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Volumn 16, Issue 12, 2007, Pages 961-976

Hard cornification in reptilian epidermis in comparison to cornification in mammalian epidermis

Author keywords

Amniote cornification; Beta keratins; Epidermis; Keratin associated proteins; Reptiles

Indexed keywords

AMINO ACID; CYTOKERATIN; GLYCINE; KERATIN; MATRIX PROTEIN; MESSENGER RNA; NUCLEOTIDE; PROLINE; SERINE; SULFUR; TYROSINE;

EID: 36448947235     PISSN: 09066705     EISSN: 16000625     Source Type: Journal    
DOI: 10.1111/j.1600-0625.2007.00609.x     Document Type: Review
Times cited : (48)

References (66)
  • 2
    • 0002102286 scopus 로고
    • When? Why? and How? Some speculations on the evolution of the vertebrate integument
    • Maderson P F A. When? Why? and How? Some speculations on the evolution of the vertebrate integument. Am Zool 1972: 12: 159-171.
    • (1972) Am Zool , vol.12 , pp. 159-171
    • Maderson, P.F.A.1
  • 3
    • 0042674063 scopus 로고    scopus 로고
    • Mammalian skin evolution: A reevaluation
    • Maderson P F A. Mammalian skin evolution: A reevaluation. Exp Dermatol 2003: 12: 233-236.
    • (2003) Exp Dermatol , vol.12 , pp. 233-236
    • Maderson, P.F.A.1
  • 4
    • 4344691326 scopus 로고    scopus 로고
    • Dermo-epidermal interactions in reptilian scales: Speculations on the evolution of scales, feathers, and hairs
    • Alibardi L. Dermo-epidermal interactions in reptilian scales: speculations on the evolution of scales, feathers, and hairs. J Exp Zool 2004: 302B: 365-383.
    • (2004) J Exp Zool , vol.302 B , pp. 365-383
    • Alibardi, L.1
  • 7
    • 0036468732 scopus 로고    scopus 로고
    • 'Hard'and 'soft'principles defining the structure, function and regulation of keratin intermediate filaments
    • Coulombe P A, Omary M B. 'Hard'and 'soft'principles defining the structure, function and regulation of keratin intermediate filaments. Curr Opin Cell Biol 2002: 14: 110-122.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 110-122
    • Coulombe, P.A.1    Omary, M.B.2
  • 9
    • 0000757837 scopus 로고
    • Some developmental problems of the reptilian integument
    • In: Gans C, Billett F, Maderson P F, eds. New York: John Wiley & Sons
    • Maderson P F. Some developmental problems of the reptilian integument. In: Gans C, Billett F, Maderson P F, eds. Biology of Reptilia. New York: John Wiley & Sons, 1985: 525-598.
    • (1985) Biology of Reptilia , pp. 525-598
    • Maderson, P.F.1
  • 10
    • 0003356974 scopus 로고
    • The skin of Reptiles: Epidermis and dermis
    • In: Bereither-Hahn J, Matoltsy G, Sylvia-Richards K, eds. Berlin-Heidelberg-New York: Springer Verlag
    • Landmann L. The skin of Reptiles: Epidermis and dermis. In: Bereither-Hahn J, Matoltsy G, Sylvia-Richards K, eds. Biology of the Integument, Vertebrate. Berlin-Heidelberg-New York: Springer Verlag, 1986: 150-187.
    • (1986) Biology of the Integument, Vertebrate , pp. 150-187
    • Landmann, L.1
  • 11
    • 33847244108 scopus 로고    scopus 로고
    • The expression of beta (b) keratins in the epidermal appendages of reptiles and birds
    • Sawyer R H, Glenn T C, French J O et al. The expression of beta (b) keratins in the epidermal appendages of reptiles and birds. Amer Zool 2000: 40: 530-539.
