메뉴 건너뛰기




Volumn 70, Issue , 2005, Pages 143-202

Intermediate filament associated proteins

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ANKYRIN; CALPONIN; CHAPERONE; DESMOPLAKIN; ENVOPLAKIN; ENZYME; FILAGGRIN; HEAT SHOCK PROTEIN; INTERMEDIATE FILAMENT PROTEIN; ISOPROTEIN; LIPID; NEBULIN; PERIPLAKIN; PLAKOGLOBIN; PLECTIN; POLYCYSTIN 1; PROTEIN; RECEPTOR PROTEIN; SPECTRIN;

EID: 17444388553     PISSN: 00653233     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-3233(05)70006-1     Document Type: Article
Times cited : (84)

References (340)
  • 1
    • 3042832052 scopus 로고    scopus 로고
    • Periplakin gene targeting reveals a constituent of the cornified cell envelope dispensable for normal mouse development
    • Aho S., Li K., Ryoo Y., McGee C., Ishida-Yamamoto A., Uitto J., Klement J.F. Periplakin gene targeting reveals a constituent of the cornified cell envelope dispensable for normal mouse development. Mol. Cell. Biol. 24:2004;6410-6418
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6410-6418
    • Aho, S.1    Li, K.2    Ryoo, Y.3    McGee, C.4    Ishida-Yamamoto, A.5    Uitto, J.6    Klement, J.F.7
  • 2
    • 0037811950 scopus 로고    scopus 로고
    • A recessive mutation in desmoplakin causes arrhythmogenic right ventricular dysplasia, skin disorder, and woolly hair
    • Alcalai R., Metzger S., Rosenheck S., Meiner V., Chajek-Shaul T. A recessive mutation in desmoplakin causes arrhythmogenic right ventricular dysplasia, skin disorder, and woolly hair. J. Am. Coll. Cardiol. 42:2003;319-327
    • (2003) J. Am. Coll. Cardiol. , vol.42 , pp. 319-327
    • Alcalai, R.1    Metzger, S.2    Rosenheck, S.3    Meiner, V.4    Chajek-Shaul, T.5
  • 3
    • 0035110609 scopus 로고    scopus 로고
    • Anomalous apical plasma membrane phenotype in CK8-deficient mice indicates a novel role for intermediate filaments in the polarization of simple epithelia
    • Ameen N.A., Figueroa Y., Salas P.J. Anomalous apical plasma membrane phenotype in CK8-deficient mice indicates a novel role for intermediate filaments in the polarization of simple epithelia. J. Cell Sci. 114:2001a;563-575
    • (2001) J. Cell Sci. , vol.114 , pp. 563-575
    • Ameen, N.A.1    Figueroa, Y.2    Salas, P.J.3
  • 4
    • 0035110609 scopus 로고    scopus 로고
    • Anomalous apical plasma membrane phenotype in CK8-deficient mice indicates a novel role for intermediate filaments in the polarization of simple epithelia
    • Ameen N.A., Figueroa Y., Salas P.J. Anomalous apical plasma membrane phenotype in CK8-deficient mice indicates a novel role for intermediate filaments in the polarization of simple epithelia. J. Cell Sci. 114:2001b;563-575
    • (2001) J. Cell Sci. , vol.114 , pp. 563-575
    • Ameen, N.A.1    Figueroa, Y.2    Salas, P.J.3
  • 5
    • 0034010129 scopus 로고    scopus 로고
    • The p120 catenin family: Complex roles in adhesion, signaling and cancer
    • Anastasiadis P.Z., Reynolds A.B. The p120 catenin family: Complex roles in adhesion, signaling and cancer. J. Cell Sci. 113:2000;1319-1334
    • (2000) J. Cell Sci. , vol.113 , pp. 1319-1334
    • Anastasiadis, P.Z.1    Reynolds, A.B.2
  • 7
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • Andrä K., Lassmann H., Bittner R., Shorny S., Fässler R., Propst F., Wiche G. Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture. Genes Dev. 11:1997;3143-3156
    • (1997) Genes Dev. , vol.11 , pp. 3143-3156
    • Andrä, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fässler, R.5    Propst, F.6    Wiche, G.7
  • 8
    • 0032213892 scopus 로고    scopus 로고
    • Not just scaffolding: Plectin regulates actin dynamics in cultured cells
    • Andrä K., Nikolic B., Stöcher M., Drenckhahn D., Wiche G. Not just scaffolding: Plectin regulates actin dynamics in cultured cells. Genes Dev. 12:1998;3442-3451
    • (1998) Genes Dev. , vol.12 , pp. 3442-3451
    • Andrä, K.1    Nikolic, B.2    Stöcher, M.3    Drenckhahn, D.4    Wiche, G.5
  • 9
    • 0025165922 scopus 로고
    • Desmoplakin II expression is not restricted to stratified epithelia
    • Angst B.D., Nilles L.A., Green K.J. Desmoplakin II expression is not restricted to stratified epithelia. J. Cell Sci. 97:1990;247-257
    • (1990) J. Cell Sci. , vol.97 , pp. 247-257
    • Angst, B.D.1    Nilles, L.A.2    Green, K.J.3
  • 11
    • 0001089953 scopus 로고
    • Kinesin associated wth vimentin intermediate filaments contains a specific light chain
    • Avsiuk A., Minin A., Gyoeva F. Kinesin associated wth vimentin intermediate filaments contains a specific light chain. Doklady Biol. Sci. 345:1995;644-646
    • (1995) Doklady Biol. Sci. , vol.345 , pp. 644-646
    • Avsiuk, A.1    Minin, A.2    Gyoeva, F.3
  • 12
    • 18744397819 scopus 로고    scopus 로고
    • Molecular dissection of the interaction of desmin with the C-terminal region of nebulin
    • Bang M.L., Gregorio C., Labeit S. Molecular dissection of the interaction of desmin with the C-terminal region of nebulin. J. Struct. Biol. 137:2002;119-127
    • (2002) J. Struct. Biol. , vol.137 , pp. 119-127
    • Bang, M.L.1    Gregorio, C.2    Labeit, S.3
  • 13
    • 0035943673 scopus 로고    scopus 로고
    • Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres
    • Bellin R.M., Huiatt T.W., Critchley D.R., Robson R.M. Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres. J. Biol. Chem. 276:2001;32330-32337
    • (2001) J. Biol. Chem. , vol.276 , pp. 32330-32337
    • Bellin, R.M.1    Huiatt, T.W.2    Critchley, D.R.3    Robson, R.M.4
  • 14
    • 0032878518 scopus 로고    scopus 로고
    • Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with alpha-actinin may anchor synemin-containing heterofilaments
    • Bellin R.M., Sernett S.W., Becker B., Ip W., Huiatt T.W., Robson R.M. Molecular characteristics and interactions of the intermediate filament protein synemin. Interactions with alpha-actinin may anchor synemin-containing heterofilaments. J. Biol. Chem. 274:1999;29493-29499
    • (1999) J. Biol. Chem. , vol.274 , pp. 29493-29499
    • Bellin, R.M.1    Sernett, S.W.2    Becker, B.3    Ip, W.4    Huiatt, T.W.5    Robson, R.M.6
  • 15
    • 0023506775 scopus 로고
    • Association of intermediate filaments with vinculin-containing adhesion plaques of fibroblasts
