메뉴 건너뛰기




Volumn 123, Issue 4, 2004, Pages 715-732

Stratum corneum keratin structure, function, and formation: The cubic rod-packing and membrane templating model

Author keywords

Blue phases; Body centered cubic cylinder packing; Corneocytes; Cryo electron microscopy; Cubic membranes; Cubic phases; Epidermis; Intermediate filaments; Skin lipids; Skin membranes; Sponge phases; Tonofilaments

Indexed keywords

KERATIN;

EID: 4444355074     PISSN: 0022202X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0022-202X.2004.23213.x     Document Type: Article
Times cited : (140)

References (87)
  • 1
    • 33746722209 scopus 로고
    • Body-centred cubic cylinder packing and the garnet structure
    • Andersson S, O'Keeffe M: Body-centred cubic cylinder packing and the garnet structure. Nature 267:605-606, 1977
    • (1977) Nature , vol.267 , pp. 605-606
    • Andersson, S.1    O'Keeffe, M.2
  • 2
    • 85012765723 scopus 로고
    • Limitations of metabolite concentrations and the conservation of solvent capacity in the living cell
    • Horecker BL, Stadtman ER (eds), New York: Academic Press
    • Atkinson DE: Limitations of metabolite concentrations and the conservation of solvent capacity in the living cell. In: Horecker BL, Stadtman ER (eds). Current Topics in Cellular Regulation, Vol. 1. New York: Academic Press, 1969; p 29-43
    • (1969) Current Topics in Cellular Regulation , vol.1 , pp. 29-43
    • Atkinson, D.E.1
  • 4
    • 0015477715 scopus 로고
    • Twisted fibrous arrangements in biological materials and cholesteric mesophases
    • Bouligand Y: Twisted fibrous arrangements in biological materials and cholesteric mesophases. Tissue Cell 4:189-217, 1972
    • (1972) Tissue Cell , vol.4 , pp. 189-217
    • Bouligand, Y.1
  • 5
    • 0026669010 scopus 로고
    • Structure of human stratum corneum as a function of temperature and hydration: A wide-angle x-ray diffraction study
    • Bouwstra JA, Gooris GS, Salmon-de Vries MA, Van der Spek JA, Bras W: Structure of human stratum corneum as a function of temperature and hydration: A wide-angle x-ray diffraction study. Int J Pharmaceut 84: 205-216, 1992
    • (1992) Int J Pharmaceut , vol.84 , pp. 205-216
    • Bouwstra, J.A.1    Gooris, G.S.2    Salmon-De Vries, M.A.3    Van Der Spek, J.A.4    Bras, W.5
  • 6
    • 0025955486 scopus 로고
    • Structural investigations of human stratum corneum by small-angle x-ray scattering
    • Bouwstra JA, Gooris GS, Van der Spek JA, Bras W: Structural investigations of human stratum corneum by small-angle x-ray scattering. J Invest Dermatol 97:1005-1012, 1991
    • (1991) J Invest Dermatol , vol.97 , pp. 1005-1012
    • Bouwstra, J.A.1    Gooris, G.S.2    Van Der Spek, J.A.3    Bras, W.4
  • 7
    • 0015536838 scopus 로고
    • Freeze fracture replication of cells of stratum corneum of human epidermis
    • Breathnach AS, Goodman T, Stolinski C, Gross M: Freeze fracture replication of cells of stratum corneum of human epidermis. J Anat 114:65-81, 1973
    • (1973) J Anat , vol.114 , pp. 65-81
    • Breathnach, A.S.1    Goodman, T.2    Stolinski, C.3    Gross, M.4
  • 8
    • 0021734135 scopus 로고
    • The structure of cytoplasm in directly frozen cultured cells. I. Filamentous meshworks and the cytoplasmic ground substance
    • Bridgman PC, Reese TS: The structure of cytoplasm in directly frozen cultured cells. I. Filamentous meshworks and the cytoplasmic ground substance. J Cell Biol 99:1655-1668, 1984
    • (1984) J Cell Biol , vol.99 , pp. 1655-1668
    • Bridgman, P.C.1    Reese, T.S.2
  • 9
    • 0012456026 scopus 로고
    • The keratinization of epidermal cells of normal guinea pig skin as revealed by electron microscopy