    • (2000) Amer Zool , vol.40 , pp. 530-539
    • Sawyer, R.H.1    Glenn, T.C.2    French, J.O.3
  • 12
    • 0037096038 scopus 로고    scopus 로고
    • Immunocytochemical analysis of beta keratins in the epidermis of chelonians, lepidosaurians, and archosaurians
    • Alibardi L, Sawyer R H. Immunocytochemical analysis of beta keratins in the epidermis of chelonians, lepidosaurians, and archosaurians. J Exp Zool 2002: 293: 27-38.
    • (2002) J Exp Zool , vol.293 , pp. 27-38
    • Alibardi, L.1    Sawyer, R.H.2
  • 13
    • 0142119328 scopus 로고    scopus 로고
    • Adaptation to the land: The skin of reptiles in comparison to that of amphibians and endotherm amniotes
    • Alibardi L. Adaptation to the land: The skin of reptiles in comparison to that of amphibians and endotherm amniotes. J Exp Zoolog B Mol Dev Evol 2003: 298: 12-41.
    • (2003) J Exp Zoolog B Mol Dev Evol , vol.298 , pp. 12-41
    • Alibardi, L.1
  • 14
    • 0000370823 scopus 로고
    • The structural proteins of hair: Isolation, characterization and regulation of biosynthesis
    • In: Goldsmith L, ed. Oxford: Oxford University Press
    • Gillespie J M. The structural proteins of hair: Isolation, characterization and regulation of biosynthesis. In: Goldsmith L, ed. Physiology, Biochemistry and Molecular Biology of the Skin. Oxford: Oxford University Press, 1991: 625-659.
    • (1991) Physiology, Biochemistry and Molecular Biology of the Skin , pp. 625-659
    • Gillespie, J.M.1
  • 15
    • 0000634906 scopus 로고
    • Differentiation in hard keratin tissues: Hair and related structure
    • In: Leigh I, Lane B, Watt F, eds. Cambridge, UK: Cambridge University Press
    • Powell B, Rogers G. Differentiation in hard keratin tissues: Hair and related structure. In: Leigh I, Lane B, Watt F, eds. The Keratinocyte Handbook. Cambridge, UK: Cambridge University Press, 1994: 401-436.
    • (1994) The Keratinocyte Handbook , pp. 401-436
    • Powell, B.1    Rogers, G.2
  • 16
    • 3042630872 scopus 로고    scopus 로고
    • Hair follicle differentiation and regulation
    • Rogers G E. Hair follicle differentiation and regulation. Int J Dev Biol 2004: 48: 163-170.
    • (2004) Int J Dev Biol , vol.48 , pp. 163-170
    • Rogers, G.E.1
  • 18
    • 0000625315 scopus 로고
    • Feather keratins: Composition, structure and biogenesis
    • In: Bereither-Hahn J, Matoltsy G, Sylvia-Richards K, eds. Berlin-Heidelberg-New York: Springer-Verlag
    • Gregg K, Rogers G. Feather keratins: Composition, structure and biogenesis. In: Bereither-Hahn J, Matoltsy G, Sylvia-Richards K, eds. Biology of the Integument, Vertebrates. Berlin-Heidelberg-New York: Springer-Verlag, 1986: 666-694.
    • (1986) Biology of the Integument, Vertebrates , pp. 666-694
    • Gregg, K.1    Rogers, G.2
  • 19
    • 0030272341 scopus 로고    scopus 로고
    • The molecular structure of reptilian keratin
    • Fraser R D, Parry D A. The molecular structure of reptilian keratin. Int J Biol Macromol 1996: 19: 207-211.
    • (1996) Int J Biol Macromol , vol.19 , pp. 207-211
    • Fraser, R.D.1    Parry, D.A.2
  • 21
    • 0018377315 scopus 로고
    • The molecular heterogeneity and diversity of reptilian keratins
    • Wyld J A, Brush A H. The molecular heterogeneity and diversity of reptilian keratins. J Mol Evol 1979: 12: 331-347.
    • (1979) J Mol Evol , vol.12 , pp. 331-347
    • Wyld, J.A.1    Brush, A.H.2
  • 22
    • 84986467756 scopus 로고
    • Keratin diversity in the reptilian epidermis
    • Wyld J A, Brush A H. Keratin diversity in the reptilian epidermis. J Exp Zool 1983: 225: 387-396.