    • Bershadsky A.D., Tint I.S., Svitkina T.M. Association of intermediate filaments with vinculin-containing adhesion plaques of fibroblasts. Cell Motil. Cytoskel. 8:1987;274-283
    • (1987) Cell Motil. Cytoskel. , vol.8 , pp. 274-283
    • Bershadsky, A.D.1    Tint, I.S.2    Svitkina, T.M.3
  • 16
    • 0036021111 scopus 로고    scopus 로고
    • Intermediate filaments and the function of the dystrophin-protein complex
    • Blake D.J., Martin-Rendon E. Intermediate filaments and the function of the dystrophin-protein complex. Trends Cardiovasc. Med. 12:2002;224-228
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 224-228
    • Blake, D.J.1    Martin-Rendon, E.2
  • 18
    • 0035076526 scopus 로고    scopus 로고
    • Plakophilin 1 interferes with plakoglobin binding to desmoplakin, yet together with plakoglobin promotes clustering of desmosomal plaque complexes at cell-cell borders
    • Bornslaeger E., Godsel L., Corcoran C., Park J., Hatzfeld M., Kowalczyk A., Green K. Plakophilin 1 interferes with plakoglobin binding to desmoplakin, yet together with plakoglobin promotes clustering of desmosomal plaque complexes at cell-cell borders. J. Cell Sci. 114:2001;727-738
    • (2001) J. Cell Sci. , vol.114 , pp. 727-738
    • Bornslaeger, E.1    Godsel, L.2    Corcoran, C.3    Park, J.4    Hatzfeld, M.5    Kowalczyk, A.6    Green, K.7
  • 19
    • 0029847068 scopus 로고    scopus 로고
    • Breaking the connection: Displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly
    • Bornslaeger E.B., Corcoran C.M., Stappenbeck T.S., Green K.J. Breaking the connection: Displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly. J. Biol. Chem. 134:1996;985-1002
    • (1996) J. Biol. Chem. , vol.134 , pp. 985-1002
    • Bornslaeger, E.B.1    Corcoran, C.M.2    Stappenbeck, T.S.3    Green, K.J.4
  • 20
    • 0032908323 scopus 로고    scopus 로고
    • Structure and function of hemidesmosomes: More than simple adhesion complexes
    • Borradori L., Sonnenberg A. Structure and function of hemidesmosomes: More than simple adhesion complexes. J. Invest. Derm. 112:1999;411-418
    • (1999) J. Invest. Derm. , vol.112 , pp. 411-418
    • Borradori, L.1    Sonnenberg, A.2
  • 21
    • 0037904987 scopus 로고    scopus 로고
    • The integrin-actin connection, an eternal love affair
    • Brakebusch C., Fassler R. The integrin-actin connection, an eternal love affair. Embo. J. 22:2003;2324-2333
    • (2003) Embo. J. , vol.22 , pp. 2324-2333
    • Brakebusch, C.1    Fassler, R.2
  • 22
    • 0343980401 scopus 로고
    • Fimbrin is a cytoskeletal protein that crosslinks F-actin in vitro
    • Bretscher A. Fimbrin is a cytoskeletal protein that crosslinks F-actin in vitro. Proc. Natl. Acad. Sci. USA. 78:1981;6849-6853
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6849-6853
    • Bretscher, A.1
  • 23
    • 19344376145 scopus 로고    scopus 로고
    • 14-3-3 Proteins: A number of functions for a numbered protein
    • Bridges D., Moorhead G.B. 14-3-3 proteins: A number of functions for a numbered protein. Sci. STKE. 2004:(242):2004;re10
    • (2004) Sci. STKE , vol.2004 , Issue.242 , pp. 10
    • Bridges, D.1    Moorhead, G.B.2
  • 24
    • 0029035706 scopus 로고
    • The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1
    • Brown A., Bernier G., Mathieu M., Rossant J., Kothary R. The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1. Nature Genet. 10:1995;301-306
    • (1995) Nature Genet. , vol.10 , pp. 301-306
    • Brown, A.1    Bernier, G.2    Mathieu, M.3    Rossant, J.4    Kothary, R.5
  • 25
    • 0035020420 scopus 로고    scopus 로고
    • Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis
    • Byun Y., Chen F., Chang R., Trivedi M., Green K.J., Cryns V.L. Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis. Cell Death Differ. 8:2001;443-450
    • (2001) Cell Death Differ. , vol.8 , pp. 443-450
    • Byun, Y.1    Chen, F.2    Chang, R.3    Trivedi, M.4    Green, K.J.5    Cryns, V.L.6
  • 27
    • 0034839862 scopus 로고    scopus 로고
    • Desmin-related myopathies in mice and man
    • Carlsson L., Thornell L.E. Desmin-related myopathies in mice and man. Acta Physiol. Scand. 171:2001;341-348
    • (2001) Acta Physiol. Scand. , vol.171 , pp. 341-348
    • Carlsson, L.1    Thornell, L.E.2
  • 28
    • 0025316130 scopus 로고
    • A protein antigenically related to nuclear lamin B mediates the association of intermediate filaments with desmosomes
    • Cartaud A., Ludosky M.A., Courvalin J.C., Cartaud J. A protein antigenically related to nuclear lamin B mediates the association of intermediate filaments with desmosomes. J. Biol. Chem. 111:1990;581-588
    • (1990) J. Biol. Chem. , vol.111 , pp. 581-588
    • Cartaud, A.1    Ludosky, M.A.2    Courvalin, J.C.3    Cartaud, J.4
  • 29
    • 0030770449 scopus 로고    scopus 로고
    • Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis
    • Caulin C., Salvesen G.S., Oshima R.G. Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis. J. Cell Biol. 138:1997;1379-1394
    • (1997) J. Cell Biol. , vol.138 , pp. 1379-1394
    • Caulin, C.1    Salvesen, G.S.2    Oshima, R.G.3
  • 30
    • 0034599872 scopus 로고    scopus 로고
    • Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis
    • Caulin C., Ware C.F., Magin T.M., Oshima R.G. Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis. J. Cell Biol. 149:2000;17-22
    • (2000) J. Cell Biol. , vol.149 , pp. 17-22
    • Caulin, C.1    Ware, C.F.2    Magin, T.M.3    Oshima, R.G.4
  • 31
    • 3543113113 scopus 로고    scopus 로고
    • Intermediate filaments mediate cytoskeletal crosstalk
    • Chang L., Goldman R. Intermediate filaments mediate cytoskeletal crosstalk. Nat. Rev. Mol. Cell. Biol. 5:2004;601-613
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 601-613
    • Chang, L.1    Goldman, R.2
  • 32
    • 0037470243 scopus 로고    scopus 로고
    • Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis
    • Chen F., Chang R., Trivedi M., Capetanaki Y., Cryns V.L. Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis. J. Biol. Chem. 278:2003;6848-6853
    • (2003) J. Biol. Chem. , vol.278 , pp. 6848-6853
    • Chen, F.1    Chang, R.2    Trivedi, M.3    Capetanaki, Y.4    Cryns, V.L.5
