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Volumn 15, Issue 5, 2014, Pages 518-530

Keratin-based biomaterials for biomedical applications

Author keywords

Drug delivery; Keratin; Modern systems; Nanobiotechnology; Pharmaceutical technology; Sustainability

Indexed keywords

ALGINIC ACID; ALKALINE PHOSPHATASE; ANTINEOPLASTIC AGENT; ASIALOGLYCOPROTEIN RECEPTOR; BIOMATERIAL; BONE MORPHOGENETIC PROTEIN 2; CHITOSAN; CIPROFLOXACIN; COLLAGEN; COPPER ZINC SUPEROXIDE DISMUTASE; CYTOKERATIN 1; CYTOKERATIN 10; CYTOKERATIN 12; CYTOKERATIN 13; CYTOKERATIN 2; CYTOKERATIN 20; DOXORUBICIN; FIBRIN; GENTAMICIN; GLUTATHIONE; HEAT SHOCK PROTEIN; HYALURONIC ACID; HYDROXYAPATITE; KERATIN; POLYLACTIC ACID; REGULATOR PROTEIN; SILK FIBROIN; SILVER NANOPARTICLE; TRYPSIN; UNINDEXED DRUG;

EID: 84898661747     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/1389450115666140307154143     Document Type: Article
Times cited : (38)

References (196)
  • 1
    • 65449149031 scopus 로고    scopus 로고
    • Structure and functions of keratin proteins in simple, stratified, keratinized and cornified epithelia
    • Bragulla HH, Homberger DG. Structure and functions of keratin proteins in simple, stratified, keratinized and cornified epithelia. J Anat 2009; 214(4): 516-559.
    • (2009) J Anat , vol.214 , Issue.4 , pp. 516-559
    • Bragulla, H.H.1    Homberger, D.G.2
  • 2
    • 32644435175 scopus 로고    scopus 로고
    • Microbial keratinases and their prospective applications: An overview
    • Gupta R, Ramnani P. Microbial keratinases and their prospective applications: An overview. Appl Microbiol Biotechnol 2006; 70(1): 21-33.
    • (2006) Appl Microbiol Biotechnol , vol.70 , Issue.1 , pp. 21-33
    • Gupta, R.1    Ramnani, P.2
  • 3
    • 0033793829 scopus 로고    scopus 로고
    • Coiled-coil trigger motifs in the 1B and 2B rod domain segments are required for the stability of keratin intermediate filaments
    • Wu KC, Bryan JT, Morasso MI, et al. Coiled-coil trigger motifs in the 1B and 2B rod domain segments are required for the stability of keratin intermediate filaments. Mol Biol Cell 2000; 11(10): 3539-3558.
    • (2000) Mol Biol Cell , vol.11 , Issue.10 , pp. 3539-3558
    • Wu, K.C.1    Bryan, J.T.2    Morasso, M.I.3
  • 4
    • 34250122988 scopus 로고
    • Functional-morphological and biochemical correlations of the keratinized structures in the African Grey Parrot, Psittacus erithacus (Aves)
    • Homberger DG, Brush AH. Functional-morphological and biochemical correlations of the keratinized structures in the African Grey Parrot, Psittacus erithacus (Aves). Zoomorphology 1986; 106(2): 103-114.
    • (1986) Zoomorphology , vol.106 , Issue.2 , pp. 103-114
    • Homberger, D.G.1    Brush, A.H.2
  • 5
    • 65449141142 scopus 로고
    • Chemical classification of keratins
    • Block RJ. Chemical classification of keratins. Ann N Y Acad Sci 1951; 53(3): 608-612.
    • (1951) Ann N Y Acad Sci , vol.53 , Issue.3 , pp. 608-612
    • Block, R.J.1
  • 6
    • 0032496154 scopus 로고    scopus 로고
    • Biochemical evidence that small proline-rich proteins and trichohyalin function in epithelia by modulation of the biomechanical properties of their cornified cell envelopes
    • Steinert PM, Kartasova T, Marekov LN. Biochemical evidence that small proline-rich proteins and trichohyalin function in epithelia by modulation of the biomechanical properties of their cornified cell envelopes. J Biol Chem 1998; 273(19): 11758-11769.
    • (1998) J Biol Chem , vol.273 , Issue.19 , pp. 11758-11769
    • Steinert, P.M.1    Kartasova, T.2    Marekov, L.N.3
  • 7
    • 34249750035 scopus 로고    scopus 로고
    • Towards a molecular description of intermediate filament structure and assembly
    • Parry DA, Strelkov SV, Burkhard P, Aebi U, Herrmann H. Towards a molecular description of intermediate filament structure and assembly. Exp Cell Res 2007; 313(10): 2204-2216.
    • (2007) Exp Cell Res , vol.313 , Issue.10 , pp. 2204-2216
    • Parry, D.A.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4    Herrmann, H.5
  • 8
    • 12344276291 scopus 로고    scopus 로고
    • Great promises yet to be fulfilled: Defining keratin intermediate filament function in vivo
    • Coulombe PA, Tong X, Mazzalupo S, Wang Z, Wong P. Great promises yet to be fulfilled: Defining keratin intermediate filament function in vivo. Eur J Cell Biol 2004; 83(11-12): 735-746.
    • (2004) Eur J Cell Biol , vol.83 , Issue.11-12 , pp. 735-746
    • Coulombe, P.A.1    Tong, X.2    Mazzalupo, S.3    Wang, Z.4    Wong, P.5
  • 9
    • 0030272341 scopus 로고    scopus 로고
    • The molecular structure of reptilian keratin
    • Fraser RD, Parry DA. The molecular structure of reptilian keratin. Int J Biol Macromol 1996; 19(3): 207-211.
    • (1996) Int J Biol Macromol , vol.19 , Issue.3 , pp. 207-211
    • Fraser, R.D.1    Parry, D.A.2
  • 10
    • 41649093731 scopus 로고    scopus 로고
    • Molecular packing in the feather keratin filament
    • Fraser RD, Parry DA. Molecular packing in the feather keratin filament. J Struct Biol 2008; 162(1): 1-13.
    • (2008) J Struct Biol , vol.162 , Issue.1 , pp. 1-13
    • Fraser, R.D.1    Parry, D.A.2
  • 12
    • 0025284699 scopus 로고
    • The two-chain coiled-coil molecule of native epidermal keratin intermediate filaments is a type I-type II heterodimer
    • Steinert PM. The two-chain coiled-coil molecule of native epidermal keratin intermediate filaments is a type I-type II heterodimer. J Biol Chem 1990; 265(15): 8766-8774.
    • (1990) J Biol Chem , vol.265 , Issue.15 , pp. 8766-8774
    • Steinert, P.M.1
  • 13
    • 0035016216 scopus 로고    scopus 로고
    • Keratins: Dynamic, flexible structural proteins of epithelial cells
    • Steinert PM. Keratins: Dynamic, flexible structural proteins of epithelial cells. Curr Probl Dermatol 2001; 54: 193-8.
    • (2001) Curr Probl Dermatol , vol.54 , pp. 193-198
    • Steinert, P.M.1
  • 14
    • 0022348539 scopus 로고
    • Pair formation and promiscuity of cy-tokeratins: Formation in vitro of heterotypic complexes and intermediate-sized filaments by homologous and heterologous recombinations of purified polypeptides
    • Hatzfeld M, Franke WW. Pair formation and promiscuity of cy-tokeratins: Formation in vitro of heterotypic complexes and intermediate-sized filaments by homologous and heterologous recombinations of purified polypeptides. J Cell Biol 1985; 101(5 Pt 1): 1826-1841.
    • (1985) J Cell Biol , vol.101 , Issue.1-5 , pp. 1826-1841
    • Hatzfeld, M.1    Franke, W.W.2
  • 15
    • 14244253598 scopus 로고    scopus 로고
    • Isolation, characterization, and in vitro assembly of intermediate filaments
    • Herrmann H, Kreplak L, Aebi U. Isolation, characterization, and in vitro assembly of intermediate filaments. Methods Cell Biol 2004; 78: 3-24.
    • (2004) Methods Cell Biol , vol.78 , pp. 3-24
    • Herrmann, H.1    Kreplak, L.2    Aebi, U.3
  • 16
    • 0025073744 scopus 로고
    • Retrovirus-mediated transgenic keratin expression in cultured fibroblasts: Specific domain functions in keratin stabilization and filament formation
    • Lu X, Lane EB. Retrovirus-mediated transgenic keratin expression in cultured fibroblasts: Specific domain functions in keratin stabilization and filament formation. Cell 1990; 62(4): 681-696.
    • (1990) Cell , vol.62 , Issue.4 , pp. 681-696
    • Lu, X.1    Lane, E.B.2
  • 17
    • 0031594518 scopus 로고    scopus 로고
    • Characterization and chromosomal localization of human hair-specific keratin genes and comparative expression during the hair growth cycle
    • Bowden PE, Hainey SD, Parker G, et al. Characterization and chromosomal localization of human hair-specific keratin genes and comparative expression during the hair growth cycle. J Invest Der-matol 1998; 110(2): 158-164.
    • (1998) J Invest Der-matol , vol.110 , Issue.2 , pp. 158-164
    • Bowden, P.E.1    Hainey, S.D.2    Parker, G.3
  • 18
    • 0023026260 scopus 로고
    • Monoclonal antibody analysis of bovine epithelial keratins. Specific pairs as defined by coexpression
    • Cooper D, Sun TT. Monoclonal antibody analysis of bovine epithelial keratins. Specific pairs as defined by coexpression. J Biol Chem 1986; 261(10): 4646-4654.
    • (1986) J Biol Chem , vol.261 , Issue.10 , pp. 4646-4654
    • Cooper, D.1    Sun, T.T.2
  • 19
    • 0020576881 scopus 로고
    • Characterization of the proteins of human hair and nail by electrophoresis
    • Marshall RC. Characterization of the proteins of human hair and nail by electrophoresis. J Invest Dermatol 1983; 80(6): 519-524.
    • (1983) J Invest Dermatol , vol.80 , Issue.6 , pp. 519-524
    • Marshall, R.C.1
  • 20
    • 0021612262 scopus 로고
    • Proteolytic modification of acidic and basic keratins during terminal differentiation of mouse and human epidermis
    • Bowden PE, Quinlan RA, Breitkreutz D, Fusenig NE. Proteolytic modification of acidic and basic keratins during terminal differentiation of mouse and human epidermis. Eur J Biochem 1984; 142(1): 29-36.
    • (1984) Eur J Biochem , vol.142 , Issue.1 , pp. 29-36
    • Bowden, P.E.1    Quinlan, R.A.2    Breitkreutz, D.3    Fusenig, N.E.4
  • 21
    • 44149099717 scopus 로고    scopus 로고
    • The human keratins: Biology and pathology
    • Moll R, Divo M, Langbein L. The human keratins: Biology and pathology. Histochem Cell Biol 2008; 129(6): 705-733.
    • (2008) Histochem Cell Biol , vol.129 , Issue.6 , pp. 705-733
    • Moll, R.1    Divo, M.2    Langbein, L.3
  • 22
    • 0020591925 scopus 로고
    • The fibrillar substructure of keratin filaments unraveled
    • Aebi U, Fowler WE, Rew P, Sun TT. The fibrillar substructure of keratin filaments unraveled. J Cell Biol 1983; 97(4): 1131-1143.
    • (1983) J Cell Biol , vol.97 , Issue.4 , pp. 1131-1143
    • Aebi, U.1    Fowler, W.E.2    Rew, P.3    Sun, T.T.4
  • 23
    • 0025216452 scopus 로고
    • Differential extraction of keratin subunits and filaments from normal human epidermis
    • Eichner R, Kahn M. Differential extraction of keratin subunits and filaments from normal human epidermis. J Cell Biol 1990; 110(4): 1149-1168.