    • Brody I: The keratinization of epidermal cells of normal guinea pig skin as revealed by electron microscopy. J Ultrastruct Res 2:482-511, 1959
    • (1959) J Ultrastruct Res , vol.2 , pp. 482-511
    • Brody, I.1
  • 10
    • 0000411178 scopus 로고
    • The ultrastructure of the tonofibrils in the keratinization process of normal human epidermis
    • Brody I: The ultrastructure of the tonofibrils in the keratinization process of normal human epidermis. J Ultrastruct Res 4:264-297, 1960
    • (1960) J Ultrastruct Res , vol.4 , pp. 264-297
    • Brody, I.1
  • 11
    • 0035089901 scopus 로고    scopus 로고
    • In vivo confocal Raman microspectroscopy of the skin: Noninvasive determination of molecular concentration profiles
    • Gaspers PJ, Lucassen GW, Carter EA, Bruining HA, Puppels GJ: In vivo confocal Raman microspectroscopy of the skin: Noninvasive determination of molecular concentration profiles. J Invest Dermatol 116:434-442, 2001
    • (2001) J Invest Dermatol , vol.116 , pp. 434-442
    • Gaspers, P.J.1    Lucassen, G.W.2    Carter, E.A.3    Bruining, H.A.4    Puppels, G.J.5
  • 13
    • 0025341392 scopus 로고
    • Elucidating early stages of keratin filament assembly
    • Coulombe PA, Fuchs E: Elucidating early stages of keratin filament assembly. J Cell Biol 111:153-169, 1990
    • (1990) J Cell Biol , vol.111 , pp. 153-169
    • Coulombe, P.A.1    Fuchs, E.2
  • 14
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • Crick FHC: The packing of α-helices: Simple coiled-coils. Acta Crystallogr 6: 689-697, 1953
    • (1953) Acta Crystallogr , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 17
    • 0016608422 scopus 로고
    • The permeability barrier in mammalian epidermis
    • Elias PM, Friend DS: The permeability barrier in mammalian epidermis. J Cell Biol 65:180-191, 1975
    • (1975) J Cell Biol , vol.65 , pp. 180-191
    • Elias, P.M.1    Friend, D.S.2
  • 18
    • 0000963766 scopus 로고    scopus 로고
    • Non-topological saddle-splay and curvature instabilities from anisotropic membrane inclusions
    • Fournier JB: Non-topological saddle-splay and curvature instabilities from anisotropic membrane inclusions. Phys Rev Lett 76:4436-4439, 1996
    • (1996) Phys Rev Lett , vol.76 , pp. 4436-4439
    • Fournier, J.B.1
  • 19
    • 0022600845 scopus 로고
    • Genesis and regression of the figures of Eberth and occurrence of cytokeratin aggregates in the epidermis of anuran larvae
    • Fox H, Whitear M: Genesis and regression of the figures of Eberth and occurrence of cytokeratin aggregates in the epidermis of anuran larvae. Anat Embryol 174:73-82, 1986
    • (1986) Anat Embryol , vol.174 , pp. 73-82
    • Fox, H.1    Whitear, M.2
  • 20
    • 0020360150 scopus 로고
    • Intermediate filament proteins in nonfilamentous structures: Transient disintegration and inclusion of subunit proteins in granular aggregates
    • Franke WW, Schmid E, Grund C, Geiger B: Intermediate filament proteins in nonfilamentous structures: Transient disintegration and inclusion of subunit proteins in granular aggregates. Cell 30:103-113, 1982
    • (1982) Cell , vol.30 , pp. 103-113
    • Franke, W.W.1    Schmid, E.2    Grund, C.3    Geiger, B.4
  • 21
    • 0020776621 scopus 로고
    • The structure of the α-keratin microfibril
    • Fraser RDB, MacRae TP: The structure of the α-keratin microfibril. Biosci Rep 3:517-525, 1983
    • (1983) Biosci Rep , vol.3 , pp. 517-525
    • Fraser, R.D.B.1    MacRae, T.P.2
  • 23
    • 0031128277 scopus 로고    scopus 로고
    • The organization and animal-vegetal asymmetry of cytokeratin filaments in stage VI Xenopus oocytes is dependent upon f-actin and microtubules