  • 33
    • 0037155877 scopus 로고    scopus 로고
    • Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and beta-catenin signaling
    • Chen X., Bonne S., Hatzfeld M., van Roy F., Green K.J. Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and beta-catenin signaling. J. Biol. Chem. 277:2002;10512-10522
    • (2002) J. Biol. Chem. , vol.277 , pp. 10512-10522
    • Chen, X.1    Bonne, S.2    Hatzfeld, M.3    Van Roy, F.4    Green, K.J.5
  • 34
    • 0036316492 scopus 로고    scopus 로고
    • Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure
    • Choi H.J., Park-Snyder S., Pascoe L.T., Green K.J., Weis W.I. Structures of two intermediate filament-binding fragments of desmoplakin reveal a unique repeat motif structure. Nat. Struct. Biol. 9:2002;612-620
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 612-620
    • Choi, H.J.1    Park-Snyder, S.2    Pascoe, L.T.3    Green, K.J.4    Weis, W.I.5
  • 36
    • 0017257712 scopus 로고
    • A filamentous cytoskeleton in vertebrate smooth muscle fibers
    • Cooke P. A filamentous cytoskeleton in vertebrate smooth muscle fibers. J. Biol. Chem. 68:1976;539-556
    • (1976) J. Biol. Chem. , vol.68 , pp. 539-556
    • Cooke, P.1
  • 37
    • 0033598182 scopus 로고    scopus 로고
    • Integrating the actin and vimentin cytoskeletons: Adhesion-dependent formation of fimbrin-vimentin complexes in macrophages
    • Correia I., Chu D., Chou Y.H., Goldman R.D., Matsudaira P. Integrating the actin and vimentin cytoskeletons: Adhesion-dependent formation of fimbrin-vimentin complexes in macrophages. J. Cell Biol. 146:1999;831-842
    • (1999) J. Cell Biol. , vol.146 , pp. 831-842
    • Correia, I.1    Chu, D.2    Chou, Y.H.3    Goldman, R.D.4    Matsudaira, P.5
  • 39
    • 0036468732 scopus 로고    scopus 로고
    • 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments
    • Coulombe P.A., Omary M.B. 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments. Curr. Opin. Cell Biol. 14:2002;110-122
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 110-122
    • Coulombe, P.A.1    Omary, M.B.2
  • 40
    • 4143134431 scopus 로고    scopus 로고
    • Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds
    • Coulombe P.A., Wong P. Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds. Nat. Cell Biol. 6:2004;699-706
    • (2004) Nat. Cell Biol. , vol.6 , pp. 699-706
    • Coulombe, P.A.1    Wong, P.2
  • 41
    • 0021009545 scopus 로고
    • Gamma actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites
    • Craig S.W., Pardo J.V. Gamma actin, spectrin, and intermediate filament proteins colocalize with vinculin at costameres, myofibril-to-sarcolemma attachment sites. Cell Motil. 3:1983;449-462
    • (1983) Cell Motil. , vol.3 , pp. 449-462
    • Craig, S.W.1    Pardo, J.V.2
  • 42
    • 0018162580 scopus 로고
    • Assembly of stratum corneum basic protein and keratin filaments in macrofibrils
    • Dale B.A., Holbrook K.A., Steinert P.M. Assembly of stratum corneum basic protein and keratin filaments in macrofibrils. Nature. 276:1978;729-731
    • (1978) Nature , vol.276 , pp. 729-731
    • Dale, B.A.1    Holbrook, K.A.2    Steinert, P.M.3
  • 44
    • 0002765026 scopus 로고
    • Phenotypic expression and processing of filaggrin in epidermal differentiation
    • M. Darmon, & M. Blumenberg. San Diego: Academic Press
    • Dale B.A., Presland R.B., Fleckman P., Kam E., Resing K.A. Phenotypic expression and processing of filaggrin in epidermal differentiation. Darmon M., Blumenberg M. "Molecular Biology of the Skin" 1993;79-106 Academic Press, San Diego
    • (1993) "molecular Biology of the Skin" , pp. 79-106
    • Dale, B.A.1    Presland, R.B.2    Fleckman, P.3    Kam, E.4    Resing, K.A.5
  • 45
    • 0031030244 scopus 로고    scopus 로고
    • Transient expression of epidermal filaggrin in cultured cells causes collapse of intermediate filament networks with alteration of cell shape and nuclear integrity
    • Dale B.A., Presland R.B., Lewis S.P., Underwood R.A., Fleckman P. Transient expression of epidermal filaggrin in cultured cells causes collapse of intermediate filament networks with alteration of cell shape and nuclear integrity. J. Invest. Dermatol. 108:1997;179-187
    • (1997) J. Invest. Dermatol. , vol.108 , pp. 179-187
    • Dale, B.A.1    Presland, R.B.2    Lewis, S.P.3    Underwood, R.A.4    Fleckman, P.5
  • 46
    • 0002247658 scopus 로고
    • Keratohyalin granule proteins
    • I.M. Leigh, E.B. Lane, & F.M. Watt. Cambridge UK: Cambridge University Press
    • Dale B.A., Resing K.A., Presland R.B. Keratohyalin granule proteins. Leigh I.M., Lane E.B., Watt F.M. "The Keratinocyte Handbook" 1994;323-350 Cambridge University Press, Cambridge UK
    • (1994) "the Keratinocyte Handbook" , pp. 323-350
    • Dale, B.A.1    Resing, K.A.2    Presland, R.B.3
  • 47
    • 0033564136 scopus 로고    scopus 로고
    • Dystonin-deficient mice exhibit an intrinsic muscle weakness and an instability of skeletal muscle cytoarchitecture
    • Dalpe G., Mathieu M., Comtois A., Zhu E., Wasiak S., De Repentigny Y., Leclerc N., Kothary R. Dystonin-deficient mice exhibit an intrinsic muscle weakness and an instability of skeletal muscle cytoarchitecture. Dev. Biol. 210:1999;367-380
    • (1999) Dev. Biol. , vol.210 , pp. 367-380
    • Dalpe, G.1    Mathieu, M.2    Comtois, A.3    Zhu, E.4    Wasiak, S.5    De Repentigny, Y.6    Leclerc, N.7    Kothary, R.8
  • 48
    • 0026739841 scopus 로고
    • Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes
    • Danowski B.A., Imanaka-Yoshida K., Sanger J.M., Sanger J.W. Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes. J. Biol. Chem. 118:1992;1411-1420
    • (1992) J. Biol. Chem. , vol.118 , pp. 1411-1420
    • Danowski, B.A.1    Imanaka-Yoshida, K.2    Sanger, J.M.3    Sanger, J.W.4
  • 49
    • 0034735518 scopus 로고    scopus 로고
    • Subcellular distribution of envoplakin and periplakin: Insights into their role as precursors of the epidermal cornified envelope
    • DiColandrea T., Karashima T., Maatta A., Watt F.M. Subcellular distribution of envoplakin and periplakin: Insights into their role as precursors of the epidermal cornified envelope. J. Cell Biol. 151:2000;573-586