    • (1990) J Cell Biol , vol.110 , Issue.4 , pp. 1149-1168
    • Eichner, R.1    Kahn, M.2
  • 24
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct in-tracellular scaffolds
    • Herrmann H, Aebi U. Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct in-tracellular scaffolds. Annu Rev Biochem 2004; 73: 749-789.
    • (2004) Annu Rev Biochem , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 25
    • 0033498452 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular architecture, assembly, dynamics, and polymorphism
    • Parry DA, Steinert PM. Intermediate filaments: Molecular architecture, assembly, dynamics, and polymorphism. Q Rev Biophys 1999; 32(2): 99-187.
    • (1999) Q Rev Biophys , vol.32 , Issue.2 , pp. 99-187
    • Parry, D.A.1    Steinert, P.M.2
  • 26
    • 34249723830 scopus 로고    scopus 로고
    • Structural and regulatory functions of keratins
    • Magin TM, Vijayaraj P, Leube RE. Structural and regulatory functions of keratins. Exp Cell Res 2007; 313(10): 2021-2032.
    • (2007) Exp Cell Res , vol.313 , Issue.10 , pp. 2021-2032
    • Magin, T.M.1    Vijayaraj, P.2    Leube, R.E.3
  • 28
    • 0026640553 scopus 로고
    • The roles of K5 and K14 head, tail, and R/K L L E G E domains in keratin filament assembly in vitro
    • Wilson AK, Coulombe PA, Fuchs E. The roles of K5 and K14 head, tail, and R/K L L E G E domains in keratin filament assembly in vitro. J Cell Biol 1992; 119(2): 401-414.
    • (1992) J Cell Biol , vol.119 , Issue.2 , pp. 401-414
    • Wilson, A.K.1    Coulombe, P.A.2    Fuchs, E.3
  • 29
    • 0029433677 scopus 로고
    • The mineralization of crystalline inorganic components in Japanese serow horn
    • Hashiguchi K, Hashimoto K. The mineralization of crystalline inorganic components in Japanese serow horn. Okajimas Folia Anat Jpn 1995; 72(5): 235-243.
    • (1995) Okajimas Folia Anat Jpn , vol.72 , Issue.5 , pp. 235-243
    • Hashiguchi, K.1    Hashimoto, K.2
  • 30
    • 0035351262 scopus 로고    scopus 로고
    • Morphological character of crystalline components present in saiga horn
    • Hashiguchi K, Hashimoto K, Akao M. Morphological character of crystalline components present in saiga horn. Okajimas Folia Anat Jpn 2001; 78(1): 43-48.
    • (2001) Okajimas Folia Anat Jpn , vol.78 , Issue.1 , pp. 43-48
    • Hashiguchi, K.1    Hashimoto, K.2    Akao, M.3
  • 31
    • 0014087779 scopus 로고
    • Similarities of keratinization and amelogenesis
    • Toto PD, O'Malley JJ, Grandel ER. Similarities of keratinization and amelogenesis. J Dent Res 1967; 46(3): 602-607.
    • (1967) J Dent Res , vol.46 , Issue.3 , pp. 602-607
    • Toto, P.D.1    O'Malley, J.J.2    Grandel, E.R.3
  • 32
    • 33748956630 scopus 로고    scopus 로고
    • Structure of white rhinoceros (Ceratotherium simum) horn investigated by X-ray computed tomography and histology with implications for growth and external form
    • Hieronymus TL, Witmer LM, Ridgely RC. Structure of white rhinoceros (Ceratotherium simum) horn investigated by X-ray computed tomography and histology with implications for growth and external form. J Morphol 2006; 267(10): 1172-1176.
    • (2006) J Morphol , vol.267 , Issue.10 , pp. 1172-1176
    • Hieronymus, T.L.1    Witmer, L.M.2    Ridgely, R.C.3
  • 33
    • 21044438783 scopus 로고    scopus 로고
    • Nail calcium and magnesium content in relation to age and bone mineral density
    • Ohgitani S, Fujita T, Fujii Y, Hayashi C, Nishio H. Nail calcium and magnesium content in relation to age and bone mineral density. J Bone Miner Metab 2005; 23(4): 318-322.
    • (2005) J Bone Miner Metab , vol.23 , Issue.4 , pp. 318-322
    • Ohgitani, S.1    Fujita, T.2    Fujii, Y.3    Hayashi, C.4    Nishio, H.5
  • 34
    • 0029068439 scopus 로고
    • Calcium and magnesium in human toenails do not reflect bone mineral density
    • Vecht-Hart CM, Bode P, Trouerbach WT, Collette HJ. Calcium and magnesium in human toenails do not reflect bone mineral density. Clin Chim Acta 1995; 236(1): 1-6.
    • (1995) Clin Chim Acta , vol.236 , Issue.1 , pp. 1-6
    • Vecht-Hart, C.M.1    Bode, P.2    Trouerbach, W.T.3    Collette, H.J.4
  • 35
    • 0015262922 scopus 로고
    • The mineralization of hair follicle tissue. I. An in vivo study
    • Pearce EI, Cousins FB, Smillie AC. The mineralization of hair follicle tissue. I. An in vivo study. Calcif Tissue Res 1972; 8(3): 228-236.
    • (1972) Calcif Tissue Res , vol.8 , Issue.3 , pp. 228-236
    • Pearce, E.I.1    Cousins, F.B.2    Smillie, A.C.3
  • 36
    • 0018632331 scopus 로고
    • Histochemical and electron microscopical investigations on the calcified keratin in the horn pearls of a glans carcinoma (calcified keratin)
    • Bonucci E, De Matteis A, Anceschi C. Histochemical and electron microscopical investigations on the calcified keratin in the horn pearls of a glans carcinoma (calcified keratin). Basic Appl Histo-chem 1979; 23(2): 93-102.
    • (1979) Basic Appl Histo-chem , vol.23 , Issue.2 , pp. 93-102
    • Bonucci, E.1    de Matteis, A.2    Anceschi, C.3
  • 37
    • 0020467073 scopus 로고
    • The catalog of human cytokeratins: Patterns of expression in normal epithe-lia, tumors and cultured cells
    • Moll R, Franke WW, Schiller DL, Geiger B, Krepler R. The catalog of human cytokeratins: Patterns of expression in normal epithe-lia, tumors and cultured cells. Cell 1982; 31(1): 11-24.
    • (1982) Cell , vol.31 , Issue.1 , pp. 11-24
    • Moll, R.1    Franke, W.W.2    Schiller, D.L.3    Geiger, B.4    Krepler, R.5
  • 38
    • 0020604736 scopus 로고
    • Keratin classes: Molecular markers for different types of epithelial differentiation
    • Sun TT, Eichner R, Nelson WG, et al. Keratin classes: Molecular markers for different types of epithelial differentiation. J Invest Dermatol 1983; 81(1): 109s-115s.
    • (1983) J Invest Dermatol , vol.81 , Issue.1
    • Sun, T.T.1    Eichner, R.2    Nelson, W.G.3
  • 39
    • 33746097413 scopus 로고    scopus 로고
    • New consensus nomenclature for mammalian keratins
    • Schweizer J, Bowden PE, Coulombe PA, et al. New consensus nomenclature for mammalian keratins. J Cell Biol 2006; 174(2): 169-174.
    • (2006) J Cell Biol , vol.174 , Issue.2 , pp. 169-174
    • Schweizer, J.1    Bowden, P.E.2    Coulombe, P.A.3
  • 40
    • 0025341392 scopus 로고
    • Elucidating the early stages of keratin filament assembly
    • Coulombe PA, Fuchs E. Elucidating the early stages of keratin filament assembly. J Cell Biol 1990; 111(1): 153-169.
    • (1990) J Cell Biol , vol.111 , Issue.1 , pp. 153-169
    • Coulombe, P.A.1    Fuchs, E.2
  • 41
    • 0032103749 scopus 로고    scopus 로고
    • Type I keratin 16 forms relatively unstable tetrameric assembly subunits with various type II keratin partners: Biochemical basis and functional implications
    • discussion 365-66
    • Coulombe PA, Wawersik M, Paladini RD, Noensie E. Type I keratin 16 forms relatively unstable tetrameric assembly subunits with various type II keratin partners: Biochemical basis and functional implications. Biol Bull 1998; 194(3): 364-365, discussion 365-66.
    • (1998) Biol Bull , vol.194 , Issue.3 , pp. 364-365
    • Coulombe, P.A.1    Wawersik, M.2    Paladini, R.D.3    Noensie, E.4
  • 42
    • 0024466880 scopus 로고
    • Expression of keratin K14 in the epidermis and hair follicle: Insights into complex programs of differentiation
    • Coulombe PA, Kopan R, Fuchs E. Expression of keratin K14 in the epidermis and hair follicle: Insights into complex programs of differentiation. J Cell Biol 1989; 109(5): 2295-2312.
    • (1989) J Cell Biol , vol.109 , Issue.5 , pp. 2295-2312
    • Coulombe, P.A.1    Kopan, R.2    Fuchs, E.3
  • 43
    • 0036468732 scopus 로고    scopus 로고
    • 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments
    • Coulombe PA, Omary MB. 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments. Curr Opin Cell Biol 2002; 14(1): 110-122.
    • (2002) Curr Opin Cell Biol , vol.14 , Issue.1 , pp. 110-122
    • Coulombe, P.A.1    Omary, M.B.2
  • 44
    • 0019783487 scopus 로고
    • Two distinct classes of keratin genes and their evolutionary significance
    • Fuchs EV, Coppock SM, Green H, Cleveland DW. Two distinct classes of keratin genes and their evolutionary significance. Cell 1981; 27(1 Pt 2): 75-84.
    • (1981) Cell , vol.27 , Issue.1-2 , pp. 75-84
    • Fuchs, E.V.1    Coppock, S.M.2    Green, H.3    Cleveland, D.W.4
  • 45
    • 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
  • 46
    • 33750051685 scopus 로고    scopus 로고
    • K25 (K25irs1), K26 (K25irs2), K27 (K25irs3), and K28 (K25irs4) represent the type I inner root sheath keratins of the human hair follicle
    • Langbein L, Rogers MA, Praetzel-Wunder S, Helmke B, Schir-macher P, Schweizer J. K25 (K25irs1), K26 (K25irs2), K27 (K25irs3), and K28 (K25irs4) represent the type I inner root sheath keratins of the human hair follicle. J Invest Dermatol 2006; 126(11): 2377-2386.
    • (2006) J Invest Dermatol , vol.126 , Issue.11 , pp. 2377-2386
    • Langbein, L.1    Rogers, M.A.2    Praetzel-Wunder, S.3    Helmke, B.4    Schir-Macher, P.5    Schweizer, J.6
  • 47
    • 4544320330 scopus 로고    scopus 로고
    • Expression of hair keratins in the adult nail unit: An immunohistochemical analysis of the ony-chogenesis in the proximal nail fold, matrix and nail bed
    • Perrin C, Langbein L, Schweizer J. Expression of hair keratins in the adult nail unit: An immunohistochemical analysis of the ony-chogenesis in the proximal nail fold, matrix and nail bed. Br J Dermatol 2004; 151(2): 362-371.
