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Volumn 5, Issue 7, 2006, Pages 698-706

Characterisation of photo-oxidation products within photoyellowed wool proteins: Tryptophan and tyrosine derived chromophores

Author keywords

[No Author keywords available]

Indexed keywords

5 HYDROXYTRYPTOPHAN; DITYROSINE DERIVATIVE; DOPA; FORMYLKYNURENINE; KYNURENINE; PROTEIN; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG; WOOL PROTEIN;

EID: 33745728806     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/b603030k     Document Type: Article
Times cited : (101)

References (69)
  • 1
    • 0141628349 scopus 로고    scopus 로고
    • Chemical and photo-oxidative hair damage studied by dye diffusion and electrophoresis
    • S. B. Ruetsch B. Yang Y. K. Yamath Chemical and photo-oxidative hair damage studied by dye diffusion and electrophoresis Cosmet. Sci. 2003 54 379-394.
    • (2003) Cosmet. Sci. , vol.54 , pp. 379-394
    • Ruetsch, S.B.1    Yang, B.2    Yamath, Y.K.3
  • 2
    • 3142718195 scopus 로고    scopus 로고
    • 3-hydroxypyridine chromophores are endogenous sensitizers of photooxidative stress in human skin cells
    • G. T. Wondrak M. J. Roberts M. K. Jacobson E. L. Jacobson 3-hydroxypyridine chromophores are endogenous sensitizers of photooxidative stress in human skin cells J. Biol. Chem. 2004 279 30009-30020.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30009-30020
    • Wondrak, G.T.1    Roberts, M.J.2    Jacobson, M.K.3    Jacobson, E.L.4
  • 5
    • 0032985811 scopus 로고    scopus 로고
    • Protection against UVB inactivation (In vitro) of rat lens enzymes by natural antioxidants
    • G. B. Reddy K. S. Bhat Protection against UVB inactivation (in vitro) of rat lens enzymes by natural antioxidants Mol. Cell. Biochem. 1999 194 41-45.
    • (1999) Mol. Cell. Biochem. , vol.194 , pp. 41-45
    • Reddy, G.B.1    Bhat, K.S.2
  • 6
    • 0037492957 scopus 로고    scopus 로고
    • Molecular dynamics study of early events during photooxidation of eye lens protein gamma-beta crystallin
    • K. Kubiak M. Kowalska W. Nowak Molecular dynamics study of early events during photooxidation of eye lens protein gamma-beta crystallin J. Mol. Struct. (THEOCHEM) 2003 630 315-325.
    • (2003) J. Mol. Struct. (THEOCHEM) , vol.630 , pp. 315-325
    • Kubiak, K.1    Kowalska, M.2    Nowak, W.3
  • 7
    • 16644388652 scopus 로고    scopus 로고
    • The damaging effect of UV-C irradiation on lens alpha-crystallin
    • N. Fujii H. Uchida T. Saito The damaging effect of UV-C irradiation on lens alpha-crystallin Mol. Vis. 2004 10 814-820.
    • (2004) Mol. Vis. , vol.10 , pp. 814-820
    • Fujii, N.1    Uchida, H.2    Saito, T.3
  • 8
    • 0000394046 scopus 로고
    • Ultraviolet radiation and plants: Burning questions
    • A. E. Stapleton Ultraviolet radiation and plants: Burning questions Plant Cell 1992 4 1353-1358.
    • (1992) Plant Cell , vol.4 , pp. 1353-1358
    • Stapleton, A.E.1
  • 9
    • 0000019999 scopus 로고
    • Ultraviolet-induced photodegradation of cucumber (Cucumis sativus L.) microsomal and soluble protein tryptophanyl residues in vitro
    • C. R. Caldwell Ultraviolet-induced photodegradation of cucumber (Cucumis sativus L.) microsomal and soluble protein tryptophanyl residues in vitro Plant Physiol. 1993 101 947-953.
    • (1993) Plant Physiol. , vol.101 , pp. 947-953
    • Caldwell, C.R.1
  • 10
    • 0001835116 scopus 로고    scopus 로고
    • Tryptophan photolysis leads to a UVB-induced 66 kD photoproduct of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in vitro and in vivo
    • K. E. Gerhardt M. I. Wilson B. M. Greenberg Tryptophan photolysis leads to a UVB-induced 66 kD photoproduct of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) in vitro and in vivo Photochem. Photobiol. 1999 70 49-56.