    • (1983) J Exp Zool , vol.225 , pp. 387-396
    • Wyld, J.A.1    Brush, A.H.2
  • 23
    • 0001842915 scopus 로고
    • The origin of feather: A novel approach
    • In: Farner D, Kling J, Parker K, eds. New York: Academic Press
    • Brush A H. The origin of feather: A novel approach. In: Farner D, Kling J, Parker K, eds. Avian Biology. New York: Academic Press, 1993: 121-162.
    • (1993) Avian Biology , pp. 121-162
    • Brush, A.H.1
  • 24
    • 33645874501 scopus 로고    scopus 로고
    • Cytochemical, biochemical and molecular aspects of the process of keratinization in the epidermis of reptilian scales
    • Alibardi L, Toni M. Cytochemical, biochemical and molecular aspects of the process of keratinization in the epidermis of reptilian scales. Prog Histochem Cytochem 2006: 40: 73-134.
    • (2006) Prog Histochem Cytochem , vol.40 , pp. 73-134
    • Alibardi, L.1    Toni, M.2
  • 25
    • 33846242975 scopus 로고    scopus 로고
    • Structural and immunocytochemical characterization of keratinization in vertebrate epidermis and epidermal derivatives
    • Alibardi L. Structural and immunocytochemical characterization of keratinization in vertebrate epidermis and epidermal derivatives. Int Rev Cytol 2006: 253: 177-259.
    • (2006) Int Rev Cytol , vol.253 , pp. 177-259
    • Alibardi, L.1
  • 26
    • 0014807151 scopus 로고
    • Morphological and biophysical identification of fibrous proteins in the amniote epidermis
    • Baden H P, Maderson P F. Morphological and biophysical identification of fibrous proteins in the amniote epidermis. J Exp Zool 1970: 174: 225-232.
    • (1970) J Exp Zool , vol.174 , pp. 225-232
    • Baden, H.P.1    Maderson, P.F.2
  • 27
    • 0020021267 scopus 로고
    • A comparison of lizard claw keratin proteins with those of avian beak and claw
    • Gillespie J M, Marshall R C, Woods E F. A comparison of lizard claw keratin proteins with those of avian beak and claw. J Mol Evol 1982: 18: 121-129.
    • (1982) J Mol Evol , vol.18 , pp. 121-129
    • Gillespie, J.M.1    Marshall, R.C.2    Woods, E.F.3
  • 28
    • 0020016149 scopus 로고
    • The tryptophan-rich keratin protein fraction of claws of the lizard Varanus gouldii
    • Marshall R C, Gillespie J M. The tryptophan-rich keratin protein fraction of claws of the lizard Varanus gouldii. Comp Biochem Physiol B 1982: 71: 623-628.
    • (1982) Comp Biochem Physiol B , vol.71 , pp. 623-628
    • Marshall, R.C.1    Gillespie, J.M.2
  • 29
    • 0002458070 scopus 로고
    • Sequence of a glycine-rich protein from lizard claw: Unusual dilute acid and heptafluorobutyric acid cleavage
    • In: L'Italien J L, ed. New York-London: Plenum Press
    • Inglis A, Gillespie J M, Roxburgh C, Whittaker L, Casagranda F. Sequence of a glycine-rich protein from lizard claw: Unusual dilute acid and heptafluorobutyric acid cleavage. In: L'Italien J L, ed. Protein, Structure and Function. New York-London: Plenum Press, 1987: 757-764.
    • (1987) Protein, Structure and Function , pp. 757-764
    • Inglis, A.1    Gillespie, J.M.2    Roxburgh, C.3    Whittaker, L.4    Casagranda, F.5
  • 30
    • 0027301205 scopus 로고
    • Region-specific patterns of beta keratin expression during avian skin development
    • Knapp L W, Shames R B, Barnes G L, Sawyer R H. Region-specific patterns of beta keratin expression during avian skin development. Dev Dyn 1993: 196: 283-290.