    • (2004) Br J Dermatol , vol.151 , Issue.2 , pp. 362-371
    • Perrin, C.1    Langbein, L.2    Schweizer, J.3
  • 48
    • 0023806770 scopus 로고
    • Patterns of expression of tricho-cytic and epithelial cytokeratins in mammalian tissues. II. Concomitant and mutually exclusive synthesis of trichocytic and epithelial cytokeratins in diverse human and bovine tissues (hair follicle, nail bed and matrix, lingual papilla, thymic reticulum)
    • Heid HW, Moll I, Franke WW. Patterns of expression of tricho-cytic and epithelial cytokeratins in mammalian tissues. II. Concomitant and mutually exclusive synthesis of trichocytic and epithelial cytokeratins in diverse human and bovine tissues (hair follicle, nail bed and matrix, lingual papilla, thymic reticulum). Differentiation 1988; 37(3): 215-230.
    • (1988) Differentiation , vol.37 , Issue.3 , pp. 215-230
    • Heid, H.W.1    Moll, I.2    Franke, W.W.3
  • 49
    • 1542402212 scopus 로고    scopus 로고
    • Functional analysis of keratin components in the mouse hair follicle inner root sheath
    • Porter RM, Gandi M, Wilson NJ, Wood P, McLean WH, Lane EB. Functional analysis of keratin components in the mouse hair follicle inner root sheath. Br J Dermatol 2004; 150(2): 195-204.
    • (2004) Br J Dermatol , vol.150 , Issue.2 , pp. 195-204
    • Porter, R.M.1    Gandi, M.2    Wilson, N.J.3    Wood, P.4    McLean, W.H.5    Lane, E.B.6
  • 50
    • 15044364200 scopus 로고    scopus 로고
    • Characterization of new members of the human type II keratin gene family and a general evaluation of the keratin gene domain on chromosome 12q13.13
    • Rogers MA, Edler L, Winter H, Langbein L, Beckmann I, Schweizer J. Characterization of new members of the human type II keratin gene family and a general evaluation of the keratin gene domain on chromosome 12q13.13. J Invest Dermatol 2005; 124(3): 536-544.
    • (2005) J Invest Dermatol , vol.124 , Issue.3 , pp. 536-544
    • Rogers, M.A.1    Edler, L.2    Winter, H.3    Langbein, L.4    Beckmann, I.5    Schweizer, J.6
  • 51
    • 21644472656 scopus 로고    scopus 로고
    • The human type I keratin gene family: Characterization of new hair follicle specific members and evaluation of the chromosome 17q21.2 gene domain
    • Rogers MA, Winter H, Langbein L, Bleiler R, Schweizer J. The human type I keratin gene family: Characterization of new hair follicle specific members and evaluation of the chromosome 17q21.2 gene domain. Differentiation 2004; 72(9-10): 527-540.
    • (2004) Differentiation , vol.72 , Issue.9-10 , pp. 527-540
    • Rogers, M.A.1    Winter, H.2    Langbein, L.3    Bleiler, R.4    Schweizer, J.5
  • 52
    • 0018866880 scopus 로고
    • Changes in keratin gene expression during terminal differentiation of the keratinocyte
    • Fuchs E, Green H. Changes in keratin gene expression during terminal differentiation of the keratinocyte. Cell 1980; 19(4): 1033-1042.
    • (1980) Cell , vol.19 , Issue.4 , pp. 1033-1042
    • Fuchs, E.1    Green, H.2
  • 53
    • 0023064240 scopus 로고
    • Regulation of keratin gene expression during differentiation of epidermal and vaginal epithelial cells
    • Roop DR. Regulation of keratin gene expression during differentiation of epidermal and vaginal epithelial cells. Curr Top Dev Biol 1987; 22: 195-207.
    • (1987) Curr Top Dev Biol , vol.22 , pp. 195-207
    • Roop, D.R.1
  • 54
    • 0023683885 scopus 로고
    • Use of monospecific antis-era and cRNA probes to localize the major changes in keratin expression during normal and abnormal epidermal differentiation
    • Stoler A, Kopan R, Duvic M, Fuchs E. Use of monospecific antis-era and cRNA probes to localize the major changes in keratin expression during normal and abnormal epidermal differentiation. J Cell Biol 1988; 107(2): 427-446.
    • (1988) J Cell Biol , vol.107 , Issue.2 , pp. 427-446
    • Stoler, A.1    Kopan, R.2    Duvic, M.3    Fuchs, E.4
  • 55
    • 0027535762 scopus 로고
    • Mouse differentiation-specific keratins 1 and 10 require a preexisting keratin scaffold to form a filament network
    • Kartasova T, Roop DR, Holbrook KA, Yuspa SH. Mouse differentiation-specific keratins 1 and 10 require a preexisting keratin scaffold to form a filament network. J Cell Biol 1993; 120(5): 1251-1261.
    • (1993) J Cell Biol , vol.120 , Issue.5 , pp. 1251-1261
    • Kartasova, T.1    Roop, D.R.2    Holbrook, K.A.3    Yuspa, S.H.4
  • 56
    • 6344272398 scopus 로고    scopus 로고
    • The role of keratins in epidermal development and homeostasis - Going beyond the obvious
    • Koch PJ, Roop DR. The role of keratins in epidermal development and homeostasis - Going beyond the obvious. J Invest Dermatol 2004; 123(5): x-xi.
    • (2004) J Invest Dermatol , vol.123 , Issue.5
    • Koch, P.J.1    Roop, D.R.2
  • 57
    • 0026666391 scopus 로고
    • Characterization of human cytokeratin 2, an epidermal cytoskeletal protein synthesized late during differentiation
    • Collin C, Moll R, Kubicka S, Ouhayoun JP, Franke WW. Characterization of human cytokeratin 2, an epidermal cytoskeletal protein synthesized late during differentiation. Exp Cell Res 1992; 202(1): 132-141.
    • (1992) Exp Cell Res , vol.202 , Issue.1 , pp. 132-141
    • Collin, C.1    Moll, R.2    Kubicka, S.3    Ouhayoun, J.P.4    Franke, W.W.5
  • 58
    • 0345074092 scopus 로고    scopus 로고
    • Expression of keratin K2e in cutaneous and oral lesions: Association with keratinocyte activation, proliferation, and keratinization
    • Bloor BK, Tidman N, Leigh IM, et al. Expression of keratin K2e in cutaneous and oral lesions: Association with keratinocyte activation, proliferation, and keratinization. Am J Pathol 2003; 162(3): 963-975.
    • (2003) Am J Pathol , vol.162 , Issue.3 , pp. 963-975
    • Bloor, B.K.1    Tidman, N.2    Leigh, I.M.3
  • 60
    • 0023072758 scopus 로고
    • Distribution of a special subset of keratinocytes characterized by the expression of cytokeratin 9 in adult and fetal human epidermis of various body sites
    • Moll I, Heid H, Franke WW, Moll R. Distribution of a special subset of keratinocytes characterized by the expression of cytokeratin 9 in adult and fetal human epidermis of various body sites. Differentiation 1987; 33(3): 254-265.
    • (1987) Differentiation , vol.33 , Issue.3 , pp. 254-265
    • Moll, I.1    Heid, H.2    Franke, W.W.3    Moll, R.4
  • 61
    • 0022033592 scopus 로고
    • Classification of human epithelia and their neoplasms using monoclonal antibodies to keratins: Strategies, applications, and limitations
    • Cooper D, Schermer A, Sun TT. Classification of human epithelia and their neoplasms using monoclonal antibodies to keratins: Strategies, applications, and limitations. Lab Invest 1985; 52(3): 243-256.
    • (1985) Lab Invest , vol.52 , Issue.3 , pp. 243-256
    • Cooper, D.1    Schermer, A.2    Sun, T.T.3
  • 62
    • 34249781403 scopus 로고    scopus 로고
    • Intermediate filaments and stress
    • Pekny M, Lane EB. Intermediate filaments and stress. Exp Cell Res 2007; 313(10): 2244-2254.
    • (2007) Exp Cell Res , vol.313 , Issue.10 , pp. 2244-2254
    • Pekny, M.1    Lane, E.B.2
  • 63
    • 0021940478 scopus 로고
    • Cytokeratin polypep-tide patterns of different epithelia of the human male urogenital tract: Immunofluorescence and gel electrophoretic studies
    • Achtstätter T, Moll R, Moore B, Franke WW. Cytokeratin polypep-tide patterns of different epithelia of the human male urogenital tract: Immunofluorescence and gel electrophoretic studies. J Histo-chem Cytochem 1985; 33(5): 415-426.
    • (1985) J Histo-chem Cytochem , vol.33 , Issue.5 , pp. 415-426
    • Achtstätter, T.1    Moll, R.2    Moore, B.3    Franke, W.W.4
  • 64
    • 0028025616 scopus 로고
    • Programming gene expression in developing epidermis
    • Byrne C, Tainsky M, Fuchs E. Programming gene expression in developing epidermis. Development 1994; 120(9): 2369-2383.
    • (1994) Development , vol.120 , Issue.9 , pp. 2369-2383
    • Byrne, C.1    Tainsky, M.2    Fuchs, E.3
  • 65
    • 34247243262 scopus 로고    scopus 로고
    • Keratin expression provides novel insight into the morphogenesis and function of the companion layer in hair follicles
    • Gu LH, Coulombe PA. Keratin expression provides novel insight into the morphogenesis and function of the companion layer in hair follicles. J Invest Dermatol 2007; 127(5): 1061-1073.
    • (2007) J Invest Dermatol , vol.127 , Issue.5 , pp. 1061-1073
    • Gu, L.H.1    Coulombe, P.A.2
  • 66
    • 0032457223 scopus 로고    scopus 로고
    • A novel human type II cytokeratin, K6hf, specifically expressed in the companion layer of the hair follicle
    • Winter H, Langbein L, Praetzel S, et al. A novel human type II cytokeratin, K6hf, specifically expressed in the companion layer of the hair follicle. J Invest Dermatol 1998; 111(6): 955-962.
    • (1998) J Invest Dermatol , vol.111 , Issue.6 , pp. 955-962
    • Winter, H.1    Langbein, L.2    Praetzel, S.3
  • 67
    • 36349026451 scopus 로고    scopus 로고
    • Expression of follicular sheath keratins in the normal nail with special reference to the morphological analysis of the distal nail unit
    • Perrin C. Expression of follicular sheath keratins in the normal nail with special reference to the morphological analysis of the distal nail unit. Am J Dermatopathol 2007; 29(6): 543-550.
    • (2007) Am J Dermatopathol , vol.29 , Issue.6 , pp. 543-550
    • Perrin, C.1
  • 68
    • 0023907744 scopus 로고
    • Patterns of expression of tricho-cytic and epithelial cytokeratins in mammalian tissues. I. Human and bovine hair follicles
    • Heid HW, Moll I, Franke WW. Patterns of expression of tricho-cytic and epithelial cytokeratins in mammalian tissues. I. Human and bovine hair follicles. Differentiation 1988; 37(2): 137-157.
    • (1988) Differentiation , vol.37 , Issue.2 , pp. 137-157
    • Heid, H.W.1    Moll, I.2    Franke, W.W.3
  • 69
    • 0029116226 scopus 로고
    • Elements controlling the expression and induction of the skin hyperproliferation-associated keratin K6
    • Navarro JM, Casatorres J, Jorcano JL. Elements controlling the expression and induction of the skin hyperproliferation-associated keratin K6. J Biol Chem 1995; 270(36): 21362-21367.
    • (1995) J Biol Chem , vol.270 , Issue.36 , pp. 21362-21367
    • Navarro, J.M.1    Casatorres, J.2    Jorcano, J.L.3
  • 70
    • 0022760931 scopus 로고
    • Amino acid sequence and gene organization of cytokeratin no. 19, an exceptional tail-less intermediate filament protein
    • Bader BL, Magin TM, Hatzfeld M, Franke WW. Amino acid sequence and gene organization of cytokeratin no. 19, an exceptional tail-less intermediate filament protein. EMBO J 1986; 5(8): 1865-1875.
