviour of wool fibers. J Macromol Sci Phys 1971; B5(4): 633-660.
    • (1971) J Macromol Sci Phys , vol.B5 , Issue.4 , pp. 633-660
    • Chapman, B.M.1    Hearle, J.W.S.2
  • 251
    • 84964143506 scopus 로고
    • A new theory of non-linear viscous elasticity
    • Burte H, Halsey G. A new theory of non-linear viscous elasticity. Text Res J 1947; 17(9): 465-476.
    • (1947) Text Res J , vol.17 , Issue.9 , pp. 465-476
    • Burte, H.1    Halsey, G.2
  • 253
    • 0024621144 scopus 로고
    • A viscoelastic analysis of the keratin composite, part I: Longitudinal and transverse mechanical properties
    • Tao X, Postle R. A viscoelastic analysis of the keratin composite, part I: Longitudinal and transverse mechanical properties. Text Res J 1989; 59: 123-138.
    • (1989) Text Res J , vol.59 , pp. 123-138
    • Tao, X.1    Postle, R.2
  • 254
    • 0024656803 scopus 로고
    • A viscoelastic analysis of the keratin composite, part II: Thermal and hydral expansion
    • Tao X, Postle R. A viscoelastic analysis of the keratin composite, part II: thermal and hydral expansion. Text Res J 1989; 59: 300-306.
    • (1989) Text Res J , vol.59 , pp. 300-306
    • Tao, X.1    Postle, R.2
  • 255
    • 0022097876 scopus 로고
    • A micromechanics analysis of the mechanical behavior of the alpha-keratin composite at low strains-theoretical formulation
    • Curiskis JI, Feughelman M. A micromechanics analysis of the mechanical behavior of the alpha-keratin composite at low strains-theoretical formulation. Text Res J 1985; 55: 425-444.
    • (1985) Text Res J , vol.55 , pp. 425-444
    • Curiskis, J.I.1    Feughelman, M.2
  • 256
    • 0020749320 scopus 로고
    • Finite element analysis of the composite fiber, alpha keratin
    • Curiskis JI, Feughelman M. Finite element analysis of the composite fiber, alpha keratin. Text Res J 1983; 53: 271-274.
    • (1983) Text Res J , vol.53 , pp. 271-274
    • Curiskis, J.I.1    Feughelman, M.2
  • 257
    • 0040033891 scopus 로고
    • The effect of grooming on the hair cuticle
    • Kelly NC, Robinson VNE. The effect of grooming on the hair cuticle. J Soc Cosmet Chem 1982; 33: 203-215.
    • (1982) J Soc Cosmet Chem , vol.33 , pp. 203-215
    • Kelly, N.C.1    Robinson, V.N.E.2
  • 258
    • 85056955580 scopus 로고
    • Studies on the mechanism of split ends generation and on the factors to cause the exfoliation of the cuticle cell layers in human hair
    • Kambe T, Fukuchi Y, Torii K. Studies on the mechanism of split ends generation and on the factors to cause the exfoliation of the cuticle cell layers in human hair. Proc 6th Int Hair Sci Symp DWI (Lüneburg) (1988).
    • (1988) Proc 6th Int Hair Sci Symp DWI (Lüneburg)
    • Kambe, T.1    Fukuchi, Y.2    Torii, K.3
  • 260
    • 0009781203 scopus 로고    scopus 로고
    • The cracking of human hair cuticles by cyclical thermal stresses
    • Gamez-Garcia M. The cracking of human hair cuticles by cyclical thermal stresses. J Soc Cosmet Sci 1998; 49: 141-153.
    • (1998) J Soc Cosmet Sci , vol.49 , pp. 141-153
    • Gamez-Garcia, M.1
  • 261
    • 0040633200 scopus 로고    scopus 로고
    • Cuticle decementation and cuticle buckling produced by Poisson contraction on the cuticular envelope of human hair
    • Gamez-Garcia M. Cuticle decementation and cuticle buckling produced by Poisson contraction on the cuticular envelope of human hair. J Soc Cosmet Sci 1998; 49: 213-222.