    • (1999) Photochem. Photobiol. , vol.70 , pp. 49-56
    • Gerhardt, K.E.1    Wilson, M.I.2    Greenberg, B.M.3
  • 11
    • 0023992403 scopus 로고
    • Possible long-term changes in biologically active ultraviolet radiation reaching the ground
    • J. E. Frederick D. Lubin Possible long-term changes in biologically active ultraviolet radiation reaching the ground Photochem. Photobiol. 1988 47 571-578.
    • (1988) Photochem. Photobiol. , vol.47 , pp. 571-578
    • Frederick, J.E.1    Lubin, D.2
  • 13
    • 84970166853 scopus 로고
    • The photochemical oxidation of wool in the presence of fluorescent compounds
    • D. Graham K. Statham The photochemical oxidation of wool in the presence of fluorescent compounds J. Soc. Dyers Colour 1956 72 434-438.
    • (1956) J. Soc. Dyers Colour , vol.72 , pp. 434-438
    • Graham, D.1    Statham, K.2
  • 14
    • 0017533121 scopus 로고
    • The formation of carbonyl groups during irradiation of wool and its relevance to photoyellowing
    • L. A. Holt B. Milligan The formation of carbonyl groups during irradiation of wool and its relevance to photoyellowing Text. Res. J. 1977 47 620-624.
    • (1977) Text. Res. J. , vol.47 , pp. 620-624
    • Holt, L.A.1    Milligan, B.2
  • 15
    • 0005168387 scopus 로고
    • Sunlight yellowing of white wool: A complex problem
    • South African Wool and Textile Research Institute of the Council for Scientific and Industrial Research, Pretoria, South Africa
    • B. Milligan, Sunlight yellowing of white wool: A complex problem, in Proc. 6th Int. Wool Text. Res. Conf., South African Wool and Textile Research Institute of the Council for Scientific and Industrial Research, Pretoria, South Africa, 1980, pp. 167–181.
    • (1980) Proc. 6th Int. Wool Text. Res. Conf. , pp. 167-181
    • Milligan, B.1
  • 17
    • 0002452246 scopus 로고
    • Chemical structure of chromophores formed during photoyellowing of wool
    • The Society of Fiber Science and Technology, Tokyo, Japan
    • K. Roper, and E. Finnimore, Chemical structure of chromophores formed during photoyellowing of wool, in Proc. 7th Int. Wool Text. Res. Conf., The Society of Fiber Science and Technology, Tokyo, Japan, 1985, pp. 21–30.
    • (1985) Proc. 7th Int. Wool Text. Res. Conf. , pp. 21-30
    • Roper, K.1    Finnimore, E.2
  • 19
    • 0006593626 scopus 로고
    • Effects of ultraviolet radiation as related to the yellowing of wool
    • R. S. Asquith, L. Hirst and D. E. Rivett, Effects of ultraviolet radiation as related to the yellowing of wool, in Applied Polymer Symposium, 1971, pp. 333–335.
    • (1971) Applied Polymer Symposium , pp. 333-335
    • Asquith, R.S.1    Hirst, L.2    Rivett, D.E.3
  • 20
    • 0015135793 scopus 로고
    • Studies on the photooxidation of tryptophan
    • R. S. Asquith D. E. Rivett Studies on the photooxidation of tryptophan Biochim. Biophys. Acta 1971 252 111-116.
    • (1971) Biochim. Biophys. Acta , vol.252 , pp. 111-116
    • Asquith, R.S.1    Rivett, D.E.2
  • 21
    • 0005227479 scopus 로고    scopus 로고
    • Identification of the sites of hydroxyl radical reaction with peptides by hydrogen/deuterium exchange: Prevalence of reactions with the side chains
    • M. B. Goshe Y. H. Chen V. E. Anderson Identification of the sites of hydroxyl radical reaction with peptides by hydrogen/deuterium exchange: Prevalence of reactions with the side chains Biochemistry 2000 39 1761-1770.
    • (2000) Biochemistry , vol.39 , pp. 1761-1770
    • Goshe, M.B.1    Chen, Y.H.2    Anderson, V.E.3
  • 22
    • 0042699132 scopus 로고
    • Yellowing of wool keratin on exposure to ultraviolet radiation
    • R. S. Asquith K. E. Brooke Yellowing of wool keratin on exposure to ultraviolet radiation J. Soc. Dyers Colour 1968 84 159-165.