    • (2000) J. Cell Biol. , vol.151 , pp. 573-586
    • Dicolandrea, T.1    Karashima, T.2    Maatta, A.3    Watt, F.M.4
  • 50
    • 1542289716 scopus 로고    scopus 로고
    • Intermediate filaments control the intracellular distribution of caspases during apoptosis
    • Dinsdale D., Lee J.C., Dewson G., Cohen G.M., Peter M.E. Intermediate filaments control the intracellular distribution of caspases during apoptosis. Am. J. Pathol. 164:2004;395-407
    • (2004) Am. J. Pathol. , vol.164 , pp. 395-407
    • Dinsdale, D.1    Lee, J.C.2    Dewson, G.3    Cohen, G.M.4    Peter, M.E.5
  • 51
    • 0030724879 scopus 로고    scopus 로고
    • AlphaB-crystallin interacts with intermediate filaments in response to stress
    • Djabali K., de Nechaud B., Landon F., Portier M.M. AlphaB-crystallin interacts with intermediate filaments in response to stress. J. Cell Sci. 110:1997;2759-2769
    • (1997) J. Cell Sci. , vol.110 , pp. 2759-2769
    • Djabali, K.1    De Nechaud, B.2    Landon, F.3    Portier, M.M.4
  • 52
    • 0033571984 scopus 로고    scopus 로고
    • AlphaB-crystallin interacts with cytoplasmic intermediate filament bundles during mitosis
    • Djabali K., Piron G., de Nechaud B., Portier M.M. alphaB-crystallin interacts with cytoplasmic intermediate filament bundles during mitosis. Exp. Cell Res. 253:1999;649-662
    • (1999) Exp. Cell Res. , vol.253 , pp. 649-662
    • Djabali, K.1    Piron, G.2    De Nechaud, B.3    Portier, M.M.4
  • 55
    • 0030906239 scopus 로고    scopus 로고
    • Polarisation-dependent association of plectin with desmoplakin and the lateral submembrane skeleton in MDCK cells
    • Eger A., Stockinger A., Wiche G., Foisner R. Polarisation-dependent association of plectin with desmoplakin and the lateral submembrane skeleton in MDCK cells. J. Cell Sci. 110:1997;1307-1316
    • (1997) J. Cell Sci. , vol.110 , pp. 1307-1316
    • Eger, A.1    Stockinger, A.2    Wiche, G.3    Foisner, R.4
  • 56
    • 0031570308 scopus 로고    scopus 로고
    • Plectin transcript diversity: Identification and tissue distribution of variants with distinct first coding exons and rodless isoforms
    • Elliott C.E., Becker B., Oehler S., Castanon M.J., Hauptmann R., Wiche G. Plectin transcript diversity: Identification and tissue distribution of variants with distinct first coding exons and rodless isoforms. Genomics. 42:1997;115-125
    • (1997) Genomics , vol.42 , pp. 115-125
    • Elliott, C.E.1    Becker, B.2    Oehler, S.3    Castanon, M.J.4    Hauptmann, R.5    Wiche, G.6
  • 57
    • 0038190993 scopus 로고    scopus 로고
    • Costameres: The Achilles' heel of Herculean muscle
    • Ervasti J.M. Costameres: The Achilles' heel of Herculean muscle. J. Biol. Chem. 278:2003;13591-13594
    • (2003) J. Biol. Chem. , vol.278 , pp. 13591-13594
    • Ervasti, J.M.1
  • 58
    • 0033790324 scopus 로고    scopus 로고
    • Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery
    • Faigle W., Colucci-Guyon E., Louvard D., Amigorena S., Galli T. Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery. Mol. Biol. Cell. 11:2000;3485-3494
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3485-3494
    • Faigle, W.1    Colucci-Guyon, E.2    Louvard, D.3    Amigorena, S.4    Galli, T.5
  • 59
    • 0025814581 scopus 로고
    • Characterization of keratocalmin, a calmodulin-binding protein from human epidermis
    • Fairley J.A., Scott G.A., Jensen K.D., Goldsmith L.A., Diaz L.A. Characterization of keratocalmin, a calmodulin-binding protein from human epidermis. J. Clin. Invest. 88:1991;315-322
    • (1991) J. Clin. Invest. , vol.88 , pp. 315-322
    • Fairley, J.A.1    Scott, G.A.2    Jensen, K.D.3    Goldsmith, L.A.4    Diaz, L.A.5
  • 60
    • 0029620499 scopus 로고
    • Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression
    • Foisner R., Bohn W., Mannweiler K., Wiche G. Distribution and ultrastructure of plectin arrays in subclones of rat glioma C6 cells differing in intermediate filament protein (vimentin) expression. J. Struct. Biol. 115:1995;304-317
    • (1995) J. Struct. Biol. , vol.115 , pp. 304-317
    • Foisner, R.1    Bohn, W.2    Mannweiler, K.3    Wiche, G.4
  • 61
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • Foisner R., Leichtfried F.E., Herrmann H., Small J.V., Lawson D., Wiche G. Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J. Biol. Chem. 106:1988;723-733
    • (1988) J. Biol. Chem. , vol.106 , pp. 723-733
    • Foisner, R.1    Leichtfried, F.E.2    Herrmann, H.3    Small, J.V.4    Lawson, D.5    Wiche, G.6
  • 62
    • 0025797361 scopus 로고
    • Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin
    • Foisner R., Traub P., Wiche G. Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. Proc. Natl. Acad. Sci. 88:1991;3812-3816
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 3812-3816
    • Foisner, R.1    Traub, P.2    Wiche, G.3
  • 63
    • 0023645941 scopus 로고
    • Structure and hydrodynamic properties of plectin molecules
    • Foisner R., Wiche G. Structure and hydrodynamic properties of plectin molecules. J. Mol. Biol. 198:1987;515-531
    • (1987) J. Mol. Biol. , vol.198 , pp. 515-531
    • Foisner, R.1    Wiche, G.2
  • 64
    • 0038247863 scopus 로고    scopus 로고
    • Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus
    • Fontao L., Favre B., Riou S., Geerts D., Jaunin F., Saurat J.H., Green K.J., Sonnenberg A., Borradori L. Interaction of the bullous pemphigoid antigen 1 (BP230) and desmoplakin with intermediate filaments is mediated by distinct sequences within their COOH terminus. Mol. Biol. Cell. 14:2003;1978-1992
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1978-1992
    • Fontao, L.1    Favre, B.2    Riou, S.3    Geerts, D.4    Jaunin, F.5    Saurat, J.H.6    Green, K.J.7    Sonnenberg, A.8    Borradori, L.9
  • 65
    • 0034953789 scopus 로고    scopus 로고
    • The interaction of plectin with actin: Evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin
    • Fontao L., Geerts D., Kuikman I., Koster J., Kramer D., Sonnenberg A. The interaction of plectin with actin: Evidence for cross-linking of actin filaments by dimerization of the actin-binding domain of plectin. J. Cell Sci. 114:2001;2065-2076