    • (1993) Dev Dyn , vol.196 , pp. 283-290
    • Knapp, L.W.1    Shames, R.B.2    Barnes, G.L.3    Sawyer, R.H.4
  • 31
    • 34447519202 scopus 로고    scopus 로고
    • Beta-keratins of differentiating epidermis of snake show that they are glycine-proline-rich proteins with an avian-like gene organizaton
    • Dalla Valle L, Nardi A, Belvedere P, Toni M, Alibardi L Beta-keratins of differentiating epidermis of snake show that they are glycine-proline-rich proteins with an avian-like gene organizaton. Dev Dyn 2007: 236: 1939-1953.
    • (2007) Dev Dyn , vol.236 , pp. 1939-1953
    • Dalla Valle, L.1    Nardi, A.2    Belvedere, P.3    Toni, M.4    Alibardi, L.5
  • 32
    • 33846899735 scopus 로고    scopus 로고
    • Cloning and characterization of scale b-keratins in the differentiating epidermis of Geckoes show they are glycine-proline-serine-rich proteins with a central motif homologous to avian beta-keratins
    • Dalla Valle L, Nardi A, Toffolo V, Niero C, Toni M, Alibardi L. Cloning and characterization of scale b-keratins in the differentiating epidermis of Geckoes show they are glycine-proline-serine-rich proteins with a central motif homologous to avian beta-keratins. Dev Dyn 2006: 236: 374-388.
    • (2006) Dev Dyn , vol.236 , pp. 374-388
    • Dalla Valle, L.1    Nardi, A.2    Toffolo, V.3    Niero, C.4    Toni, M.5    Alibardi, L.6
  • 33
    • 0027254919 scopus 로고
    • The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis
    • Mack J W, Steven A C, Steinert P M. The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis. J Mol Biol 1993: 232: 50-66.
    • (1993) J Mol Biol , vol.232 , pp. 50-66
    • Mack, J.W.1    Steven, A.C.2    Steinert, P.M.3
  • 35
    • 0013095884 scopus 로고    scopus 로고
    • Late events and the regulation of keratinocyte differentiation in hair and feather follicles
    • In: Chuong C M, ed. Molecular Biology Intelligence Unit. Austin, TX: Landes, R. G
    • Rogers G E, Dunn S, Powell B. Late events and the regulation of keratinocyte differentiation in hair and feather follicles. In: Chuong C M, ed. Molecular Basis of Epithelial Appendages and Morphogenesis. Molecular Biology Intelligence Unit. Austin, TX: Landes, R. G, 1999: 315-338.
    • (1999) Molecular Basis of Epithelial Appendages and Morphogenesis , pp. 315-338
    • Rogers, G.E.1    Dunn, S.2    Powell, B.3
  • 36
    • 28444488281 scopus 로고    scopus 로고
    • Isolation of a mRNA encoding a glycine-proline-rich beta-keratin expressed in the regenerating epidermis of lizard
    • Dalla Valle L, Toffolo V, Belvedere P, Alibardi L. Isolation of a mRNA encoding a glycine-proline-rich beta-keratin expressed in the regenerating epidermis of lizard. Dev Dyn 2005: 234: 934-947.
    • (2005) Dev Dyn , vol.234 , pp. 934-947
    • Dalla Valle, L.1    Toffolo, V.2    Belvedere, P.3    Alibardi, L.4
  • 37
    • 0033061571 scopus 로고    scopus 로고
    • Initiation of translation in prokaryotes and eukaryotes
    • Kozak M. Initiation of translation in prokaryotes and eukaryotes. Gene 1999: 234: 187-208.
    • (1999) Gene , vol.234 , pp. 187-208
    • Kozak, M.1
  • 38
    • 0021307696 scopus 로고
    • A comparison of genomic coding sequences for feather and scale keratins: Structural and evolutionary implications
    • Gregg K, Wilton S, Parry D A, Rogers G. A comparison of genomic coding sequences for feather and scale keratins: Structural and evolutionary implications. EMBO J 1984: 3: 175-178.