    • (1968) J. Soc. Dyers Colour , vol.84 , pp. 159-165
    • Asquith, R.S.1    Brooke, K.E.2
  • 23
    • 0014537639 scopus 로고
    • The photolysis of tyrosine and its possible relationship to the yellowing of wool
    • R. S. Asquith D. E. Rivett The photolysis of tyrosine and its possible relationship to the yellowing of wool Text. Res. J. 1969 39 633-637.
    • (1969) Text. Res. J. , vol.39 , pp. 633-637
    • Asquith, R.S.1    Rivett, D.E.2
  • 24
    • 84970442677 scopus 로고
    • Fluorescence and phosphorescence of wool keratin excited by UV-A radiation
    • G. J. Smith W. H. Melhuish Fluorescence and phosphorescence of wool keratin excited by UV-A radiation Text. Res. J. 1985 55 304-307.
    • (1985) Text. Res. J. , vol.55 , pp. 304-307
    • Smith, G.J.1    Melhuish, W.H.2
  • 25
    • 0025957980 scopus 로고
    • The natural fluorescence of wool
    • K. Schäfer The natural fluorescence of wool J. Soc. Dyers Colour 1991 107 206-211.
    • (1991) J. Soc. Dyers Colour , vol.107 , pp. 206-211
    • Schäfer, K.1
  • 26
    • 33746609431 scopus 로고
    • Origins of variation in the fluorescence patterns of wool and wool proteins
    • Citta degli Studi Biella and International Wool Secrariat, Biella, Italy
    • W. S. Simpson, Origins of variation in the fluorescence patterns of wool and wool proteins, in Proc. 9th Int. Wool Text. Res. Conf., 1995, Citta degli Studi Biella and International Wool Secrariat, Biella, Italy, pp. 429–439.
    • (1995) Proc. 9th Int. Wool Text. Res. Conf. , pp. 429-439
    • Simpson, W.S.1
  • 28
    • 0000217491 scopus 로고    scopus 로고
    • Oxidation of free tryptophan and tryptophan residues in peptides and proteins
    • T. J. Simat H. Steinhart Oxidation of free tryptophan and tryptophan residues in peptides and proteins J. Agric. Food Chem. 1998 46 490-498.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 490-498
    • Simat, T.J.1    Steinhart, H.2
  • 29
    • 84964183112 scopus 로고
    • Studies in wool yellowing. Part IV: Changes in amino acid composition due to irradiation
    • A. S. Inglis F. G. Lennox Studies in wool yellowing. Part IV: Changes in amino acid composition due to irradiation Text. Res. J. 1963 33 431-434.
    • (1963) Text. Res. J. , vol.33 , pp. 431-434
    • Inglis, A.S.1    Lennox, F.G.2
  • 30
    • 0017017063 scopus 로고
    • Primary reactions in the photoyellowing of wool keratin
    • C. Nicholls M. Pailthorpe Primary reactions in the photoyellowing of wool keratin J. Text. Inst. 1976 67 397-403.
    • (1976) J. Text. Inst. , vol.67 , pp. 397-403
    • Nicholls, C.1    Pailthorpe, M.2
  • 32
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • B. S. Berlett E. R. Stadtman Protein oxidation in aging, disease, and oxidative stress J. Biol. Chem. 1997 272 20313-20316.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 33
    • 0034480310 scopus 로고    scopus 로고
    • Electrospray mass and tandem mass spectrometry identification of ozone oxidation products of amino acids and small peptides
    • T. Kotiaho M. N. Eberlin P. Vainiotalo R. Kostiainen Electrospray mass and tandem mass spectrometry identification of ozone oxidation products of amino acids and small peptides J. Am. Soc. Mass Spectrom. 2000 11 526-535.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 526-535
    • Kotiaho, T.1    Eberlin, M.N.2    Vainiotalo, P.3    Kostiainen, R.4
  • 35
    • 84987419408 scopus 로고
    • Proposal for a common nomenclature for sequence ions in mass spectra of peptides
    • P. Roepstorff J. Fohlman Proposal for a common nomenclature for sequence ions in mass spectra of peptides Biomed. Mass Spectrom. 1984 11 601.
    • (1984) Biomed. Mass Spectrom. , vol.11 , pp. 601
    • Roepstorff, P.1    Fohlman, J.2
  • 36
    • 0023449998 scopus 로고
    • Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: Differentiation of leucine and isoleucine
    • R. Johnson S. Martin K. Biemann J. Stults J. T. Watson Novel fragmentation process of peptides by collision-induced decomposition in a tandem mass spectrometer: Differentiation of leucine and isoleucine Anal. Chem. 1987 59 2621-2625.