    • (1998) J Soc Cosmet Sci , vol.49 , pp. 213-222
    • Gamez-Garcia, M.1
  • 262
    • 0040570983 scopus 로고    scopus 로고
    • Use of atomic force microscopy for high-resolution non-invasive structural studies of human hair
    • Smith JR. Use of atomic force microscopy for high-resolution non-invasive structural studies of human hair. J Soc Cosmet Chem 1997; 48: 199-208.
    • (1997) J Soc Cosmet Chem , vol.48 , pp. 199-208
    • Smith, J.R.1
  • 263
    • 3042569457 scopus 로고    scopus 로고
    • Correlation of AFM/LFM with combing forces of human hair
    • McMullen RL, Kelty SP, Jachowicz J. Correlation of AFM/LFM with combing forces of human hair. Int J Cosmet Sci 2000; 51: 334-335.
    • (2000) Int J Cosmet Sci , vol.51 , pp. 334-335
    • McMullen, R.L.1    Kelty, S.P.2    Jachowicz, J.3
  • 264
    • 0035307127 scopus 로고    scopus 로고
    • Changes in the covalently bound surface lipid layer of damaged wool fibers and their effects on surface properties
    • Baba T, Nagazawa N, Ito H, Yaida O, Miyamoto T. Changes in the covalently bound surface lipid layer of damaged wool fibers and their effects on surface properties. Textile Res J 2001; 71: 308-312.
    • (2001) Textile Res J , vol.71 , pp. 308-312
    • Baba, T.1    Nagazawa, N.2    Ito, H.3    Yaida, O.4    Miyamoto, T.5
  • 265
    • 0035483152 scopus 로고    scopus 로고
    • Recovery of the surface properties of damaged wool fibers
    • Baba T, Nagasawa N, Ito H, Yaida O, Miyamoto T. Recovery of the surface properties of damaged wool fibers. Text Res J 2001; 71: 885-890.
    • (2001) Text Res J , vol.71 , pp. 885-890
    • Baba, T.1    Nagasawa, N.2    Ito, H.3    Yaida, O.4    Miyamoto, T.5
  • 266
    • 84965853483 scopus 로고
    • Thermally-induced structural changes in wool
    • Menefee E, Yee G. Thermally-induced structural changes in wool. Text Res J 1965; 35: 801-812.
    • (1965) Text Res J , vol.35 , pp. 801-812
    • Menefee, E.1    Yee, G.2
  • 267
    • 84965920370 scopus 로고
    • Thermal transitions in keratin, part II: Thermal transitions in stressed keratin fibers
    • Mason P. Thermal transitions in keratin, part II: thermal transitions in stressed keratin fibers. Text Res J 1964; 34: 1021-1026.
    • (1964) Text Res J , vol.34 , pp. 1021-1026
    • Mason, P.1
  • 268
    • 84965958675 scopus 로고
    • Thermal transitions in keratin, part I: Thermal expansion and structural transitions in alpha-keratin
    • Mason P. Thermal transitions in keratin, part I: thermal expansion and structural transitions in alpha-keratin. Text Res J 1964; 34: 913-917.
    • (1964) Text Res J , vol.34 , pp. 913-917
    • Mason, P.1
  • 269
    • 0026690226 scopus 로고
    • A comparative study of the thermal stability of three different wools
    • Rama Rao D, Gupta VB. A comparative study of the thermal stability of three different wools. J Macromol Sci Phys 1992; B31(3): 319-327.
    • (1992) J Macromol Sci Phys , vol.B31 , Issue.3 , pp. 319-327
    • Rama Rao, D.1    Gupta, V.B.2
  • 270
    • 0026754931 scopus 로고
    • Thermal characteristics of wool fibers
    • Rama Rao D, Gupta VB. Thermal characteristics of wool fibers. J Macromol Sci Phys 1992; B31(2): 149-162.