    • Gard DL, Cha BJ, King E: The organization and animal-vegetal asymmetry of cytokeratin filaments in stage VI Xenopus oocytes is dependent upon f-actin and microtubules. Dev Biol 184:95-114, 1997
    • (1997) Dev Biol , vol.184 , pp. 95-114
    • Gard, D.L.1    Cha, B.J.2    King, E.3
  • 25
    • 0015811685 scopus 로고
    • Ultrastructures tegumentaires chez un crustace copepode Cletocampus retroressus
    • Gharagozlou-van Ginneken ID, Bouligand Y: Ultrastructures tegumentaires chez un crustace copepode Cletocampus retrogressus. Tissue Cell 5:413-439, 1973
    • (1973) Tissue Cell , vol.5 , pp. 413-439
    • Gharagozlou-Van Ginneken, I.D.1    Bouligand, Y.2
  • 26
    • 0026689736 scopus 로고
    • Association of glycosphingolipids with intermediate filaments of mesenchymal, epithelial, gllal, and muscle cells
    • Gillard BK, Thurmon LT, Marcus DM: Association of glycosphingolipids with intermediate filaments of mesenchymal, epithelial, gllal, and muscle cells. Cell Mot Cytoskel 21:255-271, 1992
    • (1992) Cell Mot Cytoskel , vol.21 , pp. 255-271
    • Gillard, B.K.1    Thurmon, L.T.2    Marcus, D.M.3
  • 27
    • 0032053588 scopus 로고    scopus 로고
    • Intermediate filament assembly: Fibrillogenesis is driven by decisive dimer-dimer interactions
    • Herrmann H, Aebi U: Intermediate filament assembly: Fibrillogenesis is driven by decisive dimer-dimer interactions. Curr Opin Struct Biol 8:177-185, 1998
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 177-185
    • Herrmann, H.1    Aebi, U.2
  • 28
    • 0033618848 scopus 로고    scopus 로고
    • Intermediate filament assembly: Temperature sensitivity and polymorphism
    • Herrmann H, Aebi U: Intermediate filament assembly: Temperature sensitivity and polymorphism. Cell Mol Life Sci 55:1416-1431, 1999
    • (1999) Cell Mol Life Sci , vol.55 , pp. 1416-1431
    • Herrmann, H.1    Aebi, U.2
  • 29
    • 0033960790 scopus 로고    scopus 로고
    • Intermediate filaments and their associates: Multitalented structural elements specifying cytoarchitecture and cytodynamics
    • Herrmann H, Aebi U: Intermediate filaments and their associates: Multitalented structural elements specifying cytoarchitecture and cytodynamics. Curr Opin Cell Biol 12:79-90, 2000
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 79-90
    • Herrmann, H.1    Aebi, U.2
  • 30
    • 0030596170 scopus 로고    scopus 로고
    • Structure and assembly properties of the intermediate filament protein vimentin: The role of its head, rod and tail domains
    • Herrmann H, Häner M, Brettel M, Müller SA, Goldie K, Fedtke B: Structure and assembly properties of the intermediate filament protein vimentin: The role of its head, rod and tail domains. J Mol Biol 264:933-953, 1996
    • (1996) J Mol Biol , vol.264 , pp. 933-953
    • Herrmann, H.1    Häner, M.2    Brettel, M.3    Müller, S.A.4    Goldie, K.5    Fedtke, B.6
  • 31
    • 0019308174 scopus 로고
    • Filament organization revealed in platinum replicas of freeze-dried cytoskeletons
    • Heuser JE, Kirschner MW: Filament organization revealed in platinum replicas of freeze-dried cytoskeletons. J Cell Biol 86:212-234, 1980
    • (1980) J Cell Biol , vol.86 , pp. 212-234
    • Heuser, J.E.1    Kirschner, M.W.2
  • 33
    • 0040914687 scopus 로고    scopus 로고
    • Lipid bilayer standing wave conformation in aqueous cubic phases
    • Jacob M, Larsson K, Andersson S: Lipid bilayer standing wave conformation in aqueous cubic phases. Z Kristallogr 212:5-8, 1997
    • (1997) Z Kristallogr , vol.212 , pp. 5-8
    • Jacob, M.1    Larsson, K.2    Andersson, S.3
  • 34
    • 0028849331 scopus 로고