    • (1987) Anal. Chem. , vol.59 , pp. 2621-2625
    • Johnson, R.1    Martin, S.2    Biemann, K.3    Stults, J.4    Watson, J.T.5
  • 37
    • 0023804303 scopus 로고
    • Contributions of mass spectrometry to peptide and protein structure
    • K. Biemann Contributions of mass spectrometry to peptide and protein structure Biomed. Environ. Mass Spectrom. 1988 16 99-111.
    • (1988) Biomed. Environ. Mass Spectrom. , vol.16 , pp. 99-111
    • Biemann, K.1
  • 39
    • 3042544639 scopus 로고    scopus 로고
    • The generation of superoxide and hydrogen peroxide by exposure of fluorescent whitening agents to UVA radiation and its relevance to the rapid photoyellowing of whitened wool
    • K. R. Millington G. Maurdev The generation of superoxide and hydrogen peroxide by exposure of fluorescent whitening agents to UVA radiation and its relevance to the rapid photoyellowing of whitened wool J. Photochem. Photobiol., A 2004 165 177-185.
    • (2004) J. Photochem. Photobiol., A , vol.165 , pp. 177-185
    • Millington, K.R.1    Maurdev, G.2
  • 40
    • 0036183624 scopus 로고    scopus 로고
    • Detection of hydroxyl radicals in photoirradiated wool, cotton, nylon and polyester fabrics using a fluorescent probe
    • K. R. Millington L. J. Kirschenbaum Detection of hydroxyl radicals in photoirradiated wool, cotton, nylon and polyester fabrics using a fluorescent probe Color. Tech. 2002 118 6-14.
    • (2002) Color. Tech. , vol.118 , pp. 6-14
    • Millington, K.R.1    Kirschenbaum, L.J.2
  • 41
    • 15844394137 scopus 로고    scopus 로고
    • Reactive oxygen species, aging, and antioxidative nutraceuticals
    • L. Lee N. Koo D. B. Min Reactive oxygen species, aging, and antioxidative nutraceuticals Compr. Rev. Food Sci. Food Safety 2004 3 21-33.
    • (2004) Compr. Rev. Food Sci. Food Safety , vol.3 , pp. 21-33
    • Lee, L.1    Koo, N.2    Min, D.B.3
  • 43
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • R. T. Dean S. Fu R. Stocker M. J. Davies Biochemistry and pathology of radical-mediated protein oxidation Biochem. J. 1997 324 1-18.
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 46
    • 0030832112 scopus 로고    scopus 로고
    • Different kynurenine pathway enzymes limit quinolinic acid formation by various human cell types
    • M. P. Heyes C. Y. Chen E. O. Major K. Saito Different kynurenine pathway enzymes limit quinolinic acid formation by various human cell types Biochem. J. 1997 326 Pt 2 351-356.
    • (1997) Biochem. J. , vol.326 , pp. 351-356
    • Heyes, M.P.1    Chen, C.Y.2    Major, E.O.3    Saito, K.4
  • 47
    • 0033974564 scopus 로고    scopus 로고
    • Non-oxidative modification of lens crystallins by kynurenine: A novel post-translational protein modification with possible relevance to ageing and cataract
    • B. Garner D. C. Shaw R. A. Lindner J. A. Carver R. J. Truscott Non-oxidative modification of lens crystallins by kynurenine: a novel post-translational protein modification with possible relevance to ageing and cataract Biochim. Biophys. Acta 2000 1476 265-278.
    • (2000) Biochim. Biophys. Acta , vol.1476 , pp. 265-278
    • Garner, B.1    Shaw, D.C.2    Lindner, R.A.3    Carver, J.A.4    Truscott, R.J.5
  • 49
    • 33646235182 scopus 로고    scopus 로고
    • Determination of photo-oxidation products within photoyellowed bleached wool proteins
    • J. M. Dyer S. D. Bringans W. G. Bryson Determination of photo-oxidation products within photoyellowed bleached wool proteins Photochem. Photobiol. 2006 82 551-7.
    • (2006) Photochem. Photobiol. , vol.82 , pp. 551-557
    • Dyer, J.M.1    Bringans, S.D.2    Bryson, W.G.3
  • 50
    • 33646235078 scopus 로고    scopus 로고
    • Kynurenine located within keratin proteins isolated from photoyellowed wool fabric
    • S. D. Bringans J. M. Dyer J. E. Plowman W. G. Bryson Kynurenine located within keratin proteins isolated from photoyellowed wool fabric Text. Res. J. 2006 76 288-294.