    • (1992) J Macromol Sci Phys , vol.B31 , Issue.2 , pp. 149-162
    • Rama Rao, D.1    Gupta, V.B.2
  • 271
    • 0026942666 scopus 로고
    • The mechanism and stability of thermal transitions in hair keratin
    • Milczarek P, Zielinski M, Garcia ML. The mechanism and stability of thermal transitions in hair keratin. Colloid Polym Sci 1992; 270: 1106-1115.
    • (1992) Colloid Polym Sci , vol.270 , pp. 1106-1115
    • Milczarek, P.1    Zielinski, M.2    Garcia, M.L.3
  • 272
    • 84964181584 scopus 로고
    • A second order transition temperature in wool fibres in the post-yield region
    • Feughelman M, Haly AR, Rigby BJ. A second order transition temperature in wool fibres in the post-yield region. Text Res J 1959; 29: 311-313.
    • (1959) Text Res J , vol.29 , pp. 311-313
    • Feughelman, M.1    Haly, A.R.2    Rigby, B.J.3
  • 273
    • 0022024708 scopus 로고
    • Detecting a glass transition in wool by differential scanning calorimetry
    • Phillips DG. Detecting a glass transition in wool by differential scanning calorimetry. Text Res J 1985; 55: 171-174.
    • (1985) Text Res J , vol.55 , pp. 171-174
    • Phillips, D.G.1
  • 274
    • 84964171363 scopus 로고
    • The differential thermal analysis of natural and modified wool and mohair
    • Dale FELI, MCDowall MA, Eyring H. The differential thermal analysis of natural and modified wool and mohair. Text Res J 1963; 33: 465-471.
    • (1963) Text Res J , vol.33 , pp. 465-471
    • Dale, F.E.L.I.1    McDowall, M.A.2    Eyring, H.3
  • 275
    • 0021202706 scopus 로고
    • Glass transition temperature of wool as a function of regain
    • Wortmann FJ, Rigby BJ, Phillips DG. Glass transition temperature of wool as a function of regain. Text Res J 1984; 54: 6-8.
    • (1984) Text Res J , vol.54 , pp. 6-8
    • Wortmann, F.J.1    Rigby, B.J.2    Phillips, D.G.3
  • 276
    • 0023288930 scopus 로고
    • States of water sorbed on wool as studied by differential scanning calorimetry
    • Sakabe H, Ito H, Miyamoto T, Inagaki H. States of water sorbed on wool as studied by differential scanning calorimetry. Text Res J 1987; 57: 66-72.
    • (1987) Text Res J , vol.57 , pp. 66-72
    • Sakabe, H.1    Ito, H.2    Miyamoto, T.3    Inagaki, H.4
  • 277
    • 0023454472 scopus 로고
    • Thermoanalytical investigations of extended and annealed keratins
    • Spei M, Holzem R. Thermoanalytical investigations of extended and annealed keratins. Colloid Polym Sci 1987; 265: 965-970.
    • (1987) Colloid Polym Sci , vol.265 , pp. 965-970
    • Spei, M.1    Holzem, R.2
  • 278
    • 84934092934 scopus 로고
    • Thermoanalytical investigations of modified fiber keratins
    • Spei M, Hueskes R. Thermoanalytical investigations of modified fiber keratins. Melliand Textilber 1985; 66(10): 759-761.
    • (1985) Melliand Textilber , vol.66 , Issue.10 , pp. 759-761
    • Spei, M.1    Hueskes, R.2
  • 280
    • 0024680891 scopus 로고
    • Thermoanalytical determination of the relative helix content of keratins
    • Spei M, Holzem R. Thermoanalytical determination of the relative helix content of keratins. Colloid Polym Sci 1989; 267: 549-551.
    • (1989) Colloid Polym Sci , vol.267 , pp. 549-551
    • Spei, M.1    Holzem, R.2
  • 281
    • 0025454955 scopus 로고
    • Further thermoanalytical investigations of annealed keratins: The time and temperature dependence
    • Spei M, Holzem R. Further thermoanalytical investigations of annealed keratins: the time and temperature dependence. Colloid Polym Sci 1990; 268: 630-635.