    • (1986) EMBO J , vol.5 , Issue.8 , pp. 1865-1875
    • Bader, B.L.1    Magin, T.M.2    Hatzfeld, M.3    Franke, W.W.4
  • 71
    • 0019888709 scopus 로고
    • Diversity of cytokeratins. Differentiation specific expression of cytokeratin polypeptides in epithelial cells and tissues
    • Franke WW, Schiller DL, Moll R, et al. Diversity of cytokeratins. Differentiation specific expression of cytokeratin polypeptides in epithelial cells and tissues. J Mol Biol 1981; 153(4): 933-959.
    • (1981) J Mol Biol , vol.153 , Issue.4 , pp. 933-959
    • Franke, W.W.1    Schiller, D.L.2    Moll, R.3
  • 72
    • 0023551789 scopus 로고
    • Cytoskeletal components of lymphoid organs. I. Synthesis of cytokeratins 8 and 18 and desmin in subpopu-lations of extrafollicular reticulum cells of human lymph nodes, tonsils, and spleen
    • Franke WW, Moll R. Cytoskeletal components of lymphoid organs. I. Synthesis of cytokeratins 8 and 18 and desmin in subpopu-lations of extrafollicular reticulum cells of human lymph nodes, tonsils, and spleen. Differentiation 1987; 36(2): 145-163.
    • (1987) Differentiation , vol.36 , Issue.2 , pp. 145-163
    • Franke, W.W.1    Moll, R.2
  • 73
    • 0027500893 scopus 로고
    • Cytokeratins 8 and 18 in smooth muscle cells. Detection in human coronary artery, peripheral vascular, and vein graft disease and in transplantation-associated arteriosclerosis
    • Jahn L, Kreuzer J, von Hodenberg E, et al. Cytokeratins 8 and 18 in smooth muscle cells. Detection in human coronary artery, peripheral vascular, and vein graft disease and in transplantation-associated arteriosclerosis. Arterioscler Thromb 1993; 13(11): 1631-1639.
    • (1993) Arterioscler Thromb , vol.13 , Issue.11 , pp. 1631-1639
    • Jahn, L.1    Kreuzer, J.2    von Hodenberg, E.3
  • 74
    • 0023787238 scopus 로고
    • Transient coexpression of desmin and cy-tokeratins 8 and 18 in developing myocardial cells of some vertebrate species
    • Kuruc N, Franke WW. Transient coexpression of desmin and cy-tokeratins 8 and 18 in developing myocardial cells of some vertebrate species. Differentiation 1988; 38(3): 177-193.
    • (1988) Differentiation , vol.38 , Issue.3 , pp. 177-193
    • Kuruc, N.1    Franke, W.W.2
  • 75
    • 0024554854 scopus 로고
    • Cy-tokeratin expression in experimental murine rhabdomyosarcomas. Intermediate filament pattern in original tumors, allotransplants, cell culture and re-established tumors from cell culture
    • Langbein L, Kosmehl H, Kiss F, Katenkamp D, Neupert G. Cy-tokeratin expression in experimental murine rhabdomyosarcomas. Intermediate filament pattern in original tumors, allotransplants, cell culture and re-established tumors from cell culture. Exp Pathol 1989; 36(1): 23-36.
    • (1989) Exp Pathol , vol.36 , Issue.1 , pp. 23-36
    • Langbein, L.1    Kosmehl, H.2    Kiss, F.3    Katenkamp, D.4    Neupert, G.5
  • 76
    • 0032937850 scopus 로고    scopus 로고
    • Regulation of keratin 9 in nonpalmoplantar keratinocytes by palmoplantar fibroblasts through epithelial-mesenchymal interactions
    • Yamaguchi Y, Itami S, Tarutani M, Hosokawa K, Miura H, Yoshi-kawa K. Regulation of keratin 9 in nonpalmoplantar keratinocytes by palmoplantar fibroblasts through epithelial-mesenchymal interactions. J Invest Dermatol 1999; 112(4): 483-488.
    • (1999) J Invest Dermatol , vol.112 , Issue.4 , pp. 483-488
    • Yamaguchi, Y.1    Itami, S.2    Tarutani, M.3    Hosokawa, K.4    Miura, H.5    Yoshi-Kawa, K.6
  • 77
    • 0022621625 scopus 로고
    • Nonepidermal members of the keratin multigene family: CDNA sequences and in situ localization of the mRNAs
    • Knapp B, Rentrop M, Schweizer J, Winter H. Nonepidermal members of the keratin multigene family: cDNA sequences and in situ localization of the mRNAs. Nucleic Acids Res 1986; 14(2): 751-763.
    • (1986) Nucleic Acids Res , vol.14 , Issue.2 , pp. 751-763
    • Knapp, B.1    Rentrop, M.2    Schweizer, J.3    Winter, H.4
  • 78
    • 0027771149 scopus 로고
    • Molecular characterization of the body site-specific human epidermal cytokeratin 9: CDNA cloning, amino acid sequence, and tissue specificity of gene expression
    • Langbein L, Heid HW, Moll I, Franke WW. Molecular characterization of the body site-specific human epidermal cytokeratin 9: cDNA cloning, amino acid sequence, and tissue specificity of gene expression. Differentiation 1993; 55(1): 57-71.
    • (1993) Differentiation , vol.55 , Issue.1 , pp. 57-71
    • Langbein, L.1    Heid, H.W.2    Moll, I.3    Franke, W.W.4
  • 79
    • 0023892995 scopus 로고
    • Molecular characterization and expression of the stratification-related cytokeratins 4 and 15
    • Leube RE, Bader BL, Bosch FX, Zimbelmann R, Achtstaetter T, Franke WW. Molecular characterization and expression of the stratification-related cytokeratins 4 and 15. J Cell Biol 1988; 106(4): 1249-1261.
    • (1988) J Cell Biol , vol.106 , Issue.4 , pp. 1249-1261
    • Leube, R.E.1    Bader, B.L.2    Bosch, F.X.3    Zimbelmann, R.4    Achtstaetter, T.5    Franke, W.W.6
  • 80
    • 0032978261 scopus 로고    scopus 로고
    • Keratin 15 expression in stratified epithelia: Downregulation in activated keratinocytes
    • Waseem A, Dogan B, Tidman N, et al. Keratin 15 expression in stratified epithelia: Downregulation in activated keratinocytes. J Invest Dermatol 1999; 112(3): 362-369.
    • (1999) J Invest Dermatol , vol.112 , Issue.3 , pp. 362-369
    • Waseem, A.1    Dogan, B.2    Tidman, N.3
  • 81
    • 48749110372 scopus 로고    scopus 로고
    • Immunohistochemical markers for corneal stem cells in the early developing human eye
    • Lyngholm M, Høyer PE, Vorum H, Nielsen K, Ehlers N, Møllgård K. Immunohistochemical markers for corneal stem cells in the early developing human eye. Exp Eye Res 2008; 87(2): 115-121.
    • (2008) Exp Eye Res , vol.87 , Issue.2 , pp. 115-121
    • Lyngholm, M.1    Høyer, P.E.2    Vorum, H.3    Nielsen, K.4    Ehlers, N.5    Møllgård, K.6
  • 82
    • 0020394537 scopus 로고
    • Different keratin polypeptides in epidermis and other epithelia of human skin: A specific cytokeratin of molecular weight 46,000 in epithelia of the pilosebaceous tract and basal cell epitheliomas
    • Moll R, Franke WW, Volc-Platzer B, Krepler R. Different keratin polypeptides in epidermis and other epithelia of human skin: A specific cytokeratin of molecular weight 46,000 in epithelia of the pilosebaceous tract and basal cell epitheliomas. J Cell Biol 1982; 95(1): 285-295.
    • (1982) J Cell Biol , vol.95 , Issue.1 , pp. 285-295
    • Moll, R.1    Franke, W.W.2    Volc-Platzer, B.3    Krepler, R.4
  • 84
    • 0034118521 scopus 로고    scopus 로고
    • Keratin 17 expression in the hard epithelial context of the hair and nail, and its relevance for the pachyonychia congenita phenotype
    • McGowan KM, Coulombe PA. Keratin 17 expression in the hard epithelial context of the hair and nail, and its relevance for the pachyonychia congenita phenotype. J Invest Dermatol 2000; 114(6): 1101-1107.
    • (2000) J Invest Dermatol , vol.114 , Issue.6 , pp. 1101-1107
    • McGowan, K.M.1    Coulombe, P.A.2
  • 85
    • 33646552082 scopus 로고    scopus 로고
    • Keratin 17 modulates hair follicle cycling in a TNFa-dependent fashion
    • Tong X, Coulombe PA. Keratin 17 modulates hair follicle cycling in a TNFa-dependent fashion. Genes Dev 2006; 20(10): 1353-1364.
    • (2006) Genes Dev , vol.20 , Issue.10 , pp. 1353-1364
    • Tong, X.1    Coulombe, P.A.2
  • 87
    • 0027396448 scopus 로고
    • Special program of differentiation expressed in keratinocytes of human haarscheiben: An analysis of individual cytokeratin polypeptides
    • Moll I, Troyanovsky SM, Moll R. Special program of differentiation expressed in keratinocytes of human haarscheiben: An analysis of individual cytokeratin polypeptides. J Invest Dermatol 1993; 100(1): 69-76.
    • (1993) J Invest Dermatol , vol.100 , Issue.1 , pp. 69-76
    • Moll, I.1    Troyanovsky, S.M.2    Moll, R.3
  • 88
    • 0035110093 scopus 로고    scopus 로고
    • Immunostaining for thyroid transcription factor 1 and cytokeratin 20 aids the distinction of small cell carcinoma from Merkel cell carcinoma, but not pulmonary from extrapulmonary small cell carcinomas
    • Cheuk W, Kwan MY, Suster S, Chan JK. Immunostaining for thyroid transcription factor 1 and cytokeratin 20 aids the distinction of small cell carcinoma from Merkel cell carcinoma, but not pulmonary from extrapulmonary small cell carcinomas. Arch Pathol Lab Med 2001; 125(2): 228-231.
    • (2001) Arch Pathol Lab Med , vol.125 , Issue.2 , pp. 228-231
    • Cheuk, W.1    Kwan, M.Y.2    Suster, S.3    Chan, J.K.4
  • 89
    • 0033795923 scopus 로고    scopus 로고
    • Cytokeratin 7 and cytokeratin 20 expression in epithelial neoplasms: A survey of 435 cases
    • Chu P, Wu E, Weiss LM. Cytokeratin 7 and cytokeratin 20 expression in epithelial neoplasms: A survey of 435 cases. Mod Pathol 2000; 13(9): 962-972.
    • (2000) Mod Pathol , vol.13 , Issue.9 , pp. 962-972
    • Chu, P.1    Wu, E.2    Weiss, L.M.3
  • 90
    • 1842471992 scopus 로고    scopus 로고
    • Comprehensive analysis of keratin gene clusters in humans and rodents
    • Hesse M, Zimek A, Weber K, Magin TM. Comprehensive analysis of keratin gene clusters in humans and rodents. Eur J Cell Biol 2004; 83(1): 19-26.
    • (2004) Eur J Cell Biol , vol.83 , Issue.1 , pp. 19-26
    • Hesse, M.1    Zimek, A.2    Weber, K.3    Magin, T.M.4
  • 91
    • 0025951847 scopus 로고
    • Keratin expression in rat intestinal crypt and villus cells. Analysis with a panel of monoclonal antibodies
    • Quaroni A, Calnek D, Quaroni E, Chandler JS. Keratin expression in rat intestinal crypt and villus cells. Analysis with a panel of monoclonal antibodies. J Biol Chem 1991; 266(18): 11923-11931.