    • (2006) Text. Res. J. , vol.76 , pp. 288-294
    • Bringans, S.D.1    Dyer, J.M.2    Plowman, J.E.3    Bryson, W.G.4
  • 51
    • 0346456881 scopus 로고    scopus 로고
    • Fluorogenic peptide sequences - Transformation of short peptides into fluorophores under ambient photo-oxidative conditions
    • G. L. Juskowiak S. J. Stachel P. Tivitmahaisoon D. L. Van Vranken Fluorogenic peptide sequences - Transformation of short peptides into fluorophores under ambient photo-oxidative conditions J. Am. Chem. Soc. 2004 126 550-556.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 550-556
    • Juskowiak, G.L.1    Stachel, S.J.2    Tivitmahaisoon, P.3    Van Vranken, D.L.4
  • 52
    • 0015106948 scopus 로고
    • Formation and breakdown of the inner root sheath and features of the pilary canal epithelium in the wool follicle
    • R. Gemmell R. Chapman Formation and breakdown of the inner root sheath and features of the pilary canal epithelium in the wool follicle J. Ultrastruct. Res. 1971 36 355-366.
    • (1971) J. Ultrastruct. Res. , vol.36 , pp. 355-366
    • Gemmell, R.1    Chapman, R.2
  • 53
    • 0022011744 scopus 로고
    • Cellular debris in the grease of wool fibres
    • D. Orwin J. L. Woods Cellular debris in the grease of wool fibres Text. Res. J. 1985 55 84-92.
    • (1985) Text. Res. J. , vol.55 , pp. 84-92
    • Orwin, D.1    Woods, J.L.2
  • 54
    • 0027568250 scopus 로고
    • Production of 14C-labeled 3-hydroxy-L-kynurenine in a butterfly, Heliconius charitonia L. (Heliconidae), and precursor studies in butterfly wing ommatins
    • P. B. Koch Production of 14C-labeled 3-hydroxy-L-kynurenine in a butterfly, Heliconius charitonia L. (Heliconidae), and precursor studies in butterfly wing ommatins Pigm. Cell Res. 1993 6 85-90.
    • (1993) Pigm. Cell Res. , vol.6 , pp. 85-90
    • Koch, P.B.1
  • 55
    • 0009445105 scopus 로고    scopus 로고
    • Ommochrome pigmentation of the linea and rosa seasonal forms of Precis coenia (Lepidoptera: Nymphalidae)
    • H. F. Nijhout Ommochrome pigmentation of the linea and rosa seasonal forms of Precis coenia (Lepidoptera: Nymphalidae) Arch. Insect Biochem. Physiol. 1997 36 215-222.
    • (1997) Arch. Insect Biochem. Physiol. , vol.36 , pp. 215-222
    • Nijhout, H.F.1
  • 56
    • 0018236590 scopus 로고
    • Xanthomatin biosynthesis in wild-type and mutant strains of Australian sheep blowfly Lucilia cuprina
    • K. M. Summers A. J. Howells Xanthomatin biosynthesis in wild-type and mutant strains of Australian sheep blowfly Lucilia cuprina Biochem. Genet. 1978 16 1153-1163.
    • (1978) Biochem. Genet. , vol.16 , pp. 1153-1163
    • Summers, K.M.1    Howells, A.J.2
  • 58
    • 0027297225 scopus 로고
    • The modification of proteins by 3-hydroxykynurenine
    • G. M. Stutchbury R. J. Truscott The modification of proteins by 3-hydroxykynurenine Exp. Eye Res. 1993 2 149-155.
    • (1993) Exp. Eye Res. , vol.2 , pp. 149-155
    • Stutchbury, G.M.1    Truscott, R.J.2
  • 59
    • 0032731157 scopus 로고    scopus 로고
    • Human lens coloration and aging. Evidence for crystallin modification by the major ultraviolet filter, 3-hydroxy-kynurenine O-beta-D-glucoside
    • B. D. Hood B. Garner R. J. Truscott Human lens coloration and aging. Evidence for crystallin modification by the major ultraviolet filter, 3-hydroxy-kynurenine O-beta-D-glucoside J. Biol. Chem. 1999 274 32547-32550.