    • On the real structure of the cytoplasmic matrix: Learning from embedment-free electron microscopy
    • Kondo H: On the real structure of the cytoplasmic matrix: Learning from embedment-free electron microscopy. Ach Histol Cytol 58:397-415, 1995
    • (1995) Ach Histol Cytol , vol.58 , pp. 397-415
    • Kondo, H.1
  • 37
    • 0030775098 scopus 로고    scopus 로고
    • On periodic curvature and standing wave motions in cell membranes
    • Larsson K: On periodic curvature and standing wave motions in cell membranes. J Chem Phys Lipids 88:15-20, 1997
    • (1997) J Chem Phys Lipids , vol.88 , pp. 15-20
    • Larsson, K.1
  • 38
    • 0024603546 scopus 로고
    • Cubic phases and isotropic structures formed by membrane lipids-possible biological relevance
    • Lindblom G, Rilfors L: Cubic phases and isotropic structures formed by membrane lipids-possible biological relevance. Biochim Biophys Acta 988:221-256, 1989
    • (1989) Biochim Biophys Acta , vol.988 , pp. 221-256
    • Lindblom, G.1    Rilfors, L.2
  • 39
    • 0344353245 scopus 로고    scopus 로고
    • Ludtke S: EMtool freeware, http://ncmi.bioch.bcm.tmc.edu/~stevel/emtool/ frame.html, 1996
    • (1996) EMtool Freeware
    • Ludtke, S.1
  • 40
    • 0032949408 scopus 로고    scopus 로고
    • Intermediate filaments in motion: Observation of intermediate filaments in cells using green fluorescent protein-vimentin
    • Martys JL, Ho C-L, Liem RKH, Gundersen GG: Intermediate filaments in motion: Observation of intermediate filaments in cells using green fluorescent protein-vimentin. Mol Biol Cell 10:1289-1295, 1999
    • (1999) Mol Biol Cell , vol.10 , pp. 1289-1295
    • Martys, J.L.1    Ho, C.-L.2    Liem, R.K.H.3    Gundersen, G.G.4
  • 42
    • 0014801236 scopus 로고
    • A large scale quasi-crystalline lamellar lattice in chloroplasts of the green alga Zygnema
    • McLean RJ, Pessoney GF: A large scale quasi-crystalline lamellar lattice in chloroplasts of the green alga Zygnema. J Cell Biol 45:522-531, 1970
    • (1970) J Cell Biol , vol.45 , pp. 522-531
    • McLean, R.J.1    Pessoney, G.F.2
  • 44
    • 0001694169 scopus 로고
    • The limits of economy of material in frame-structures
    • Michell AGM: The limits of economy of material in frame-structures. Phil Mag S6.8:589-597, 1904
    • (1904) Phil Mag , vol.S6.8 , pp. 589-597
    • Michell, A.G.M.1
  • 45
    • 0020383751 scopus 로고
    • Visualization of a 21-nm axial periodicity in shadowed keratin filaments and neurofilaments
    • Milam L, Erickson HP: Visualization of a 21-nm axial periodicity in shadowed keratin filaments and neurofilaments. J Cell Biol 94:592-596, 1982
    • (1982) J Cell Biol , vol.94 , pp. 592-596
    • Milam, L.1    Erickson, H.P.2
  • 46
    • 0027298853 scopus 로고
    • Dynamics of keratin assembly: Exogenous type I keratin rapidly associates with type II keratin In vivo
    • Miller RK, Khuon S, Goldman RD: Dynamics of keratin assembly: Exogenous type I keratin rapidly associates with type II keratin In vivo. J Cell Biol 122:123-135, 1993
    • (1993) J Cell Biol , vol.122 , pp. 123-135
    • Miller, R.K.1    Khuon, S.2    Goldman, R.D.3
  • 47
    • 0025915554 scopus 로고
    • Keratin incorporation into intermediate filament networks is a rapid process
    • Miller RK, Vikstrom K, Goldman RD: Keratin incorporation into intermediate filament networks is a rapid process. J Cell Biol 113:843-855, 1991
    • (1991) J Cell Biol , vol.113 , pp. 843-855
    • Miller, R.K.1    Vikstrom, K.2    Goldman, R.D.3
  • 48
    • 0002133971 scopus 로고
    • Theory and practice of high pressure freezing
    • Steinbrecht RA, Zierold K (eds). Berlin: Springer