    • (2001) J. Cell Sci. , vol.114 , pp. 2065-2076
    • Fontao, L.1    Geerts, D.2    Kuikman, I.3    Koster, J.4    Kramer, D.5    Sonnenberg, A.6
  • 66
    • 0023649685 scopus 로고
    • Rearrangement of the vimentin cytoskeleton during adipose conversion: Formation of an intermediate filament cage around lipid globules
    • Franke W.W., Hergt M., Grund C. Rearrangement of the vimentin cytoskeleton during adipose conversion: Formation of an intermediate filament cage around lipid globules. Cell. 49:1987;131-141
    • (1987) Cell , vol.49 , pp. 131-141
    • Franke, W.W.1    Hergt, M.2    Grund, C.3
  • 67
    • 0026524937 scopus 로고
    • Actin and neurofilament binding domain of brain spectrin beta subunit
    • Frappier T., Derancourt J., Pradel L.-A. Actin and neurofilament binding domain of brain spectrin beta subunit. Eur. J. Biochem. 205:1992;85-91
    • (1992) Eur. J. Biochem. , vol.205 , pp. 85-91
    • Frappier, T.1    Derancourt, J.2    Pradel, L.-A.3
  • 68
    • 0025754337 scopus 로고
    • Interaction domains of neurofilament light chain and brain spectrin
    • Frappier T., Stetzkowski-Marden F., Pradel L.-A. Interaction domains of neurofilament light chain and brain spectrin. Biochem. J. 275:1991;521-527
    • (1991) Biochem. J. , vol.275 , pp. 521-527
    • Frappier, T.1    Stetzkowski-Marden, F.2    Pradel, L.-A.3
  • 69
    • 0033520387 scopus 로고    scopus 로고
    • Crossroads on cytoskeletal pathways
    • Fuchs E., Yang Y. Crossroads on cytoskeletal pathways. Cell. 98:1999;547-550
    • (1999) Cell , vol.98 , pp. 547-550
    • Fuchs, E.1    Yang, Y.2
  • 71
    • 0029976981 scopus 로고    scopus 로고
    • Identification of a 450-kDa human epidermal autoantigen as a new member of the plectin family
    • Fujiwara S., Kohno K., Iwamatsu A., Naito I., Shinkai H. Identification of a 450-kDa human epidermal autoantigen as a new member of the plectin family. J. Invest. Derm. 106:1996;1125-1130
    • (1996) J. Invest. Derm. , vol.106 , pp. 1125-1130
    • Fujiwara, S.1    Kohno, K.2    Iwamatsu, A.3    Naito, I.4    Shinkai, H.5
  • 72
    • 0035918303 scopus 로고    scopus 로고
    • Epiplakin, a novel member of the Plakin family originally identified as a 450-kDa human epidermal autoantigen. Structure and tissue localization
    • Fujiwara S., Takeo N., Otani Y., Parry D.A., Kunimatsu M., Lu R., Sasaki M., Matsuo N., Khaleduzzaman M., Yoshioka H. Epiplakin, a novel member of the Plakin family originally identified as a 450-kDa human epidermal autoantigen. Structure and tissue localization. J. Biol. Chem. 276:2001;13340-13347
    • (2001) J. Biol. Chem. , vol.276 , pp. 13340-13347
    • Fujiwara, S.1    Takeo, N.2    Otani, Y.3    Parry, D.A.4    Kunimatsu, M.5    Lu, R.6    Sasaki, M.7    Matsuo, N.8    Khaleduzzaman, M.9    Yoshioka, H.10
  • 74
    • 0035066688 scopus 로고    scopus 로고
    • Rescuing desmoplakin function in extra-embryonic ectoderm reveals the importance of this protein in embryonic heart, neuroepithelium, skin and vasculature
    • Gallicano G.I., Bauer C., Fuchs E. Rescuing desmoplakin function in extra-embryonic ectoderm reveals the importance of this protein in embryonic heart, neuroepithelium, skin and vasculature. Development. 128:2001;929-941
    • (2001) Development , vol.128 , pp. 929-941
    • Gallicano, G.I.1    Bauer, C.2    Fuchs, E.3
  • 76
    • 0025154931 scopus 로고
    • Organization, structure, and polymorphisms of the human profilaggrin gene
    • Gan S.Q., McBride O.W., Idler W.W., Markova N., Steinert P.M. Organization, structure, and polymorphisms of the human profilaggrin gene. Biochemistry. 29:1990;9432-9440
    • (1990) Biochemistry , vol.29 , pp. 9432-9440
    • Gan, S.Q.1    McBride, O.W.2    Idler, W.W.3    Markova, N.4    Steinert, P.M.5
  • 77
    • 0036020958 scopus 로고    scopus 로고
    • A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein
    • Gao Y.S., Vrielink A., MacKenzie R., Sztul E. A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein. Eur. J. Cell Biol. 81:2002;391-401
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 391-401
    • Gao, Y.S.1    Vrielink, A.2    MacKenzie, R.3    Sztul, E.4
  • 78
    • 0141631492 scopus 로고    scopus 로고
    • Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4
    • Garcia-Alvarez B., Bobkov A., Sonnenberg A., de Pereda J.M. Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4. Structure (Camb.). 11:2003;615-625
    • (2003) Structure (Camb.) , vol.11 , pp. 615-625
    • Garcia-Alvarez, B.1    Bobkov, A.2    Sonnenberg, A.3    De Pereda, J.M.4
  • 79
    • 0035816721 scopus 로고    scopus 로고
    • Tyrosine phosphorylated plakoglobin is associated with desmogleins but not desmoplakin after EGFR activation
    • Gaudry C.A., Palka H.L., Dusek R.L., Huen A.C., Khandekar M.J., Hudson L.G., Green K.J. Tyrosine phosphorylated plakoglobin is associated with desmogleins but not desmoplakin after EGFR activation. J. Biol. Chem. 276:2001;24871-24880
    • (2001) J. Biol. Chem. , vol.276 , pp. 24871-24880
    • Gaudry, C.A.1    Palka, H.L.2    Dusek, R.L.3    Huen, A.C.4    Khandekar, M.J.5    Hudson, L.G.6    Green, K.J.7
  • 80
    • 0032589487 scopus 로고    scopus 로고
    • Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding
    • Geerts D., Fontao L., Nievers M.G., Schaapveld R.Q., Purkis P.E., Wheeler G.N., Lane E.B., Leigh I.M., Sonnenberg A. Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. J. Cell Biol. 147:1999;417-434
    • (1999) J. Cell Biol. , vol.147 , pp. 417-434
    • Geerts, D.1    Fontao, L.2    Nievers, M.G.3    Schaapveld, R.Q.4    Purkis, P.E.5    Wheeler, G.N.6    Lane, E.B.7    Leigh, I.M.8    Sonnenberg, A.9
  • 81
    • 0023371437 scopus 로고
    • Lamin B constitutes an intermediate filament attachment site at the nuclear envelope
    • Georgatos S.D., Blobel G. Lamin B constitutes an intermediate filament attachment site at the nuclear envelope. J. Biol. Chem. 105:1987a;117-125
    • (1987) J. Biol. Chem. , vol.105 , pp. 117-125
    • Georgatos, S.D.1    Blobel, G.2
  • 82
    • 0023372471 scopus 로고
    • Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: A basis for a vectorial assembly of intermediate filaments