    • (1990) Colloid Polym Sci , vol.268 , pp. 630-635
    • Spei, M.1    Holzem, R.2
  • 282
    • 0027909114 scopus 로고
    • Characterizing keratins using high-pressure differential scanning calorimetry
    • Wortmann FJ, Deutz H. Characterizing keratins using high-pressure differential scanning calorimetry. J Appl Polym Sci 1993; 48: 137-150.
    • (1993) J Appl Polym Sci , vol.48 , pp. 137-150
    • Wortmann, F.J.1    Deutz, H.2
  • 283
    • 0002909543 scopus 로고    scopus 로고
    • Melting study of the alpha-form crystallites in human hair keratin by DSC
    • Cao J. Melting study of the alpha-form crystallites in human hair keratin by DSC. Thermochim Acta 1999; 335: 5-9.
    • (1999) Thermochim Acta , vol.335 , pp. 5-9
    • Cao, J.1
  • 284
    • 78549239822 scopus 로고    scopus 로고
    • Differential scanning calorimetry (DSC) study of hair damage and hair restructuring by protein derivatives
    • Gao T, Bedell A. Differential scanning calorimetry (DSC) study of hair damage and hair restructuring by protein derivatives. J Cosmet Sci 2001; 52: 332-333.
    • (2001) J Cosmet Sci , vol.52 , pp. 332-333
    • Gao, T.1    Bedell, A.2
  • 285
    • 0036653776 scopus 로고    scopus 로고
    • Investigations of cosmetically treated human hair by differential scanning calorimetry in water
    • Wortmann FJ, Springob C, Sendelbach G. Investigations of cosmetically treated human hair by differential scanning calorimetry in water. J Cosmet Sci 2002; 53: 219-228.
    • (2002) J Cosmet Sci , vol.53 , pp. 219-228
    • Wortmann, F.J.1    Springob, C.2    Sendelbach, G.3
  • 286
    • 0000023451 scopus 로고
    • Electrical conduction of textiles
    • Baxter S. Electrical conduction of textiles. Trans Faraday Soc 1943; 39: 207-214.
    • (1943) Trans Faraday Soc , vol.39 , pp. 207-214
    • Baxter, S.1
  • 287
    • 0008684445 scopus 로고
    • The electrical resistance of wool fibres
    • Marsh MC, Earp K. The electrical resistance of wool fibres. Trans Faraday Soc 1933; 29: 173-193.
    • (1933) Trans Faraday Soc , vol.29 , pp. 173-193
    • Marsh, M.C.1    Earp, K.2
  • 288
    • 0008708737 scopus 로고
    • Conduction in textiles, part I: The dependence of the resistivity of cotton silk and wool on relative humidity and moisture content
    • Murphy EJ, Walker AC. Conduction in textiles, part I: the dependence of the resistivity of cotton silk and wool on relative humidity and moisture content. J Phys Chem 1928; 32: 1761-1786.
    • (1928) J Phys Chem , vol.32 , pp. 1761-1786
    • Murphy, E.J.1    Walker, A.C.2
  • 289
    • 49549126525 scopus 로고
    • Ionic conduction in keratin (wool)
    • Murphy EJ. Ionic conduction in keratin (wool). J Colloid Interf Sci 1976; 54(3): 400-408.
    • (1976) J Colloid Interf Sci , vol.54 , Issue.3 , pp. 400-408
    • Murphy, E.J.1
  • 290
    • 84965945598 scopus 로고
    • The variation of electrical resistance with strain of keratin fibers with constant water content
    • Algie JE. The variation of electrical resistance with strain of keratin fibers with constant water content. Text Res J 1964; 34: 273-274.
    • (1964) Text Res J , vol.34 , pp. 273-274
    • Algie, J.E.1
  • 291
    • 0018795026 scopus 로고
    • L’eau dans les kératines: Étude par mesures de la conductibilité électrique
    • Levêque JL, Garson JC, Boudouris G. L’eau dans les kératines: étude par mesures de la conductibilité électrique. CR Acad Sci 1979; 288: 1679-1682.