    • Moor H: Theory and practice of high pressure freezing. In: Steinbrecht RA, Zierold K (eds). Cryo-Techniques in Biological Electron Microscopy. Berlin: Springer, 1987; p 175-179
    • (1987) Cryo-Techniques in Biological Electron Microscopy , pp. 175-179
    • Moor, H.1
  • 49
    • 0014078612 scopus 로고
    • Fine structure of protein-storing plastids in bean root tips
    • Newcomb EHJ: Fine structure of protein-storing plastids in bean root tips. J Cell Biol 33:143-163, 1967
    • (1967) J Cell Biol , vol.33 , pp. 143-163
    • Newcomb, E.H.J.1
  • 50
    • 0034783382 scopus 로고    scopus 로고
    • Skin barrier formation-the membrane folding model
    • Norlén LPO: Skin barrier formation-the membrane folding model. J Invest Dermatol 17:823-829, 2001a
    • (2001) J Invest Dermatol , vol.17 , pp. 823-829
    • Norlén, L.P.O.1
  • 51
    • 0034778702 scopus 로고    scopus 로고
    • Skin barrier structure and function-the single gel-phase model
    • Norlén LPO: Skin barrier structure and function-the single gel-phase model. J Invest Dermatol 17:830-836, 2001b
    • (2001) J Invest Dermatol , vol.17 , pp. 830-836
    • Norlén, L.P.O.1
  • 52
    • 0036091146 scopus 로고    scopus 로고
    • Does the single gel-phase exist in stratum corneum? Reply
    • Norlén LPO: Does the single gel-phase exist in stratum corneum? Reply. J Invest Dermatol 118:899-901, 2002
    • (2002) J Invest Dermatol , vol.118 , pp. 899-901
    • Norlén, L.P.O.1
  • 53
    • 0037377659 scopus 로고    scopus 로고
    • A cryo-transmission electron microscopy study of skin barrier formation
    • Norlén LPO, Al-Amoudi A, Dubochet J: A cryo-transmission electron microscopy study of skin barrier formation. J Invest Dermatol 120:555-560, 2003
    • (2003) J Invest Dermatol , vol.120 , pp. 555-560
    • Norlén, L.P.O.1    Al-Amoudi, A.2    Dubochet, J.3
  • 54
    • 0030863033 scopus 로고    scopus 로고
    • Stratum corneum swelling. Biophysical and computer assisted quantitative assessments
    • Norlén LPO, Emilson A, Forslind B: Stratum corneum swelling. Biophysical and computer assisted quantitative assessments. Arch Derm Res 289: 506-513, 1997
    • (1997) Arch Derm Res , vol.289 , pp. 506-513
    • Norlén, L.P.O.1    Emilson, A.2    Forslind, B.3
  • 56
    • 0032233993 scopus 로고    scopus 로고
    • Keratin modifications and solubility properties in epithelial cells and in vitro
    • Herrmann H, Harris JR (eds), Chapter 4 New York: Plenum Press
    • Omary MB, Ku N-O, Liao J, Price D: Keratin modifications and solubility properties in epithelial cells and in vitro. In: Herrmann H, Harris JR (eds). Intermediate Filaments-Subcellular Biochemistry, Vol. 31, Chapter 4 New York: Plenum Press, 1998; p 105-140
    • (1998) Intermediate Filaments-Subcellular Biochemistry , vol.31 , pp. 105-140
    • Omary, M.B.1    Ku, N.-O.2    Liao, J.3    Price, D.4
  • 57
    • 0028135714 scopus 로고
    • Assembly dynamics of epidermal keratins K1 and K10 in transfected cells
    • Paramio JM, Jorcano JL: Assembly dynamics of epidermal keratins K1 and K10 in transfected cells. Exp Cell Res 215:319-331, 1994
    • (1994) Exp Cell Res , vol.215 , pp. 319-331
    • Paramio, J.M.1    Jorcano, J.L.2
  • 58
    • 0035914358 scopus 로고    scopus 로고
    • Subfilamentous protofibril structures in fibrous proteins-cross-linking evidence for protofibrils in intermediate filaments
    • Parry DAD, Marekov LN, Steinert PM: Subfilamentous protofibril structures in fibrous proteins-cross-linking evidence for protofibrils in intermediate filaments. J Biol Chem 276:39253-39258, 2001
    • (2001) J Biol Chem , vol.276 , pp. 39253-39258
    • Parry, D.A.D.1    Marekov, L.N.2    Steinert, P.M.3
  • 59