    • (1991) J Biol Chem , vol.266 , Issue.18 , pp. 11923-11931
    • Quaroni, A.1    Calnek, D.2    Quaroni, E.3    Chandler, J.S.4
  • 92
    • 0026044919 scopus 로고
    • Identification and characterization of rat intestinal keratins. Molecular cloning of cDNAs encoding cytokeratins 8, 19, and a new 49-kDa type I cytokeratin (cytokeratin 21) expressed by differentiated intestinal epithelial cells
    • Chandler JS, Calnek D, Quaroni A. Identification and characterization of rat intestinal keratins. Molecular cloning of cDNAs encoding cytokeratins 8, 19, and a new 49-kDa type I cytokeratin (cytokeratin 21) expressed by differentiated intestinal epithelial cells. J Biol Chem 1991; 266(18): 11932-11938.
    • (1991) J Biol Chem , vol.266 , Issue.18 , pp. 11932-11938
    • Chandler, J.S.1    Calnek, D.2    Quaroni, A.3
  • 93
    • 0034907507 scopus 로고    scopus 로고
    • Genes for intermediate filament proteins and the draft sequence of the human genome: Novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18
    • Hesse M, Magin TM, Weber K. Genes for intermediate filament proteins and the draft sequence of the human genome: Novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18. J Cell Sci 2001; 114(Pt 14): 2569-2575.
    • (2001) J Cell Sci , vol.114 , Issue.Pt 14 , pp. 2569-2575
    • Hesse, M.1    Magin, T.M.2    Weber, K.3
  • 94
    • 0036379424 scopus 로고    scopus 로고
    • Refined mapping of Nae-geli-Franceschetti-Jadassohn syndrome to a 6 cM interval on chromosome 17q11.2-q21 and investigation of candidate genes
    • Sprecher E, Itin P, Whittock NV, et al. Refined mapping of Nae-geli-Franceschetti-Jadassohn syndrome to a 6 cM interval on chromosome 17q11.2-q21 and investigation of candidate genes. J Invest Dermatol 2002; 119(3): 692-698.
    • (2002) J Invest Dermatol , vol.119 , Issue.3 , pp. 692-698
    • Sprecher, E.1    Itin, P.2    Whittock, N.V.3
  • 95
    • 0026802985 scopus 로고
    • Suprabasal marker proteins distinguishing keratinizing squamous epithelia: Cytokeratin 2 polypeptides of oral masticatory epithelium and epidermis are different
    • Collin C, Ouhayoun JP, Grund C, Franke WW. Suprabasal marker proteins distinguishing keratinizing squamous epithelia: Cytokeratin 2 polypeptides of oral masticatory epithelium and epidermis are different. Differentiation 1992; 51(2): 137-148.
    • (1992) Differentiation , vol.51 , Issue.2 , pp. 137-148
    • Collin, C.1    Ouhayoun, J.P.2    Grund, C.3    Franke, W.W.4
  • 96
    • 27144481402 scopus 로고    scopus 로고
    • Characterization of a novel human type II epithelial keratin K1b, specifically expressed in eccrine sweat glands
    • Langbein L, Rogers MA, Praetzel S, et al. Characterization of a novel human type II epithelial keratin K1b, specifically expressed in eccrine sweat glands. J Invest Dermatol 2005; 125(3): 428-444.
    • (2005) J Invest Dermatol , vol.125 , Issue.3 , pp. 428-444
    • Langbein, L.1    Rogers, M.A.2    Praetzel, S.3
  • 97
    • 44149107578 scopus 로고    scopus 로고
    • New concepts on the histogenesis of eccrine neoplasia from keratin expression in the normal eccrine gland, syringoma and poroma
    • Langbein L, Cribier B, Schirmacher P, Praetzel-Wunder S, Peltre B, Schweizer J. New concepts on the histogenesis of eccrine neoplasia from keratin expression in the normal eccrine gland, syringoma and poroma. Br J Dermatol 2008; 159(3): 633-645.
    • (2008) Br J Dermatol , vol.159 , Issue.3 , pp. 633-645
    • Langbein, L.1    Cribier, B.2    Schirmacher, P.3    Praetzel-Wunder, S.4    Peltre, B.5    Schweizer, J.6
  • 98
    • 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 MA, 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(28): 19874-19884.
    • (1999) J Biol Chem , vol.274 , Issue.28 , pp. 19874-19884
    • Langbein, L.1    Rogers, M.A.2    Winter, H.3
  • 99
    • 34248525591 scopus 로고    scopus 로고
    • Novel type I hair keratins K39 and K40 are the last to be expressed in differentiation of the hair: Completion of the human hair keratin catalog
    • Langbein L, Rogers MA, Praetzel-Wunder S, Böckler D, Schirmacher P, Schweizer J. Novel type I hair keratins K39 and K40 are the last to be expressed in differentiation of the hair: Completion of the human hair keratin catalog. J Invest Dermatol 2007; 127(6): 1532-155.
    • (2007) J Invest Dermatol , vol.127 , Issue.6 , pp. 1532-1535
    • Langbein, L.1    Rogers, M.A.2    Praetzel-Wunder, S.3    Böckler, D.4    Schirmacher, P.5    Schweizer, J.6
  • 100
    • 40549123948 scopus 로고    scopus 로고
    • The Human Intermediate Filament Database: Comprehensive information on a gene family involved in many human diseases
    • Szeverenyi I, Cassidy AJ, Chung CW, et al. The Human Intermediate Filament Database: Comprehensive information on a gene family involved in many human diseases. Hum Mutat 2008; 29(3): 351-360.
    • (2008) Hum Mutat , vol.29 , Issue.3 , pp. 351-360
    • Szeverenyi, I.1    Cassidy, A.J.2    Chung, C.W.3
  • 101
    • 2442562175 scopus 로고    scopus 로고
    • On the regulation of hair keratin expression: Lessons from studies in pilo-matricomas
    • Cribier B, Peltre B, Grosshans E, Langbein L, Schweizer J. On the regulation of hair keratin expression: Lessons from studies in pilo-matricomas. J Invest Dermatol 2004; 122(5): 1078-1083.
    • (2004) J Invest Dermatol , vol.122 , Issue.5 , pp. 1078-1083
    • Cribier, B.1    Peltre, B.2    Grosshans, E.3    Langbein, L.4    Schweizer, J.5
  • 102
    • 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(37): 35123-35132.
    • (2001) J Biol Chem , vol.276 , Issue.37 , pp. 35123-35132
    • Langbein, L.1    Rogers, M.A.2    Winter, H.3    Praetzel, S.4    Schweizer, J.5
  • 105
    • 0032722830 scopus 로고    scopus 로고
    • Whn and mHa3 are components of the genetic hierarchy controlling hair follicle differentiation
    • Meier N, Dear TN, Boehm T. Whn and mHa3 are components of the genetic hierarchy controlling hair follicle differentiation. Mech Dev 1999; 89(1-2): 215-221.
    • (1999) Mech Dev , vol.89 , Issue.1-2 , pp. 215-221
    • Meier, N.1    Dear, T.N.2    Boehm, T.3
  • 106
    • 1842639500 scopus 로고    scopus 로고
    • Androgen regulation of the human hair follicle: The type I hair keratin hHa7 is a direct target gene in trichocytes
    • Jave-Suarez LF, Langbein L, Winter H, Praetzel S, Rogers MA, Schweizer J. Androgen regulation of the human hair follicle: The type I hair keratin hHa7 is a direct target gene in trichocytes. J Invest Dermatol 2004; 122(3): 555-564.
    • (2004) J Invest Dermatol , vol.122 , Issue.3 , pp. 555-564
    • Jave-Suarez, L.F.1    Langbein, L.2    Winter, H.3    Praetzel, S.4    Rogers, M.A.5    Schweizer, J.6
  • 107
    • 0038100445 scopus 로고    scopus 로고
    • Origin of feathers: Feather beta (beta) keratins are expressed in discrete epidermal cell populations of embryonic scutate scales
    • Sawyer RH, Salvatore BA, Potylicki TT, French JO, Glenn TC, Knapp LW. Origin of feathers: Feather beta (beta) keratins are expressed in discrete epidermal cell populations of embryonic scutate scales. J Exp Zool B Mol Dev Evol 2003; 295(1): 12-24.
    • (2003) J Exp Zool B Mol Dev Evol , vol.295 , Issue.1 , 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
  • 108
    • 0026261881 scopus 로고
    • Region-specific expression of scutate scale type beta keratins in the developing chick beak
    • Shames RB, Knapp LW, Carver WE, Sawyer RH. Region-specific expression of scutate scale type beta keratins in the developing chick beak. J Exp Zool 1991; 260(2): 258-266.
    • (1991) J Exp Zool , vol.260 , Issue.2 , pp. 258-266
    • Shames, R.B.1    Knapp, L.W.2    Carver, W.E.3    Sawyer, R.H.4
  • 109
    • 0024395397 scopus 로고
    • Keratinization of the outer surface of the avian scutate scale: Interrelationship of alpha and beta keratin filaments in a cornifying tissue
    • Shames RB, Knapp LW, Carver WE, Washington LD, Sawyer RH. Keratinization of the outer surface of the avian scutate scale: Interrelationship of alpha and beta keratin filaments in a cornifying tissue. Cell Tissue Res 1989; 257(1): 85-92.
    • (1989) Cell Tissue Res , vol.257 , Issue.1 , pp. 85-92
    • Shames, R.B.1    Knapp, L.W.2    Carver, W.E.3    Washington, L.D.4    Sawyer, R.H.5
  • 110
    • 33646134612 scopus 로고    scopus 로고
    • Genes coding for intermediate filament proteins closely related to the hagfish "thread keratins (TK)" alpha and gamma also exist in lamprey, teleosts and amphibians
    • Schaffeld M, Schultess J. Genes coding for intermediate filament proteins closely related to the hagfish "thread keratins (TK)" alpha and gamma also exist in lamprey, teleosts and amphibians. Exp Cell Res 2006; 312(9): 1447-1462.
    • (2006) Exp Cell Res , vol.312 , Issue.9 , pp. 1447-1462
    • Schaffeld, M.1    Schultess, J.2
  • 111
    • 34347257429 scopus 로고    scopus 로고
    • A novel and ancient group of type I keratins with members in bichir, sturgeon and gar
    • Schaffeld M, Haberkamp M, Schätzlein S, Neumann S, Hunzinger C. A novel and ancient group of type I keratins with members in bichir, sturgeon and gar. Front Zool 2007; 4: 16.
    • (2007) Front Zool , vol.4 , pp. 16
    • Schaffeld, M.1    Haberkamp, M.2    Schätzlein, S.3    Neumann, S.4    Hunzinger, C.5
  • 112
    • 84867682806 scopus 로고    scopus 로고
    • Keratinization and its disorders
    • Shetty S, Gokul S. Keratinization and its disorders. Oman Med J 2012; 27(5): 348-357.
    • (2012) Oman Med J , vol.27 , Issue.5 , pp. 348-357
    • Shetty, S.1    Gokul, S.2
  • 113
    • 0034533621 scopus 로고    scopus 로고
    • Epithelial structural proteins of the skin and oral cavity: Function in health and disease
    • Presland RB, Dale BA. Epithelial structural proteins of the skin and oral cavity: Function in health and disease. Crit Rev Oral Biol Med 2000; 11(4): 383-408.