    • (1984) EMBO J , vol.3 , pp. 175-178
    • Gregg, K.1    Wilton, S.2    Parry, D.A.3    Rogers, G.4
  • 39
    • 33745747560 scopus 로고    scopus 로고
    • Scale keratin in lizard epidermis reveals amino acid regions homologous with avian and mammalian epidermal proteins
    • Alibardi L, Dalla Valle L, Toffolo V, Toni M. Scale keratin in lizard epidermis reveals amino acid regions homologous with avian and mammalian epidermal proteins. Anat Rec A 2006: 288: 734-752.
    • (2006) Anat Rec A , vol.288 , pp. 734-752
    • Alibardi, L.1    Dalla Valle, L.2    Toffolo, V.3    Toni, M.4
  • 40
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin L. The PSIPRED protein structure prediction server. Bioinformatics 2000: 16: 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.1
  • 41
    • 0015993985 scopus 로고
    • The structural protein of reptilian scales
    • Baden H, Sviokla S, Roth I. The structural protein of reptilian scales. J Exp Zool 1974: 187: 287-294.
    • (1974) J Exp Zool , vol.187 , pp. 287-294
    • Baden, H.1    Sviokla, S.2    Roth, I.3
  • 42
    • 19944362818 scopus 로고    scopus 로고
    • Developing antibodies to synthetic peptides based on comparative DNA sequencing of multigene families
    • Sawyer R H, Glenn T C, French J O, Knapp L W. Developing antibodies to synthetic peptides based on comparative DNA sequencing of multigene families. Meth Enzymol 2005: 395: 636-652.
    • (2005) Meth Enzymol , vol.395 , pp. 636-652
    • Sawyer, R.H.1    Glenn, T.C.2    French, J.O.3    Knapp, L.W.4
  • 43
    • 0032102681 scopus 로고    scopus 로고
    • Structural-mechanical integration of keratin intermediate filaments with cell peripheral structures in the cornified epidermal keratinocyte
    • discussion 369-370
    • Steinert P M Structural-mechanical integration of keratin intermediate filaments with cell peripheral structures in the cornified epidermal keratinocyte. Biol Bull 1998: 194: 367-368; discussion 369-370.
    • (1998) Biol Bull , vol.194 , pp. 367-368
    • Steinert, P.M.1
  • 44
    • 0036715005 scopus 로고    scopus 로고
    • Epithelial barrier function: Assembly and structural features of the cornified cell envelope
    • Kalinin A E, Kajava A V, Steinert P M. Epithelial barrier function: assembly and structural features of the cornified cell envelope. Bioessays 2002: 24: 789-800.
    • (2002) Bioessays , vol.24 , pp. 789-800
    • Kalinin, A.E.1    Kajava, A.V.2    Steinert, P.M.3
  • 45
    • 0023182683 scopus 로고
    • Evolution of keratin genes: Different protein domains evolve by different pathways
    • Klinge E M, Sylvestre Y R, Freedberg I M, Blumenberg M. Evolution of keratin genes: Different protein domains evolve by different pathways. J Mol Evol 1987: 24: 319-329.
    • (1987) J Mol Evol , vol.24 , pp. 319-329
    • Klinge, E.M.1    Sylvestre, Y.R.2    Freedberg, I.M.3    Blumenberg, M.4
  • 47
    • 0024357840 scopus 로고
    • Avian keratin genes. I. A molecular analysis of the structure and expression of a group of feather keratin genes
    • Presland R B, Gregg K, Molloy P L, Morris C P, Crocker L A, Rogers G E. Avian keratin genes. I. A molecular analysis of the structure and expression of a group of feather keratin genes. J Mol Biol 1989: 209: 549-559.
    • (1989) J Mol Biol , vol.209 , pp. 549-559
    • Presland, R.B.1    Gregg, K.2    Molloy, P.L.3    Morris, C.P.4    Crocker, L.A.5    Rogers, G.E.6
  • 48
    • 0024388202 scopus 로고
    • Avian keratin genes. II. Chromosomal arrangement and close linkage of three gene families
    • Presland R B, Whitbread L A, Rogers G E. Avian keratin genes. II. Chromosomal arrangement and close linkage of three gene families. J Mol Biol 1989: 209: 561-576.