    • 0033498452 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular architecture, assembly, dynamics and polymorphism
    • Parry DAD, Steinert PM: Intermediate filaments: Molecular architecture, assembly, dynamics and polymorphism. Quart Rev Biophys 32:99-187, 1999
    • (1999) Quart Rev Biophys , vol.32 , pp. 99-187
    • Parry, D.A.D.1    Steinert, P.M.2
  • 60
    • 0022540905 scopus 로고
    • Biogenesis of the crystalloid endoplasmic reticulum in UT-1 cells: Evidence that the newly formed endoplasmatic reticulum emerges from the nuclear envelope
    • Pathak RK, Luskey KL, Anderson RGW: Biogenesis of the crystalloid endoplasmic reticulum in UT-1 cells: Evidence that the newly formed endoplasmatic reticulum emerges from the nuclear envelope. J Cell Biol 102: 2158-2168, 1986
    • (1986) J Cell Biol , vol.102 , pp. 2158-2168
    • Pathak, R.K.1    Luskey, K.L.2    Anderson, R.G.W.3
  • 61
    • 0002732819 scopus 로고
    • Compound helical configurations of polypeptide chains: Structure of proteins of the α-keratin type
    • Pauling L, Corey RB: Compound helical configurations of polypeptide chains: Structure of proteins of the α-keratin type. Nature 171:59-61, 1953
    • (1953) Nature , vol.171 , pp. 59-61
    • Pauling, L.1    Corey, R.B.2
  • 62
    • 0022762881 scopus 로고
    • An electron microscopic study of the interaction in vitro of vimentin intermediate filaments with vesicles prepared from Ehrlich ascites tumor cells
    • Perides G, Scherbarth A, Kühn S, Traub P: An electron microscopic study of the interaction in vitro of vimentin intermediate filaments with vesicles prepared from Ehrlich ascites tumor cells. Eur J Cell Biol 41:313-325, 1986a
    • (1986) Eur J Cell Biol , vol.41 , pp. 313-325
    • Perides, G.1    Scherbarth, A.2    Kühn, S.3    Traub, P.4
  • 63
    • 0022900692 scopus 로고
    • Influence of phospholipids on the formation and stability of vimentin-type intermediate filaments
    • Perides G, Scherbarth A, Kühn S, Traub P: Influence of phospholipids on the formation and stability of vimentin-type intermediate filaments. Eur J Cell Biol 42:268-280, 1986b
    • (1986) Eur J Cell Biol , vol.42 , pp. 268-280
    • Perides, G.1    Scherbarth, A.2    Kühn, S.3    Traub, P.4
  • 64
    • 0034068163 scopus 로고    scopus 로고
    • High-pressure freezing provides new information on human epidermis: Simultaneous protein antigen and lamellar lipid structure preservation. Study on human epidermis by cryoimmobilization
    • Pfeitfer S, Vielhaber G, Vietzke J-R Wittern K-P, Hintze U, Wepf R: High-pressure freezing provides new information on human epidermis: Simultaneous protein antigen and lamellar lipid structure preservation. Study on human epidermis by cryoimmobilization. J Invest Dermatol 114:1030-1038, 2000
    • (2000) J Invest Dermatol , vol.114 , pp. 1030-1038
    • Pfeitfer, S.1    Vielhaber, G.2    Vietzke, J.-R.3    Wittern, K.-P.4    Hintze, U.5    Wepf, R.6
  • 66
    • 0018676724 scopus 로고
    • Structural transformation of epidermal tonofilaments upon cold treatment
    • Schliwa M, Euteneuer U: Structural transformation of epidermal tonofilaments upon cold treatment. Exp Cell Res 122:93-101, 1979
    • (1979) Exp Cell Res , vol.122 , pp. 93-101
    • Schliwa, M.1    Euteneuer, U.2
  • 67
    • 0342976584 scopus 로고
    • Frustration, curvature, and defect lines in metallic glasses and the cholesteric blue phase
    • Sethna JP: Frustration, curvature, and defect lines in metallic glasses and the cholesteric blue phase. Phys Rev B 31:6278-6297, 1985
    • (1985) Phys Rev B , vol.31 , pp. 6278-6297
    • Sethna, J.P.1
  • 68
    • 85012573362 scopus 로고