    • (2000) Crit Rev Oral Biol Med , vol.11 , Issue.4 , pp. 383-408
    • Presland, R.B.1    Dale, B.A.2
  • 115
    • 0037684800 scopus 로고    scopus 로고
    • Keratin 8 protection of placental barrier function
    • Jaquemar D, Kupriyanov S, Wankell M, et al. Keratin 8 protection of placental barrier function. J Cell Biol 2003; 161(4): 749-756.
    • (2003) J Cell Biol , vol.161 , Issue.4 , pp. 749-756
    • Jaquemar, D.1    Kupriyanov, S.2    Wankell, M.3
  • 116
    • 0034599872 scopus 로고    scopus 로고
    • Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis
    • Caulin C, Ware CF, Magin TM, Oshima RG. Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis. J Cell Biol 2000; 149(1): 17-22.
    • (2000) J Cell Biol , vol.149 , Issue.1 , pp. 17-22
    • Caulin, C.1    Ware, C.F.2    Magin, T.M.3    Oshima, R.G.4
  • 117
    • 7944221186 scopus 로고    scopus 로고
    • The keratin cy-toskeleton in liver diseases
    • Zatloukal K, Stumptner C, Fuchsbichler A, et al. The keratin cy-toskeleton in liver diseases. J Pathol 2004; 204(4): 367-376.
    • (2004) J Pathol , vol.204 , Issue.4 , pp. 367-376
    • Zatloukal, K.1    Stumptner, C.2    Fuchsbichler, A.3
  • 118
    • 0037847551 scopus 로고    scopus 로고
    • Keratin mutation in transgenic mice predisposes to Fas but not TNF-induced apoptosis and massive liver injury
    • Ku NO, Soetikno RM, Omary MB. Keratin mutation in transgenic mice predisposes to Fas but not TNF-induced apoptosis and massive liver injury. Hepatology 2003; 37(5): 1006-1014.
    • (2003) Hepatology , vol.37 , Issue.5 , pp. 1006-1014
    • Ku, N.O.1    Soetikno, R.M.2    Omary, M.B.3
  • 119
    • 33745003902 scopus 로고    scopus 로고
    • A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth
    • Kim S, Wong P, Coulombe PA. A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth. Nature 2006; 441(7091): 362-365.
    • (2006) Nature , vol.441 , Issue.7091 , pp. 362-365
    • Kim, S.1    Wong, P.2    Coulombe, P.A.3
  • 120
    • 34249659606 scopus 로고    scopus 로고
    • Intermediate filaments: A role in epithelial polarity
    • Oriolo AS, Wald FA, Ramsauer VP, Salas PJ. Intermediate filaments: A role in epithelial polarity. Exp Cell Res 2007; 313(10): 2255-2264.
    • (2007) Exp Cell Res , vol.313 , Issue.10 , pp. 2255-2264
    • Oriolo, A.S.1    Wald, F.A.2    Ramsauer, V.P.3    Salas, P.J.4
  • 121
    • 34848819378 scopus 로고    scopus 로고
    • Keratins: Markers of cell differentiation or regulators of cell differentiation?
    • Vaidya MM, Kanojia D. Keratins: Markers of cell differentiation or regulators of cell differentiation? J Biosci 2007; 32(4): 629-634.
    • (2007) J Biosci , vol.32 , Issue.4 , pp. 629-634
    • Vaidya, M.M.1    Kanojia, D.2
  • 122
    • 33847217610 scopus 로고    scopus 로고
    • Mechanisms of sensory transduction in the skin
    • Lumpkin EA, Caterina MJ. Mechanisms of sensory transduction in the skin. Nature 2007; 445(7130): 858-865.
    • (2007) Nature , vol.445 , Issue.7130 , pp. 858-865
    • Lumpkin, E.A.1    Caterina, M.J.2
  • 123
    • 0036090767 scopus 로고    scopus 로고
    • Keratin expression in human tissues and neoplasms
    • Chu PG, Weiss LM. Keratin expression in human tissues and neoplasms. Histopathology 2002; 40(5): 403-439.
    • (2002) Histopathology , vol.40 , Issue.5 , pp. 403-439
    • Chu, P.G.1    Weiss, L.M.2
  • 124
    • 77956092359 scopus 로고    scopus 로고
    • A Review of Keratin-Based Biomaterials for Biomedical Applications
    • Ouse JG, Van Dyke ME. A Review of Keratin-Based Biomaterials for Biomedical Applications. Materials 2010; 3, 999-1014.
    • (2010) Materials , vol.3 , pp. 999-1014
    • Ouse, J.G.1    van Dyke, M.E.2
  • 125
    • 84888394945 scopus 로고
    • Keratin and other coatings for pills
    • Dale HN. Keratin and other coatings for pills. Pharm J 1932; 129: 494-5.
    • (1932) Pharm J , vol.129 , pp. 494-495
    • Dale, H.N.1
  • 126
    • 84876728962 scopus 로고    scopus 로고
    • The use of keratin in biomedical applications
    • Vasconcelos A, Cavaco-Paulo A. The use of keratin in biomedical applications. Curr Drug Targets 2013; 14(5): 612-619.
    • (2013) Curr Drug Targets , vol.14 , Issue.5 , pp. 612-619
    • Vasconcelos, A.1    Cavaco-Paulo, A.2
  • 127
    • 78650842405 scopus 로고    scopus 로고
    • Growth factor delivery-based tissue engineering: General approaches and a review of recent developments
    • Lee K, Silva EA, Mooney DJ. Growth factor delivery-based tissue engineering: General approaches and a review of recent developments. J R Soc Interface 2011; 8(55): 153-170.
    • (2011) J R Soc Interface , vol.8 , Issue.55 , pp. 153-170
    • Lee, K.1    Silva, E.A.2    Mooney, D.J.3
  • 128
    • 84888423781 scopus 로고    scopus 로고
    • Method of preparing keratin-containing films and coatings
    • Anker CA. Method of preparing keratin-containing films and coatings. US Pat. 3,642,498.
    • US Pat. 3 , vol.642 , pp. 498
    • Anker, C.A.1
  • 129
    • 77955983599 scopus 로고
    • Film and gels of keratin
    • Kawano Y, Okamoto S. Film and gels of keratin. Kagaku Seibutsu 1975; 13: 291-292.
    • (1975) Kagaku Seibutsu , vol.13 , pp. 291-292
    • Kawano, Y.1    Okamoto, S.2
  • 130
    • 77955985476 scopus 로고
    • Formation of films from some proteins
    • Okamoto S. Formation of films from some proteins. Nippon Sho-kuhin Kogyo Gakkaishi 1977; 24: 40-50.
    • (1977) Nippon Sho-kuhin Kogyo Gakkaishi , vol.24 , pp. 40-50
    • Okamoto, S.1
  • 133
    • 84996319901 scopus 로고
    • Application of Denatured Wool Keratin Derivatives to an Antithrombogenic Biomate-rial-Vascular Graft Coated with a Heparinized Keratin Derivative
    • Noishiki Y, Ito H, Miyamoto T, Inagaki H. Application of Denatured Wool Keratin Derivatives to an Antithrombogenic Biomate-rial-Vascular Graft Coated with a Heparinized Keratin Derivative. Kobunshi Ronbunshu 1982; 39: 221-227.
    • (1982) Kobunshi Ronbunshu , vol.39 , pp. 221-227
    • Noishiki, Y.1    Ito, H.2    Miyamoto, T.3    Inagaki, H.4
  • 134
    • 0017054951 scopus 로고
    • Self-assembly of bovine epidermal keratin filaments in vitro
    • Steinert PM, Idler WW, Zimmerman SB. Self-assembly of bovine epidermal keratin filaments in vitro. J Mol Biol 1976; 108(3): 547-567.
    • (1976) J Mol Biol , vol.108 , Issue.3 , pp. 547-567
    • Steinert, P.M.1    Idler, W.W.2    Zimmerman, S.B.3
  • 135
    • 43149083069 scopus 로고    scopus 로고
    • Preparation of scaffolds from human hair proteins fortissue-engineering applications
    • Verma V, Verma P, Ray P, Ray AR. Preparation of scaffolds from human hair proteins fortissue-engineering applications. Biomed Mater 2008; 3: 25007.
    • (2008) Biomed Mater , vol.3 , pp. 25007
    • Verma, V.1    Verma, P.2    Ray, P.3    Ray, A.R.4
  • 136
    • 77956092359 scopus 로고    scopus 로고
    • A review of keratin-based biomaterials for biomedical applications
    • Rouse JG, Van Dyke ME. A review of keratin-based biomaterials for biomedical applications. Materials 2010; 3(2): 999-1014.
    • (2010) Materials , vol.3 , Issue.2 , pp. 999-1014
    • Rouse, J.G.1    van Dyke, M.E.2
  • 137
    • 84898619849 scopus 로고    scopus 로고
    • Natural products: A minefield of biomaterials
    • 2012
    • Ige OO, Umoru LE, Aribo S. Natural products: A minefield of biomaterials. ISRN Mater Sci 2012; 2012: 983062.
    • (2012) ISRN Mater Sci , pp. 983062
    • Ige, O.O.1    Umoru, L.E.2    Aribo, S.3
  • 138
    • 77955983599 scopus 로고
    • Film and gel of keratins
    • Kawano Y, Okamoto S. Film and gel of keratins. Kagaku To Seibutsu 1975; 13(5): 291-292.
    • (1975) Kagaku to Seibutsu , vol.13 , Issue.5 , pp. 291-292
    • Kawano, Y.1    Okamoto, S.2
  • 139
    • 2442480190 scopus 로고    scopus 로고
    • Convenient procedures for human hair protein films and properties of alkaline phosphatase incorporated in the film
    • Fujii T, Ogiwara D, Arimoto M. Convenient procedures for human hair protein films and properties of alkaline phosphatase incorporated in the film. Biol. Pharm. Bull. 2004; 27: 89-93.
    • (2004) Biol. Pharm. Bull , vol.27 , pp. 89-93
    • Fujii, T.1    Ogiwara, D.2    Arimoto, M.3
  • 140
    • 0030221804 scopus 로고    scopus 로고
    • Preparation of stable aqueous solution of keratins, and physio-chemical and biodegradational properties of films
    • Yamauchi K, Yamauchi A, Kusunoki T, Kohda A, Konishi Y. Preparation of stable aqueous solution of keratins, and physio-chemical and biodegradational properties of films. J Biomed Mater Res 1996; 31: 439-444.
    • (1996) J Biomed Mater Res , vol.31 , pp. 439-444
    • Yamauchi, K.1    Yamauchi, A.2    Kusunoki, T.3    Kohda, A.4    Konishi, Y.5
  • 141
    • 0031921222 scopus 로고    scopus 로고
    • Cultivation of fibroblast cells on keratin-coated substrata
    • Yamauchi K, Maniwa M, Mori T. Cultivation of fibroblast cells on keratin-coated substrata. J Biomat Sci Polym E 1998; 9: 259-270.
    • (1998) J Biomat Sci Polym E , vol.9 , pp. 259-270
    • Yamauchi, K.1    Maniwa, M.2    Mori, T.3
  • 143
    • 84871406000 scopus 로고    scopus 로고
    • Injectable hydrogel therapies and their delivery strategies for treating myocardial infarction
    • Johnson TD, Christman KL. Injectable hydrogel therapies and their delivery strategies for treating myocardial infarction. Expert Opin Drug Deliv 2013; 10(1): 59-72.
    • (2013) Expert Opin Drug Deliv , vol.10 , Issue.1 , pp. 59-72
    • Johnson, T.D.1    Christman, K.L.2
  • 144
    • 43149096456 scopus 로고    scopus 로고
    • Biodegradable materials based on silk fibroin and keratin
    • Vasconcelos A, Freddi G, Cavaco-Paulo A. Biodegradable materials based on silk fibroin and keratin. Biomacromolecules 2008; 9(4): 1299-1305.