    • (1999) J. Biol. Chem. , vol.274 , pp. 32547-32550
    • Hood, B.D.1    Garner, B.2    Truscott, R.J.3
  • 60
    • 0344293324 scopus 로고
    • Phenylalanine and tyrosine - two aromatic amino acids involved in the photoyellowing of wool
    • D. Godinger K. Schäfer H. Hocker Phenylalanine and tyrosine - two aromatic amino acids involved in the photoyellowing of wool Wool Tech. Sheep Breed. 1994 42 83-89.
    • (1994) Wool Tech. Sheep Breed. , vol.42 , pp. 83-89
    • Godinger, D.1    Schäfer, K.2    Hocker, H.3
  • 61
    • 8644286364 scopus 로고    scopus 로고
    • O-Tyrosine hydroxylation by OH radicals. 2,3,-DOPA and 2,5-DOPA formation in gamma-irradiated aqueous solution
    • H. Zegota K. Kolodziejczyk M. Krol B. Krol o-Tyrosine hydroxylation by OH radicals. 2,3,-DOPA and 2,5-DOPA formation in gamma-irradiated aqueous solution Radiat. Phys. Chem. 2005 72 25-33.
    • (2005) Radiat. Phys. Chem. , vol.72 , pp. 25-33
    • Zegota, H.1    Kolodziejczyk, K.2    Krol, M.3    Krol, B.4
  • 63
    • 0029557684 scopus 로고
    • Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds I and II. Implications, for lipoprotein peroxidation studies
    • L. A. Marquez H. B. Dunford Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds I and II. Implications, for lipoprotein peroxidation studies J. Biol. Chem. 1995 270 30434-30440.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30434-30440
    • Marquez, L.A.1    Dunford, H.B.2
  • 64
    • 0014064318 scopus 로고
    • Ultraviolet irradiation effects in poly-L-tyrosine and model compounds. Identification of bityrosine as a photoproduct
    • S. S. Lehrer G. D. Fasman Ultraviolet irradiation effects in poly-L-tyrosine and model compounds. Identification of bityrosine as a photoproduct Biochemistry 1967 6 757-767.
    • (1967) Biochemistry , vol.6 , pp. 757-767
    • Lehrer, S.S.1    Fasman, G.D.2
  • 65
    • 0027160097 scopus 로고
    • Structure, function, and dynamics of keratin intermediate filaments
    • P. M. Steinert Structure, function, and dynamics of keratin intermediate filaments J. Invest. Dermatol. 1993 100 729-734.
    • (1993) J. Invest. Dermatol. , vol.100 , pp. 729-734
    • Steinert, P.M.1
  • 66
    • 2542432658 scopus 로고    scopus 로고
    • Toward the atomic details of intermediate filament structure, assembly and dynamics
    • Deutsches Wollforschungsinstitut an der RWTH Aachen e.V, Aachen, Germany
    • S. V. Strelkov, H. Herrmann, N. Geisler, R. Zimbelmann, P. Burkhard, and U. Aebi, Toward the atomic details of intermediate filament structure, assembly and dynamics, in Proc. 10th Int. Wool Text. Res. Conf., Deutsches Wollforschungsinstitut an der RWTH Aachen e.V, Aachen, Germany, 2000, pp. KNL-4 1-11.
    • (2000) Proc. 10th Int. Wool Text. Res. Conf. , pp. 11
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Zimbelmann, R.4    Burkhard, P.5    Aebi, U.6
  • 67
    • 0004941651 scopus 로고
    • Crimping of wool fibres
    • M. Horio T. Kondo Crimping of wool fibres Text. Res. J. 1953 23 373-387.
    • (1953) Text. Res. J. , vol.23 , pp. 373-387
    • Horio, M.1    Kondo, T.2
  • 68
    • 85007539386 scopus 로고    scopus 로고
    • access via
    • Swiss-Prot database, access via http://us.expasy.org/sprot/.
    • Swiss-Prot Database
  • 69
    • 0030636267 scopus 로고    scopus 로고
    • The role of keratin proteins and their genes in the growth, structure and properties of hair
    • P. Jolláes, H. Zahn and H. Hèocker, Birkhäuser Verlag, Basel, Switzerland, 1st edn
    • B. C. Powell, and G. E. Rogers, The role of keratin proteins and their genes in the growth, structure and properties of hair, in Formation and structure of human hair, ed. P. Jolláes, H. Zahn and H. Hèocker, Birkhäuser Verlag, Basel, Switzerland, 1st edn, 1997, pp. 59–148.
    • (1997) Formation and Structure of Human Hair , pp. 59-148
    • Powell, B.C.1    Rogers, G.E.2


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