    • Concentrations of metabolites and binding sites. Implications in metabolic regulation
    • Horecker BL, Stadtman ER (eds), New York: Academic press
    • Sols A, Marco R: Concentrations of metabolites and binding sites. Implications in metabolic regulation. In: Horecker BL, Stadtman ER (eds). Current Topics In Cellular Regulation, Vol. 2. New York: Academic press, 1970; p 227-273
    • (1970) Current Topics in Cellular Regulation , vol.2 , pp. 227-273
    • Sols, A.1    Marco, R.2
  • 69
    • 0035909186 scopus 로고    scopus 로고
    • Novel process for producing cubic liquid crystalline nanoparticles (cubosomes)
    • Spicer PT, Hayden KL, Lynch ML, Ofori-Boateng A, Burns JL: Novel process for producing cubic liquid crystalline nanoparticles (cubosomes). Langmuir 17:5748-5756, 2001
    • (2001) Langmuir , vol.17 , pp. 5748-5756
    • Spicer, P.T.1    Hayden, K.L.2    Lynch, M.L.3    Ofori-Boateng, A.4    Burns, J.L.5
  • 70
    • 0025933468 scopus 로고
    • Analysis of the mechanism of assembly of mouse keratin 1/keratin 10 intermediate filaments in vitro suggests that intermediate filaments are built from multiple oligomeric units rather than a unique tetrameric building block
    • Steinert PM: Analysis of the mechanism of assembly of mouse keratin 1/keratin 10 intermediate filaments in vitro suggests that intermediate filaments are built from multiple oligomeric units rather than a unique tetrameric building block. J Struct Biol 107:175-188, 1991
    • (1991) J Struct Biol , vol.107 , pp. 175-188
    • Steinert, P.M.1
  • 71
    • 0006531513 scopus 로고
    • Computational straightening of images of curved macromolecular helices by cubic spline interpolation facilitates structural analysis by Fourier methods
    • Steven AC, Stall R, Steinert PM, Trus BL: Computational straightening of images of curved macromolecular helices by cubic spline interpolation facilitates structural analysis by Fourier methods. Proc 43rd Ann Meet EMSA 7: 738-739, 1985
    • (1985) Proc 43rd Ann Meet EMSA , vol.7 , pp. 738-739
    • Steven, A.C.1    Stall, R.2    Steinert, P.M.3    Trus, B.L.4
  • 72
    • 0003064736 scopus 로고
    • On the keratin fibrils of the skin. An X-ray small angle scattering study of the horny layer
    • Swanbeck G: On the keratin fibrils of the skin. An X-ray small angle scattering study of the horny layer. J Ultrastruct Res 3:51-57, 1959a
    • (1959) J Ultrastruct Res , vol.3 , pp. 51-57
    • Swanbeck, G.1
  • 73
    • 0343003938 scopus 로고
    • Macromolecular organisation of epidermal keratin
    • Swanbeck G: Macromolecular organisation of epidermal keratin. Acta Derm Venereol (Stockh) 39 (Suppl. 43):1-37, 1959b
    • (1959) Acta Derm Venereol (Stockh) , vol.39 , Issue.SUPPL. 43 , pp. 1-37
    • Swanbeck, G.1
  • 75
    • 0023284867 scopus 로고
    • Efficient interaction of nonpolar lipids with intermediate filaments of the vimentin type
    • Traub P, Perides G, Khün S, Scherbarth A: Efficient interaction of nonpolar lipids with intermediate filaments of the vimentin type. Eur J Cell Biol 43:55-64, 1987
    • (1987) Eur J Cell Biol , vol.43 , pp. 55-64
    • Traub, P.1    Perides, G.2    Khün, S.3    Scherbarth, A.4
  • 76
    • 0022397820 scopus 로고
    • Tenacious binding of lipids to vimentin during its isolation and purification from Ehrlich ascites tumor cells
    • Traub P, Pericles G, Scherbarth A, Traub U: Tenacious binding of lipids to vimentin during its isolation and purification from Ehrlich ascites tumor cells. FEBS Lett 193:217-222, 1985
    • (1985) FEBS Lett , vol.193 , pp. 217-222
    • Traub, P.1    Pericles, G.2    Scherbarth, A.3    Traub, U.4
  • 77
    • 0022981412 scopus 로고