    • (1989) J Mol Biol , vol.209 , pp. 561-576
    • Presland, R.B.1    Whitbread, L.A.2    Rogers, G.E.3
  • 49
    • 0038100445 scopus 로고    scopus 로고
    • Origin of feathers: Feather beta (beta) keratins are expressed in discrete epidermal cell populations of embryonic scutate scales
    • Sawyer R H, Salvatore B A, Potylicki T T, French J O, Glenn T C, Knapp L W. Origin of feathers: Feather beta (beta) keratins are expressed in discrete epidermal cell populations of embryonic scutate scales. J Exp Zoolog B Mol Dev Evol 2003: 295: 12-24.
    • (2003) J Exp Zoolog B Mol Dev Evol , vol.295 , pp. 12-24
    • Sawyer, R.H.1    Salvatore, B.A.2    Potylicki, T.T.3    French, J.O.4    Glenn, T.C.5    Knapp, L.W.6
  • 51
    • 33646034296 scopus 로고    scopus 로고
    • Cell structure of developing downfeathers in the zebrafinch with emphasis on barb ridge morphogenesis
    • Alibardi L, Sawyer R H. Cell structure of developing downfeathers in the zebrafinch with emphasis on barb ridge morphogenesis. J Anat 2006: 208: 621-642.
    • (2006) J Anat , vol.208 , pp. 621-642
    • Alibardi, L.1    Sawyer, R.H.2
  • 53
    • 0025044473 scopus 로고
    • Isolation of a chick cytokeratin cDNA clone indicative of regional specialization in early embryonic ectoderm
    • Charlebois T S, Spencer D H, Tarkington S K, Henry J J, Grainger R M. Isolation of a chick cytokeratin cDNA clone indicative of regional specialization in early embryonic ectoderm. Development 1990: 108: 33-45.
    • (1990) Development , vol.108 , pp. 33-45
    • Charlebois, T.S.1    Spencer, D.H.2    Tarkington, S.K.3    Henry, J.J.4    Grainger, R.M.5
  • 54
    • 4444271721 scopus 로고    scopus 로고
    • Simultaneous cell death and desquamation of the embryonic diffusion barrier during epidermal development
    • Saathoff M, Blum B, Quast T, Kirfel G, Herzog V. Simultaneous cell death and desquamation of the embryonic diffusion barrier during epidermal development. Exp Cell Res 2004: 299: 415-426.
    • (2004) Exp Cell Res , vol.299 , pp. 415-426
    • Saathoff, M.1    Blum, B.2    Quast, T.3    Kirfel, G.4    Herzog, V.5
  • 55
    • 16644382276 scopus 로고    scopus 로고
    • Serial cultivation of chicken keratinocytes, a composite cell type that accumulates lipids and synthesizes a novel beta-keratin
    • Vanhoutteghem A, Londero T, Ghinea N, Djian P. Serial cultivation of chicken keratinocytes, a composite cell type that accumulates lipids and synthesizes a novel beta-keratin. Differentiation 2004: 72: 123-137.
    • (2004) Differentiation , vol.72 , pp. 123-137
    • Vanhoutteghem, A.1    Londero, T.2    Ghinea, N.3    Djian, P.4
  • 56
    • 0025856204 scopus 로고
    • The structure and expression of a gene encoding chick claw keratin
    • Whitbread L A, Gregg K, Rogers G E. The structure and expression of a gene encoding chick claw keratin. Gene 1991: 101: 223-229.
    • (1991) Gene , vol.101 , pp. 223-229
    • Whitbread, L.A.1    Gregg, K.2    Rogers, G.E.3
  • 57
    • 0029257422 scopus 로고
    • Histidine-rich protein B of embryonic feathers is present in the transient embryonic layers of scutate scales
    • Barnes G L Jr, Sawyer R H. Histidine-rich protein B of embryonic feathers is present in the transient embryonic layers of scutate scales. J Exp Zool 1995: 271: 307-314.