    • (1979) CR Acad Sci , vol.288 , pp. 1679-1682
    • Levêque, J.L.1    Garson, J.C.2    Boudouris, G.3
  • 293
    • 0344789867 scopus 로고
    • The effect of strain on the electrical resistance of keratin
    • Algie JE. The effect of strain on the electrical resistance of keratin. Text Res J 1959; 29: 1-6.
    • (1959) Text Res J , vol.29 , pp. 1-6
    • Algie, J.E.1
  • 294
    • 0242289869 scopus 로고
    • Some dielectric properties of dry keratin
    • Algie JE. Some dielectric properties of dry keratin. Kolloid zz Polym 1967; 223(1): 13-23.
    • (1967) Kolloid zz Polym , vol.223 , Issue.1 , pp. 13-23
    • Algie, J.E.1
  • 295
    • 0002567196 scopus 로고
    • Dielectric properties of wool and horn containing absorbed water
    • Algie JE, Gamble RA. Dielectric properties of wool and horn containing absorbed water. Kolloid zz Polym 1973; 251: 554-562.
    • (1973) Kolloid zz Polym , vol.251 , pp. 554-562
    • Algie, J.E.1    Gamble, R.A.2
  • 296
    • 0346009823 scopus 로고
    • Dielectric properties of wool-water systems at 3000 and 9300 megacycles
    • Windle JJ, Shaw TM. Dielectric properties of wool-water systems at 3000 and 9300 megacycles. J Chem Phys 1954; 22(10): 1752-1756.
    • (1954) J Chem Phys , vol.22 , Issue.10 , pp. 1752-1756
    • Windle, J.J.1    Shaw, T.M.2
  • 297
    • 36849119225 scopus 로고
    • Dielectric properties of wool-water systems, part II: 26000 megacycles
    • Windle JJ, Shaw TM. Dielectric properties of wool-water systems, part II: 26000 megacycles. J Chem Phys 1956; 25(3): 435-439.
    • (1956) J Chem Phys , vol.25 , Issue.3 , pp. 435-439
    • Windle, J.J.1    Shaw, T.M.2
  • 298
    • 0014585752 scopus 로고
    • Some dielectric properties of wool
    • Algie JE. Some dielectric properties of wool. Kolloid zz Polym 1969; 234(2): 1069-1078.
    • (1969) Kolloid zz Polym , vol.234 , Issue.2 , pp. 1069-1078
    • Algie, J.E.1
  • 299
    • 84965954627 scopus 로고
    • Dielectric constant and conductance changes in wool fibers produced by step changes in the relative humidity
    • Algie JE. Dielectric constant and conductance changes in wool fibers produced by step changes in the relative humidity. Text Res J 1964; 34: 477-486.
    • (1964) Text Res J , vol.34 , pp. 477-486
    • Algie, J.E.1
  • 300
    • 0016079813 scopus 로고
    • Depolarization thermal currents in keratin fibers
    • Levêque JL, Garson JC, Boudouris G. Depolarization thermal currents in keratin fibers. Text Res J 1974; 44: 504-505.
    • (1974) Text Res J , vol.44 , pp. 504-505
    • Levêque, J.L.1    Garson, J.C.2    Boudouris, G.3
  • 301
    • 0017375217 scopus 로고
    • Water in keratin: Study of the depolarization thermal current peak II
    • Levêque JL, Garson JC, Boudouris G. Water in keratin: study of the depolarization thermal current peak II. Biopolymers 1977; 16: 1725-1733.
    • (1977) Biopolymers , vol.16 , pp. 1725-1733
    • Levêque, J.L.1    Garson, J.C.2    Boudouris, G.3
  • 302
    • 0019841713 scopus 로고
    • Free water in hair keratin? A depolarization thermal-current study
    • Levêque JL, Garson JC, Boudouris G. Free water in hair keratin? A depolarization thermal-current study. Biopolymers 1981; 20: 2649-2656.
    • (1981) Biopolymers , vol.20 , pp. 2649-2656
    • Levêque, J.L.1    Garson, J.C.2    Boudouris, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.