    • Interaction in vitro of nonepithelial intermediate filament proteins with total cellular lipids, individual phospholipids, and a phospholipid mixture
    • Traub P, Perides G, Schimmel H, Scherbarth A: Interaction in vitro of nonepithelial intermediate filament proteins with total cellular lipids, individual phospholipids, and a phospholipid mixture. J Biol Chem 261:10558-10568, 1986
    • (1986) J Biol Chem , vol.261 , pp. 10558-10568
    • Traub, P.1    Perides, G.2    Schimmel, H.3    Scherbarth, A.4
  • 78
    • 0032249645 scopus 로고    scopus 로고
    • Transient electric birefringence in the study of intermediate filament assembly
    • Chapter 13 New York: Plenum Press
    • Herrmann H, Harris JR (eds). Van Amerongen H, Kooijman M, Bloemendal M: Transient electric birefringence in the study of intermediate filament assembly. In: Herrmann H, Harris JR (eds). Intermediate Filaments-Subcellular Biochemistry, Vol. 31, Chapter 13 New York: Plenum Press, 1998; p 399-421
    • (1998) Intermediate Filaments-Subcellular Biochemistry , vol.31 , pp. 399-421
    • Van Amerongen, H.1    Kooijman, M.2    Bloemendal, M.3
  • 80
    • 4644359589 scopus 로고
    • The curvature of chemical structures
    • Von Schnering HG, Nesper R: The curvature of chemical structures. Coll Phys 51 (Suppl. 23):C7383-C7396, 1990
    • (1990) Coll Phys , vol.51 , Issue.SUPPL. 23
    • Von Schnering, H.G.1    Nesper, R.2
  • 83
    • 0023863210 scopus 로고
    • Electron probe analysis of human skin: Determination of the water concentration profile
    • Warner RR, Myers MC, Taylor DA: Electron probe analysis of human skin: Determination of the water concentration profile. J Invest Dermatol 90: 218-224, 1988
    • (1988) J Invest Dermatol , vol.90 , pp. 218-224
    • Warner, R.R.1    Myers, M.C.2    Taylor, D.A.3
  • 84
    • 0037315465 scopus 로고    scopus 로고
    • Hydration disrupts human stratum corneum ultrastructure
    • Warner RR, Stone KJ, Boissy YL: Hydration disrupts human stratum corneum ultrastructure. J Invest Dermatol 120:275-284, 2003
    • (2003) J Invest Dermatol , vol.120 , pp. 275-284
    • Warner, R.R.1    Stone, K.J.2    Boissy, Y.L.3
  • 85
    • 0024290394 scopus 로고
    • Structure of lamellar lipid domains and corneocyte envelopes of murine stratum corneum. An x-ray diffraction study
    • White SH, Mirejovsky D, King GI: Structure of lamellar lipid domains and corneocyte envelopes of murine stratum corneum. An x-ray diffraction study. Biochemistry 27:3725-3732, 1988
    • (1988) Biochemistry , vol.27 , pp. 3725-3732
    • White, S.H.1    Mirejovsky, D.2    King, G.I.3
  • 86
    • 0015938086 scopus 로고
    • Structure-property relations of human and neonatal rat stratum corneum. I. Thermal stability of the crystalline lipid structure as studied by x-ray diffraction and differential thermal analysis
    • Wilkes GL, Nguyen A-L, Wildnauer R: Structure-property relations of human and neonatal rat stratum corneum. I. Thermal stability of the crystalline lipid structure as studied by x-ray diffraction and differential thermal analysis. Biochim Biophys Acta 304:267-275, 1973
    • (1973) Biochim Biophys Acta , vol.304 , pp. 267-275
    • Wilkes, G.L.1    Nguyen, A.-L.2    Wildnauer, R.3
  • 87
    • 0033375650 scopus 로고    scopus 로고
    • Detection of cytokeratin dynamics by time-lapse fluorescence microscopy in living cells
    • Windoffer R, Leube RE: Detection of cytokeratin dynamics by time-lapse fluorescence microscopy in living cells. J Cell Sci 112:4521-4534, 1999
    • (1999) J Cell Sci , vol.112 , pp. 4521-4534
    • Windoffer, R.1    Leube, R.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.