    • (2008) Biomacromolecules , vol.9 , Issue.4 , pp. 1299-1305
    • Vasconcelos, A.1    Freddi, G.2    Cavaco-Paulo, A.3
  • 146
    • 2342445077 scopus 로고    scopus 로고
    • A covalent method of gen-tamicin bonding to silica supports
    • Ginalska G, Osihska M, Uryniak A. A covalent method of gen-tamicin bonding to silica supports. J Biomater Appl 2004; 18(4): 279-289.
    • (2004) J Biomater Appl , vol.18 , Issue.4 , pp. 279-289
    • Ginalska, G.1    Osihska, M.2    Uryniak, A.3
  • 147
    • 65549127212 scopus 로고    scopus 로고
    • Covalent coating of hy-droxyapatite by keratin stabilizes gentamicin release
    • Belcarz A, Ginalska G, Zalewska J, et al. Covalent coating of hy-droxyapatite by keratin stabilizes gentamicin release. J Biomed Mater Res B Appl Biomater 2009; 89(1): 102-113.
    • (2009) J Biomed Mater Res B Appl Biomater , vol.89 , Issue.1 , pp. 102-113
    • Belcarz, A.1    Ginalska, G.2    Zalewska, J.3
  • 148
    • 80051470807 scopus 로고    scopus 로고
    • Keratin hydrogels support the sustained release of bioactive ciprofloxacin
    • Saul JM, Ellenburg MD, de Guzman RC, Van Dyke M. Keratin hydrogels support the sustained release of bioactive ciprofloxacin. J Biomed Mater Res A 2011; 98(4): 544-553.
    • (2011) J Biomed Mater Res A , vol.98 , Issue.4 , pp. 544-553
    • Saul, J.M.1    Ellenburg, M.D.2    de Guzman, R.C.3    van Dyke, M.4
  • 149
    • 80052085881 scopus 로고    scopus 로고
    • Keratin capped silver nanoparticles - Synthesis and characterization of a nanoma-terial with desirable handling properties
    • Martin JJ, Cardamone JM, Irwin PL, Brown EM. Keratin capped silver nanoparticles - Synthesis and characterization of a nanoma-terial with desirable handling properties. Colloids Surf B Biointer-faces 2011; 88(1): 354-361.
    • (2011) Colloids Surf B Biointer-faces , vol.88 , Issue.1 , pp. 354-361
    • Martin, J.J.1    Cardamone, J.M.2    Irwin, P.L.3    Brown, E.M.4
  • 150
    • 0036132496 scopus 로고    scopus 로고
    • Preparation and characterization of keratinchitosan composite film
    • Tanabe T, Okitsu N, Tachibana A, Yamauchi K. Preparation and characterization of keratinchitosan composite film. Biomaterials 2002; 23: 817-825.
    • (2002) Biomaterials , vol.23 , pp. 817-825
    • Tanabe, T.1    Okitsu, N.2    Tachibana, A.3    Yamauchi, K.4
  • 152
    • 0031687593 scopus 로고    scopus 로고
    • Effect of surface properties on the antithrombogenicity of silk fibroin/S-carboxymethyl kerateine blend films
    • Lee KY, Kong SJ, Park WH, Ha WS, Kwon IC. Effect of surface properties on the antithrombogenicity of silk fibroin/S-carboxymethyl kerateine blend films. J Biomater Sci Polym Ed 1998; 9: 905-914.
    • (1998) J Biomater Sci Polym Ed , vol.9 , pp. 905-914
    • Lee, K.Y.1    Kong, S.J.2    Park, W.H.3    Ha, W.S.4    Kwon, I.C.5
  • 154
    • 84865788328 scopus 로고    scopus 로고
    • Biological stimuli responsive drug carriers based on keratin for triggerable drug delivery
    • Li Q, Zhu L, Liu R, et al. Biological stimuli responsive drug carriers based on keratin for triggerable drug delivery. J Mater Chem 2012; 22: 19964-19973.
    • (2012) J Mater Chem , vol.22 , pp. 19964-19973
    • Li, Q.1    Zhu, L.2    Liu, R.3
  • 156
    • 42449142255 scopus 로고    scopus 로고
    • Cosmetic effectiveness of topically applied hydrolysed keratin peptides and lipids derived from wool
    • Barba C, Méndez S, Roddick-Lanzilotta A, Kelly R, Parra JL, Coderch L. Cosmetic effectiveness of topically applied hydrolysed keratin peptides and lipids derived from wool. Skin Res Technol 2008; 14(2): 24324-8.
    • (2008) Skin Res Technol , vol.14 , Issue.2 , pp. 24324-24328
    • Barba, C.1    Méndez, S.2    Roddick-Lanzilotta, A.3    Kelly, R.4    Parra, J.L.5    Coderch, L.6
  • 157
    • 84861207737 scopus 로고    scopus 로고
    • Keratin films from chicken feathers for controlled drug release
    • Li FY, Wang RM, He YF, et al. Keratin films from chicken feathers for controlled drug release. J Control Release 2011; 152(Suppl 1): e92-e93.
    • (2011) J Control Release , vol.152 , Issue.SUPPL. 1
    • Li, F.Y.1    Wang, R.M.2    He, Y.F.3
  • 158
    • 84885332218 scopus 로고    scopus 로고
    • Study on effective extraction of chicken feather keratins and their films for controlling drug release
    • Yin XC, Li FY, He YF, Wang Y, Wang RM. Study on effective extraction of chicken feather keratins and their films for controlling drug release. Biomater Sci 2013; 1(5): 528-536.
    • (2013) Biomater Sci , vol.1 , Issue.5 , pp. 528-536
    • Yin, X.C.1    Li, F.Y.2    He, Y.F.3    Wang, Y.4    Wang, R.M.5
  • 159
    • 0029874973 scopus 로고    scopus 로고
    • The physicochemical and bio-pharmaceutical properties of fragmented keratin as a new drug carrier
    • Noda J, Imai T, Kida K, Otagiri M. The physicochemical and bio-pharmaceutical properties of fragmented keratin as a new drug carrier. Biol Pharm Bull 1996; 19(3): 466-473.
    • (1996) Biol Pharm Bull , vol.19 , Issue.3 , pp. 466-473
    • Noda, J.1    Imai, T.2    Kida, K.3    Otagiri, M.4
  • 160
    • 84885914397 scopus 로고    scopus 로고
    • Regenerated keratin proteins as potential biomaterial for drug delivery
    • in press, early view online version (Jul 24)
    • Cilurzo F, Selmin F, Aluigi A, Bellosta S. Regenerated keratin proteins as potential biomaterial for drug delivery. Polym Adv Technol 2013; in press, early view online version (Jul 24).
    • (2013) Polym Adv Technol
    • Cilurzo, F.1    Selmin, F.2    Aluigi, A.3    Bellosta, S.4
  • 161
    • 0030438462 scopus 로고    scopus 로고
    • Pharmacological advantages of conjugation of Cu,Zn-superoxide dismutase with succiny-lated keratin fragment: Improvement of biological properties and resistance to oxidative damage
    • Noda J, Otagiri M, Akaike T, Maeda H. Pharmacological advantages of conjugation of Cu,Zn-superoxide dismutase with succiny-lated keratin fragment: Improvement of biological properties and resistance to oxidative damage. J Pharmacol Exp Ther 1996; 279(1): 162-171.
    • (1996) J Pharmacol Exp Ther , vol.279 , Issue.1 , pp. 162-171
    • Noda, J.1    Otagiri, M.2    Akaike, T.3    Maeda, H.4
  • 163
    • 84876728962 scopus 로고    scopus 로고
    • The use of keratin in biomedical applications
    • Vasconcelos A, Cavaco-Paulo A. The use of keratin in biomedical applications. Curr Drug Targets 2013; 14(5): 612-619.
    • (2013) Curr Drug Targets , vol.14 , Issue.5 , pp. 612-619
    • Vasconcelos, A.1    Cavaco-Paulo, A.2
  • 164
    • 84856747493 scopus 로고    scopus 로고
    • Characterization of keratin- collagen 3D scaffold for biomedical applications
    • Balaji S, Kumar R, Sripriya R, et al. Characterization of keratin- collagen 3D scaffold for biomedical applications. Polym Adv Technol 2012; 23(3): 500-507.
    • (2012) Polym Adv Technol , vol.23 , Issue.3 , pp. 500-507
    • Balaji, S.1    Kumar, R.2    Sripriya, R.3
  • 165
    • 84863400618 scopus 로고    scopus 로고
    • Preparation and comparative characterization of keratin-chitosan and keratin-gelatin composite scaffolds for tissue engineering applications
    • Balaji S, Kumar R, Sripriya R, et al. Preparation and comparative characterization of keratin-chitosan and keratin-gelatin composite scaffolds for tissue engineering applications. Mater Sci Eng C 2012; 32(4): 975-982.
    • (2012) Mater Sci Eng C , vol.32 , Issue.4 , pp. 975-982
    • Balaji, S.1    Kumar, R.2    Sripriya, R.3
  • 166
    • 84881160805 scopus 로고    scopus 로고
    • Fabrication of nanofibrous scaffold using a PLA and hagfish thread keratin composite; its effect on cell adherence, growth, and osteoblast differentiation
    • Kim BS, Park KE, Park WH, Lee J. Fabrication of nanofibrous scaffold using a PLA and hagfish thread keratin composite; its effect on cell adherence, growth, and osteoblast differentiation. Bio-med Mater 2013; 8(4): 045006.
    • (2013) Bio-med Mater , vol.8 , Issue.4 , pp. 045006
    • Kim, B.S.1    Park, K.E.2    Park, W.H.3    Lee, J.4
  • 167
    • 78249265611 scopus 로고    scopus 로고
    • Photochemical crosslinking of soluble wool keratins produces a mechanically stable biomaterial that supports cell adhesion and proliferation
    • Sando L, Kim M, Colgrave ML, Ramshaw JA, Werkmeister JA, Elvin CM. Photochemical crosslinking of soluble wool keratins produces a mechanically stable biomaterial that supports cell adhesion and proliferation. J Biomed Mater Res A 2010; 95(3): 901-911.
    • (2010) J Biomed Mater Res A , vol.95 , Issue.3 , pp. 901-911
    • Sando, L.1    Kim, M.2    Colgrave, M.L.3    Ramshaw, J.A.4    Werkmeister, J.A.5    Elvin, C.M.6
  • 168
    • 70350208796 scopus 로고    scopus 로고
    • Films based on human hair keratin as substrates for cell culture and tissue engineering
    • Reichl S. Films based on human hair keratin as substrates for cell culture and tissue engineering. Biomaterials 2009; 30(36): 6854-6866.
    • (2009) Biomaterials , vol.30 , Issue.36 , pp. 6854-6866
    • Reichl, S.1
  • 169
    • 84873099789 scopus 로고    scopus 로고
    • Hemostatic properties and the role of cell receptor recognition in human hair keratin protein hydrogels
    • Burnett LR, Rahmany MB, Richter JR, et al. Hemostatic properties and the role of cell receptor recognition in human hair keratin protein hydrogels. Biomaterials 2013; 34(11): 2632-2640.
    • (2013) Biomaterials , vol.34 , Issue.11 , pp. 2632-2640
    • Burnett, L.R.1    Rahmany, M.B.2    Richter, J.R.3
  • 170
    • 0345869626 scopus 로고    scopus 로고
    • Preparation and physicochemical properties of compression-molded keratin films
    • Katoh K, Shibayama M, Tanabe T, Yamauchi K. Preparation and physicochemical properties of compression-molded keratin films. Biomaterials 2004; 25(12): 2265-2272.