    • Georgatos S.D., Blobel G. Two distinct attachment sites for vimentin along the plasma membrane and the nuclear envelope in avian erythrocytes: A basis for a vectorial assembly of intermediate filaments. J. Biol. Chem. 105:1987b;105-115
    • (1987) J. Biol. Chem. , vol.105 , pp. 105-115
    • Georgatos, S.D.1    Blobel, G.2
  • 83
    • 85012338162 scopus 로고
    • The binding of vimentin to human erythrocyte membranes: A model system for the study of intermediate filament-membrane interactions
    • Georgatos S.D., Marchesi V.T. The binding of vimentin to human erythrocyte membranes: A model system for the study of intermediate filament-membrane interactions. J. Biol. Chem. 100:1985;1955-1961
    • (1985) J. Biol. Chem. , vol.100 , pp. 1955-1961
    • Georgatos, S.D.1    Marchesi, V.T.2
  • 84
    • 0021811570 scopus 로고
    • Site specificity in vimentin-membrane interactions: Intermediate filament subunits associate with the plasma membrane via their head domains
    • Georgatos S.D., Weaver D.C., Marchesi V.T. Site specificity in vimentin-membrane interactions: Intermediate filament subunits associate with the plasma membrane via their head domains. J. Biol. Chem. 100:1985;1962-1967
    • (1985) J. Biol. Chem. , vol.100 , pp. 1962-1967
    • Georgatos, S.D.1    Weaver, D.C.2    Marchesi, V.T.3
  • 85
    • 0023430563 scopus 로고
    • Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: Evidence for a conserved site-specificity in intermediate filament-membrane interactions
    • Georgatos S.D., Weber K., Geisler N., Blobel G. Binding of two desmin derivatives to the plasma membrane and the nuclear envelope of avian erythrocytes: Evidence for a conserved site-specificity in intermediate filament-membrane interactions. Proc. Natl. Acad. Sci. 84:1987;6780-6784
    • (1987) Proc. Natl. Acad. Sci. , vol.84 , pp. 6780-6784
    • Georgatos, S.D.1    Weber, K.2    Geisler, N.3    Blobel, G.4
  • 87
    • 0035921430 scopus 로고    scopus 로고
    • Simple epithelium keratins 8 and 18 provide resistance to Fas-mediated apoptosis. The protection occurs through a receptor-targeting modulation
    • Gilbert S., Loranger A., Daigle N., Marceau N. Simple epithelium keratins 8 and 18 provide resistance to Fas-mediated apoptosis. The protection occurs through a receptor-targeting modulation. J. Cell Biol. 154:2001;763-774
    • (2001) J. Cell Biol. , vol.154 , pp. 763-774
    • Gilbert, S.1    Loranger, A.2    Daigle, N.3    Marceau, N.4
  • 88
    • 3543009577 scopus 로고    scopus 로고
    • Keratins modulate c-Flip/extracellular signal-regulated kinase 1 and 2 antiapoptotic signaling in simple epithelial cells
    • Gilbert S., Loranger A., Marceau N. Keratins modulate c-Flip/extracellular signal-regulated kinase 1 and 2 antiapoptotic signaling in simple epithelial cells. Mol. Cell. Biol. 24:2004;7072-7081
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7072-7081
    • Gilbert, S.1    Loranger, A.2    Marceau, N.3
  • 90
    • 0019780969 scopus 로고
    • F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvillus core filaments
    • Glenney J.R. Jr., Kaulfus P., Matsudaira P., Weber K. F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvillus core filaments. J. Biol. Chem. 256:1981;9283-9288
    • (1981) J. Biol. Chem. , vol.256 , pp. 9283-9288
    • Glenney Jr., J.R.1    Kaulfus, P.2    Matsudaira, P.3    Weber, K.4
  • 93
    • 0034078008 scopus 로고    scopus 로고
    • Microtubule-based transport systems in neurons: The roles of kinesins and dyneins
    • Goldstein L.S., Yang Z. Microtubule-based transport systems in neurons: the roles of kinesins and dyneins. Annu. Rev. Neurosci. 23:2000;39-71
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 39-71
    • Goldstein, L.S.1    Yang, Z.2
  • 96
    • 0019195947 scopus 로고
    • Synemin: A new high molecular weight protein associated with desmin and vimentin filaments in muscle
    • Granger B.L., Lazarides E. Synemin: A new high molecular weight protein associated with desmin and vimentin filaments in muscle. Cell. 22:1980;727-738
    • (1980) Cell , vol.22 , pp. 727-738
    • Granger, B.L.1    Lazarides, E.2
  • 97
    • 0020411150 scopus 로고
    • Structural association of synemin and vimentin in avian erythrocytes revealed by immunoelectron microscopy
    • Granger B.L., Lazarides E. Structural association of synemin and vimentin in avian erythrocytes revealed by immunoelectron microscopy. Cell. 30:1982;263-275
    • (1982) Cell , vol.30 , pp. 263-275
    • Granger, B.L.1    Lazarides, E.2
  • 98
    • 0034832115 scopus 로고    scopus 로고
    • Cyclin-dependent protein kinase 5 (Cdk5) and the regulation of neurofilament metabolism
    • Grant P., Sharma P., Pant H.C. Cyclin-dependent protein kinase 5 (Cdk5) and the regulation of neurofilament metabolism. Eur. J. Biochem. 268:2001;1534-1546
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1534-1546
    • Grant, P.1    Sharma, P.2    Pant, H.C.3
  • 100
    • 0027096705 scopus 로고
    • Structure of desmoplakin and its association with intermediate filaments
    • Green K.J., Stappenbeck T.S., Parry D.A.D., Virata M.L.A. Structure of desmoplakin and its association with intermediate filaments. J. Dermatol. 19:1992a;765-769
    • (1992) J. Dermatol. , vol.19 , pp. 765-769
    • Green, K.J.1    Stappenbeck, T.S.2    Parry, D.A.D.3    Virata, M.L.A.4
  • 101
    • 0026755162 scopus 로고
    • Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: Members of a new gene family involved in organization of intermediate filaments
    • Green K.J., Virata M.L.A., Elgart G.W., Stanley J.R., Parry D.A.D. Comparative structural analysis of desmoplakin, bullous pemphigoid antigen and plectin: Members of a new gene family involved in organization of intermediate filaments. Int. J. Biol. Macromol. 14:1992b;145-153
    • (1992) Int. J. Biol. Macromol. , vol.14 , pp. 145-153
    • Green, K.J.1    Virata, M.L.A.2    Elgart, G.W.3    Stanley, J.R.4    Parry, D.A.D.5
  • 102
    • 4444230618 scopus 로고    scopus 로고
    • Kazrin, a novel periplakin-interacting protein associated with desmosomes and the keratinocyte plasma membrane