    • (1995) J Exp Zool , vol.271 , pp. 307-314
    • Barnes Jr., G.L.1    Sawyer, R.H.2
  • 58
    • 0023951297 scopus 로고
    • Molecular and cellular biology of intermediate filaments
    • Steinert P M, Roop D R. Molecular and cellular biology of intermediate filaments. Annu Rev Biochem 1988: 57: 593-625.
    • (1988) Annu Rev Biochem , vol.57 , pp. 593-625
    • Steinert, P.M.1    Roop, D.R.2
  • 59
    • 0033538528 scopus 로고    scopus 로고
    • The catalog of human hair keratins. I. Expression of the nine type I members in the hair follicle
    • Langbein L, Rogers M A, Winter H et al. The catalog of human hair keratins. I. Expression of the nine type I members in the hair follicle. J Biol Chem 1999: 274: 19874-19884.
    • (1999) J Biol Chem , vol.274 , pp. 19874-19884
    • Langbein, L.1    Rogers, M.A.2    Winter, H.3
  • 60
    • 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 M A, 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
  • 61
    • 16844383908 scopus 로고    scopus 로고
    • Keratins of the human hair follicle
    • Langbein L, Schweizer J. Keratins of the human hair follicle. Int Rev Cytol 2005: 243: 1-78.
    • (2005) Int Rev Cytol , vol.243 , pp. 1-78
    • Langbein, L.1    Schweizer, J.2
  • 62
    • 33750625712 scopus 로고    scopus 로고
    • Biology of the wool follicle: An excursion into a unique tissue interaction system waiting to be re-discovered
    • Rogers G. Biology of the wool follicle: An excursion into a unique tissue interaction system waiting to be re-discovered. Exp Dermatol 2006: 15: 931-949.
    • (2006) Exp Dermatol , vol.15 , pp. 931-949
    • Rogers, G.1
  • 63
    • 0027154641 scopus 로고
    • Analysis of the sheep trichohyalin gene: Potential structural and calcium-binding roles of trichohyalin in the hair follicle
    • Fietz M J, McLaughlan C J, Campbell M T, Rogers G E. Analysis of the sheep trichohyalin gene: Potential structural and calcium-binding roles of trichohyalin in the hair follicle. J Cell Biol 1993: 121: 855-865.
    • (1993) J Cell Biol , vol.121 , pp. 855-865
    • Fietz, M.J.1    McLaughlan, C.J.2    Campbell, M.T.3    Rogers, G.E.4
  • 64
    • 0027534138 scopus 로고
    • Human trichohyalin gene is clustered with the genes for other epidermal structural proteins and calcium-binding proteins at chromosomal locus 1q21
    • Lee S C, Wang M, McBride O W, O'Keefe E J, Kim I G, Steinert P M. Human trichohyalin gene is clustered with the genes for other epidermal structural proteins and calcium-binding proteins at chromosomal locus 1q21. J Invest Dermatol 1993: 100: 65-68.
    • (1993) J Invest Dermatol , vol.100 , pp. 65-68
    • Lee, S.C.1    Wang, M.2    McBride, O.W.3    O'Keefe, E.J.4    Kim, I.G.5    Steinert, P.M.6
  • 65
    • 0025078367 scopus 로고
    • The structure of the gene for mouse filaggrin and a comparison of the repeating units
    • Rothnagel J A, Steinert P M The structure of the gene for mouse filaggrin and a comparison of the repeating units. J Biol Chem 1990: 265: 1862-1865.
    • (1990) J Biol Chem , vol.265 , pp. 1862-1865
    • Rothnagel, J.A.1    Steinert, P.M.2
  • 66
    • 0002247658 scopus 로고
    • Keratohyalin granule proteins
    • In: Leigh I, Lane B, Watt F, eds. Cambridge: University Press
    • Dale B A, Resing K A, Presland R B. Keratohyalin granule proteins. In: Leigh I, Lane B, Watt F, eds. The Keratinocyte Handbook. Cambridge: University Press, 1994: 323-350.
    • (1994) The Keratinocyte Handbook , pp. 323-350
    • Dale, B.A.1    Resing, K.A.2    Presland, R.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.