    • (2004) Biomaterials , vol.25 , Issue.12 , pp. 2265-2272
    • Katoh, K.1    Shibayama, M.2    Tanabe, T.3    Yamauchi, K.4
  • 171
    • 84862817788 scopus 로고    scopus 로고
    • Human keratin hydrogels support fibroblast attachment and proliferation in vitro
    • Wang S, Taraballi F, Tan LP, Ng KW. Human keratin hydrogels support fibroblast attachment and proliferation in vitro. Cell Tissue Res 2012; 347(3): 795-802.
    • (2012) Cell Tissue Res , vol.347 , Issue.3 , pp. 795-802
    • Wang, S.1    Taraballi, F.2    Tan, L.P.3    Ng, K.W.4
  • 172
    • 0037074717 scopus 로고    scopus 로고
    • Fabrication of wool keratin sponge scaffolds for long-term cell cultivation
    • Tachibana A, Furuta Y, Takeshima H, Tanabe T, Yamauchi K. Fabrication of wool keratin sponge scaffolds for long-term cell cultivation. J Biotechnol 2002; 93(2): 165-170.
    • (2002) J Biotechnol , vol.93 , Issue.2 , pp. 165-170
    • Tachibana, A.1    Furuta, Y.2    Takeshima, H.3    Tanabe, T.4    Yamauchi, K.5
  • 173
    • 3242678876 scopus 로고    scopus 로고
    • Rapid fabrication of keratin-hydroxyapatite hybrid sponges toward osteoblast cultivation and differentiation
    • Tachibana A, Kaneko S, Tanabe T, Yamauchi K. Rapid fabrication of keratin-hydroxyapatite hybrid sponges toward osteoblast cultivation and differentiation. Biomaterials 2005; 26(3): 297-302.
    • (2005) Biomaterials , vol.26 , Issue.3 , pp. 297-302
    • Tachibana, A.1    Kaneko, S.2    Tanabe, T.3    Yamauchi, K.4
  • 174
    • 0036132496 scopus 로고    scopus 로고
    • Preparation and characterization of keratin-chitosan composite film
    • Tanabe T, Okitsu N, Tachibana A, Yamauchi K. Preparation and characterization of keratin-chitosan composite film. Biomaterials 2002; 23(3): 817-825.
    • (2002) Biomaterials , vol.23 , Issue.3 , pp. 817-825
    • Tanabe, T.1    Okitsu, N.2    Tachibana, A.3    Yamauchi, K.4
  • 175
    • 80655139381 scopus 로고    scopus 로고
    • Preparation and mechanical evaluations of a novel keratin-chitosan-gelatin composite film
    • Bazargan-Lari R, Bahrololoom ME, Nemati A. Preparation and mechanical evaluations of a novel keratin-chitosan-gelatin composite film. World Appl Sci J 2009; 7(6): 763-768.
    • (2009) World Appl Sci J , vol.7 , Issue.6 , pp. 763-768
    • Bazargan-Lari, R.1    Bahrololoom, M.E.2    Nemati, A.3
  • 176
    • 3242678876 scopus 로고    scopus 로고
    • Rapid fabrication of keratin-hydroxyapatite hybrid sponges toward osteoblast cultivation and differentiation
    • Tachibana A, Kaneko S, Tanabe T, Yamauchi K. Rapid fabrication of keratin-hydroxyapatite hybrid sponges toward osteoblast cultivation and differentiation. Biomaterials 2005; 26: 297-302.
    • (2005) Biomaterials , vol.26 , pp. 297-302
    • Tachibana, A.1    Kaneko, S.2    Tanabe, T.3    Yamauchi, K.4
  • 177
    • 33845624475 scopus 로고    scopus 로고
    • Modified keratin sponge: Binding of bone morphoge-netic protein-2 and osteoblast differentiation
    • Tachibana A, Nishikawa Y, Nishino M, Kaneko S, Tanabe T, Ya-mauchi K. Modified keratin sponge: Binding of bone morphoge-netic protein-2 and osteoblast differentiation. J Biosci Bioeng 2006; 102: 425-429.
    • (2006) J Biosci Bioeng , vol.102 , pp. 425-429
    • Tachibana, A.1    Nishikawa, Y.2    Nishino, M.3    Kaneko, S.4    Tanabe, T.5    Ya-Mauchi, K.6
  • 181
    • 84855939485 scopus 로고    scopus 로고
    • Structure-property relationships of meta-kerateine biomaterials derived from human hair
    • Richter JR, de Guzman RC, Greengauz-Roberts OK, Van Dyke M. Structure-property relationships of meta-kerateine biomaterials derived from human hair. Acta Biomater 2012; 8(1): 274-281.
    • (2012) Acta Biomater , vol.8 , Issue.1 , pp. 274-281
    • Richter, J.R.1    de Guzman, R.C.2    Greengauz-Roberts, O.K.3    van Dyke, M.4
  • 182
    • 80051550967 scopus 로고    scopus 로고
    • Mechanisms of hepa-tocyte attachment to keratin biomaterials
    • Richter JR, de Guzman RC, Van Dyke ME. Mechanisms of hepa-tocyte attachment to keratin biomaterials. Biomaterials 2011; 32(30): 7555-75561.
    • (2011) Biomaterials , vol.32 , Issue.30 , pp. 7555-75561
    • Richter, J.R.1    de Guzman, R.C.2    van Dyke, M.E.3
  • 184
    • 43149083069 scopus 로고    scopus 로고
    • Preparation of scaffolds from human hair proteins for tissue-engineering applications
    • Verma V, Verma P, Ray P, Ray AR. Preparation of scaffolds from human hair proteins for tissue-engineering applications. Biomed Mater 2008; 3(2): 025007.
    • (2008) Biomed Mater , vol.3 , Issue.2 , pp. 025007
    • Verma, V.1    Verma, P.2    Ray, P.3    Ray, A.R.4
  • 185
    • 79952769793 scopus 로고    scopus 로고
    • Preparation of keratino-cyte culture medium for the clinical applications of regenerative medicine
    • Takagi R, Yamato M, Murakami D, et al. Preparation of keratino-cyte culture medium for the clinical applications of regenerative medicine. J Tissue Eng Regen Med 2011; 5(4): e63-e73.
    • (2011) J Tissue Eng Regen Med , vol.5 , Issue.4
    • Takagi, R.1    Yamato, M.2    Murakami, D.3
  • 186
    • 34848904509 scopus 로고    scopus 로고
    • Hypertrophic scar formation following burns and trauma: New approaches to treatment
    • Aarabi S, Longaker MT, Gurtner GC. Hypertrophic scar formation following burns and trauma: New approaches to treatment. PLoS Med 2007; 4(9): e234.
    • (2007) PLoS Med , vol.4 , Issue.9
    • Aarabi, S.1    Longaker, M.T.2    Gurtner, G.C.3
  • 187
    • 55449114249 scopus 로고    scopus 로고
    • Prevention and management of hypertrophic scars and keloids after burns in children
    • Berman B, Viera MH, Amini S, Huo R, Jones IS. Prevention and management of hypertrophic scars and keloids after burns in children. J Craniofac Surg 2008; 19(4): 989-1006.
    • (2008) J Craniofac Surg , vol.19 , Issue.4 , pp. 989-1006
    • Berman, B.1    Viera, M.H.2    Amini, S.3    Huo, R.4    Jones, I.S.5
  • 188
    • 34249823651 scopus 로고    scopus 로고
    • Tissue engineering of replacement skin: The crossroads of biomaterials, wound healing, embryonic development, stem cells and regeneration
    • Metcalfe AD, Ferguson MW. Tissue engineering of replacement skin: The crossroads of biomaterials, wound healing, embryonic development, stem cells and regeneration. J R Soc Interface 2007; 4(14): 413-437.
    • (2007) J R Soc Interface , vol.4 , Issue.14 , pp. 413-437
    • Metcalfe, A.D.1    Ferguson, M.W.2
  • 189
    • 34547764903 scopus 로고    scopus 로고
    • Design and development of three-dimensional scaffolds for tissue engineering
    • Liu C, Xia Z, Czernuszka JT. Design and development of three-dimensional scaffolds for tissue engineering. Chem Eng Res Des 2007; 85(7): 1051-1064.
    • (2007) Chem Eng Res Des , vol.85 , Issue.7 , pp. 1051-1064
    • Liu, C.1    Xia, Z.2    Czernuszka, J.T.3
  • 190
    • 84862917924 scopus 로고    scopus 로고
    • Hair follicle regeneration in skin grafts: Current concepts and future perspectives
    • Mahjour SB, Ghaffarpasand F, Wang H. Hair follicle regeneration in skin grafts: Current concepts and future perspectives. Tissue Eng Part B Rev 2012; 18(1): 15-23.
    • (2012) Tissue Eng Part B Rev , vol.18 , Issue.1 , pp. 15-23
    • Mahjour, S.B.1    Ghaffarpasand, F.2    Wang, H.3
  • 191
    • 55949103864 scopus 로고    scopus 로고
    • Hair morphogenesis in vitro: Formation of hair structures suitable for implantation
    • Qiao J, Turetsky A, Kemp P, Teumer J. Hair morphogenesis in vitro: Formation of hair structures suitable for implantation. Regen Med 2008; 3(5): 683-692.
    • (2008) Regen Med , vol.3 , Issue.5 , pp. 683-692
    • Qiao, J.1    Turetsky, A.2    Kemp, P.3    Teumer, J.4
  • 192
    • 0026680528 scopus 로고
    • Cultured dermal papilla cells induce follicle formation and hair growth by transdifferentiation of an adult epidermis
    • Reynolds AJ, Jahoda CAB. Cultured dermal papilla cells induce follicle formation and hair growth by transdifferentiation of an adult epidermis. Development 1992; 115(2): 587-593.
    • (1992) Development , vol.115 , Issue.2 , pp. 587-593
    • Reynolds, A.J.1    Jahoda, C.A.B.2
  • 194
    • 35348929350 scopus 로고    scopus 로고
    • The use of keratin biomaterials derived from human hair for the promotion of rapid regeneration of peripheral nerves
    • Sierpinski P, Garrett J, Ma J, et al. The use of keratin biomaterials derived from human hair for the promotion of rapid regeneration of peripheral nerves. Biomaterials 2008; 29: 118-128.
    • (2008) Biomaterials , vol.29 , pp. 118-128
    • Sierpinski, P.1    Garrett, J.2    Ma, J.3
  • 195
    • 54849413370 scopus 로고    scopus 로고
    • Peripheral nerve regeneration using a keratin-based scaffold: Long-term functional and his-tological outcomes in a mouse model
    • Apel PJ, Garrett JP, Sierpinski P, et al. Peripheral nerve regeneration using a keratin-based scaffold: Long-term functional and his-tological outcomes in a mouse model. J Hand Surg Am 2008; 33: 1541-1547.
    • (2008) J Hand Surg Am , vol.33 , pp. 1541-1547
    • Apel, P.J.1    Garrett, J.P.2    Sierpinski, P.3
  • 196
    • 67650812796 scopus 로고    scopus 로고
    • A Keratin biomaterial gel hemostat derived from human hair: Evaluation in a rabbit model of lethal liver injury
    • Aboushwareb T, Eberli D, Ward C, et al. A Keratin biomaterial gel hemostat derived from human hair: Evaluation in a rabbit model of lethal liver injury. J Biomed Mater Res B 2009; 90: 45-54.
    • (2009) J Biomed Mater Res B , vol.90 , pp. 45-54
    • Aboushwareb, T.1    Eberli, D.2    Ward, C.3


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