    • Groot K.R., Sevilla L.M., Nishi K., DiColandrea T., Watt F.M. Kazrin, a novel periplakin-interacting protein associated with desmosomes and the keratinocyte plasma membrane. J. Cell Biol. 166:2004;653-659
    • (2004) J. Cell Biol. , vol.166 , pp. 653-659
    • Groot, K.R.1    Sevilla, L.M.2    Nishi, K.3    Dicolandrea, T.4    Watt, F.M.5
  • 103
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • Guo L., Degenstein L., Dowling J., Yu Q.-C., Wollmann R., Perman B., Fuchs E. Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell. 81:1995;233-243
    • (1995) Cell , vol.81 , pp. 233-243
    • Guo, L.1    Degenstein, L.2    Dowling, J.3    Yu, Q.-C.4    Wollmann, R.5    Perman, B.6    Fuchs, E.7
  • 104
    • 0015228522 scopus 로고
    • Epsilon-(gamma-glutamyl)lysine cross-linkage in citrulline-containing protein fractions from hair
    • Harding H.W., Rogers G.E. Epsilon-(gamma-glutamyl)lysine cross-linkage in citrulline-containing protein fractions from hair. Biochemistry. 10:1971;624-630
    • (1971) Biochemistry , vol.10 , pp. 624-630
    • Harding, H.W.1    Rogers, G.E.2
  • 105
    • 0015514883 scopus 로고
    • Formation of the -(-glutamyl) lysine cross-link in hair proteins. Investigation of transamidases in hair follicles
    • Harding H.W., Rogers G.E. Formation of the -(-glutamyl) lysine cross-link in hair proteins. Investigation of transamidases in hair follicles. Biochemistry. 11:1972;2858-2863
    • (1972) Biochemistry , vol.11 , pp. 2858-2863
    • Harding, H.W.1    Rogers, G.E.2
  • 106
    • 0017258176 scopus 로고
    • Isolation of peptides containing citrulline and the cross-link, epsilon-(gamma-glutamyl)lysine, from hair medulla protein
    • Harding H.W., Rogers G.E. Isolation of peptides containing citrulline and the cross-link, epsilon-(gamma-glutamyl)lysine, from hair medulla protein. Biochim. Biophys. Acta. 427:1976;315-324
    • (1976) Biochim. Biophys. Acta , vol.427 , pp. 315-324
    • Harding, H.W.1    Rogers, G.E.2
  • 107
    • 0031754774 scopus 로고    scopus 로고
    • The armadillo family of structural proteins
    • Hatzfeld M. The armadillo family of structural proteins. Int. Rev. Cytol. 186:1999;179-224
    • (1999) Int. Rev. Cytol. , vol.186 , pp. 179-224
    • Hatzfeld, M.1
  • 108
    • 0037385290 scopus 로고    scopus 로고
    • Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains
    • Hatzfeld M., Green K.J., Sauter H. Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains. J. Cell Sci. 116:2003;1219-1233
    • (2003) J. Cell Sci. , vol.116 , pp. 1219-1233
    • Hatzfeld, M.1    Green, K.J.2    Sauter, H.3
  • 109
    • 0034599841 scopus 로고    scopus 로고
    • The function of plakophilin 1 in desmosome assembly and actin filament organization
    • Hatzfeld M., Haffner C., Schulze K., Vinzens U. The function of plakophilin 1 in desmosome assembly and actin filament organization. J. Cell Biol. 149:2000;209-222
    • (2000) J. Cell Biol. , vol.149 , pp. 209-222
    • Hatzfeld, M.1    Haffner, C.2    Schulze, K.3    Vinzens, U.4
  • 110
    • 0028144738 scopus 로고
    • Band 6 protein, a major constituent of desmosomes from stratified epithelia, is a novel member of the armadillo multigene family
    • Hatzfeld M., Kristjansson G.I., Plessmann U., Weber K. Band 6 protein, a major constituent of desmosomes from stratified epithelia, is a novel member of the armadillo multigene family. J. Cell Sci. 107:1994;2259-2270
    • (1994) J. Cell Sci. , vol.107 , pp. 2259-2270
    • Hatzfeld, M.1    Kristjansson, G.I.2    Plessmann, U.3    Weber, K.4
  • 111
    • 1642503683 scopus 로고    scopus 로고
    • Intermediate filaments are dynamic and motile elements of cellular architecture
    • Helfand B.T., Chang L., Goldman R.D. Intermediate filaments are dynamic and motile elements of cellular architecture. J. Cell Sci. 117:2004;133-141
    • (2004) J. Cell Sci. , vol.117 , pp. 133-141
    • Helfand, B.T.1    Chang, L.2    Goldman, R.D.3
  • 112
    • 0038010428 scopus 로고    scopus 로고
    • Rapid transport of neural intermediate filament protein
    • Helfand B.T., Loomis P., Yoon M., Goldman R.D. Rapid transport of neural intermediate filament protein. J. Cell Sci. 116:2003;2345-2359
    • (2003) J. Cell Sci. , vol.116 , pp. 2345-2359
    • Helfand, B.T.1    Loomis, P.2    Yoon, M.3    Goldman, R.D.4
  • 113
    • 0037182581 scopus 로고    scopus 로고
    • A requirement for cytoplasmic dynein and dynactin in intermediate filament network assembly and organization
    • Helfand B.T., Mikami A., Vallee R.B., Goldman R.D. A requirement for cytoplasmic dynein and dynactin in intermediate filament network assembly and organization. J. Cell Biol. 157:2002;795-806
    • (2002) J. Cell Biol. , vol.157 , pp. 795-806
    • Helfand, B.T.1    Mikami, A.2    Vallee, R.B.3    Goldman, R.D.4
  • 114
    • 0031453038 scopus 로고    scopus 로고
    • Molecular characteristics of the novel intermediate filament protein paranemin. Sequence reveals EAP-300 and IFAPa-400 are highly homologous to paranemin
    • Hemken P.M., Bellin R.M., Sernett S.W., Becker B., Huiatt T.W., Robson R.M. Molecular characteristics of the novel intermediate filament protein paranemin. Sequence reveals EAP-300 and IFAPa-400 are highly homologous to paranemin. J. Biol. Chem. 272:1997;32489-32499
    • (1997) J. Biol. Chem. , vol.272 , pp. 32489-32499
    • Hemken, P.M.1    Bellin, R.M.2    Sernett, S.W.3    Becker, B.4    Huiatt, T.W.5    Robson, R.M.6
  • 115
    • 0033960790 scopus 로고    scopus 로고
    • Intermediate filaments and their associates: Multi-talented structural elements specifying cytoarchitecture and cytodynamics
    • Herrmann H., Aebi U. Intermediate filaments and their associates: Multi-talented structural elements specifying cytoarchitecture and cytodynamics. Curr. Opin. Cell Biol. 12:2000;79-90
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 79-90
    • Herrmann, H.1    Aebi, U.2
  • 116
    • 0042329786 scopus 로고    scopus 로고
    • Intermediate filaments: Novel assembly models and exciting new functions for nuclear lamins
    • Herrmann H., Foisner R. Intermediate filaments: Novel assembly models and exciting new functions for nuclear lamins. Cell Mol. Life Sci. 60:2003;1607-1612
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 1607-1612
    • Herrmann, H.1    Foisner, R.2
  • 117
    • 0023126564 scopus 로고
    • Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240 kilodalton subunit of spectrin
    • Herrmann H., Wiche G. Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240 kilodalton subunit of spectrin. J. Biol. Chem. 262:1987;1320-1325
    • (1987) J. Biol. Chem. , vol.262 , pp. 1320-1325
    • Herrmann, H.1    Wiche, G.2
  • 118
    • 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 T.M., 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. 114:2001;2569-2575
    • (2001) J. Cell Sci. , vol.114 , pp. 2569-2575
    • Hesse, M.1    Magin, T.M.2    Weber, K.3
  • 119
    • 0032899830 scopus 로고    scopus 로고
    • Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers
    • Hijikata T., Murakami T., Imamura M., Fujimaki N., Ishikawa H. Plectin is a linker of intermediate filaments to Z-discs in skeletal muscle fibers. J. Cell Sci. 112:1999;867-876
    • (1999) J. Cell Sci. , vol.112 , pp. 867-876
    • Hijikata, T.1    Murakami, T.2    Imamura, M.3    Fujimaki, N.4    Ishikawa, H.5
  • 120
    • 0037295486 scopus 로고    scopus 로고
    • Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin
    • Hijikata T., Murakami T., Ishikawa H., Yorifuji H. Plectin tethers desmin intermediate filaments onto subsarcolemmal dense plaques containing dystrophin and vinculin. Histochem. Cell Biol. 119:2003;109-123
    • (2003) Histochem. Cell Biol. , vol.119 , pp. 109-123
    • Hijikata, T.1    Murakami, T.2    Ishikawa, H.3    Yorifuji, H.4
  • 121
    • 0033868312 scopus 로고    scopus 로고
    • Interaction of plakophilins with desmoplakin and intermediate filament proteins: An in vitro analysis
    • Hofmann I., Mertens C., Brettel M., Nimmrich V., Schnolzer N., Herrmann H. Interaction of plakophilins with desmoplakin and intermediate filament proteins: An in vitro analysis. J. Cell Sci. 113:2000;2471-2483
    • (2000) J. Cell Sci. , vol.113 , pp. 2471-2483
    • Hofmann, I.1    Mertens, C.2    Brettel, M.3    Nimmrich, V.4    Schnolzer, N.5    Herrmann, H.6
  • 122
  • 123
    • 0033973133 scopus 로고    scopus 로고
    • The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome
    • Hopkinson S.B., Jones J.C. The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome. Mol. Biol. Cell. 11:2000;277-286
    • (2000) Mol. Biol. Cell , vol.11 , pp. 277-286
    • Hopkinson, S.B.1    Jones, J.C.2
  • 124
    • 0033581916 scopus 로고    scopus 로고
    • Cytoskeletal linnkers: New MAPs for old destinations
    • Houseweart M.K., Cleveland D.W. Cytoskeletal linnkers: New MAPs for old destinations. Curr. Biol. 9:1999;R864-R866
    • (1999) Curr. Biol. , vol.9
    • Houseweart, M.K.1    Cleveland, D.W.2
  • 127
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: Bidirectional, allosteric signaling machines. Cell. 110:2002;673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 129
    • 0030738788 scopus 로고    scopus 로고
    • Distinctive expression of filaggrin and trichohyalin during various pathways of epithelial differentiation
    • Ishida-Yamamoto A., Hashimoto Y., Manabe M., O'Guin W.M., Dale B.A., Iizuka H. Distinctive expression of filaggrin and trichohyalin during various pathways of epithelial differentiation. Br. J. Dermatol. 137:1997;9-16
    • (1997) Br. J. Dermatol. , vol.137 , pp. 9-16
    • Ishida-Yamamoto, A.1    Hashimoto, Y.2    Manabe, M.3    O'Guin, W.M.4    Dale, B.A.5    Iizuka, H.6
  • 130
    • 0034602272 scopus 로고    scopus 로고
    • Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein
    • Izawa I., Nishizawa M., Ohtakara K., Ohtsuka K., Inada H., Inagaki M. Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory protein. J. Biol. Chem. 275:2000;34521-34527
    • (2000) J. Biol. Chem. , vol.275 , pp. 34521-34527
    • Izawa, I.1    Nishizawa, M.2    Ohtakara, K.3    Ohtsuka, K.4    Inada, H.5    Inagaki, M.6
  • 131
    • 3042822399 scopus 로고    scopus 로고
    • Plakins: Goliaths that link cell junctions and the cytoskeleton
    • Jefferson J.J., Leung C.L., Liem R.K. Plakins: Goliaths that link cell junctions and the cytoskeleton. Nat. Rev. Mol. Cell. Biol. 5:2004;542-553
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , pp. 542-553
    • Jefferson, J.J.1    Leung, C.L.2    Liem, R.K.3
  • 133
    • 0033050072 scopus 로고    scopus 로고
    • Hereditary skin diseases of hemidesmosomes
    • Jonkman M.F. Hereditary skin diseases of hemidesmosomes. J. Dermatol. Sci. 20:1999;103-121
    • (1999) J. Dermatol. Sci. , vol.20 , pp. 103-121
    • Jonkman, M.F.1
  • 134
    • 2542428252 scopus 로고    scopus 로고
    • Co-assembly of envoplakin and periplakin into oligomers and Ca(2+)-dependent vesicle binding: Implications for cornified cell envelope formation in stratified squamous epithelia
    • Kalinin A.E., Idler W.W., Marekov L.N., McPhie P., Bowers B., Steinert P.M., Steven A.C. Co-assembly of envoplakin and periplakin into oligomers and Ca(2+)-dependent vesicle binding: Implications for cornified cell envelope formation in stratified squamous epithelia. J. Biol. Chem. 279:2004;22773-22780
    • (2004) J. Biol. Chem. , vol.279 , pp. 22773-22780
    • Kalinin, A.E.1    Idler, W.W.2    Marekov, L.N.3    McPhie, P.4    Bowers, B.5    Steinert, P.M.6    Steven, A.C.7
  • 135
    • 0023917828 scopus 로고
    • Identification of a basic protein of Mr 75,000 as an accessory desmosomal plaque protein in stratified and complex epithelia
    • Kapprell H.-P., Owaribe K., Franke W.W. Identification of a basic protein of Mr 75,000 as an accessory desmosomal plaque protein in stratified and complex epithelia. J. Biol. Chem. 106:1988;1679-1691
    • (1988) J. Biol. Chem. , vol.106 , pp. 1679-1691
    • Kapprell, H.-P.1    Owaribe, K.2    Franke, W.W.3
  • 136
    • 0037115692 scopus 로고    scopus 로고
    • Interaction of periplakin and envoplakin with intermediate filaments
    • Karashima T., Watt F.M. Interaction of periplakin and envoplakin with intermediate filaments. J. Cell Sci. 115:2002;5027-5037
    • (2002) J. Cell Sci. , vol.115 , pp. 5027-5037
    • Karashima, T.1    Watt, F.M.2
  • 137
    • 0036781634 scopus 로고    scopus 로고
    • Unique role for the periplakin tail in intermediate filament association: Specific binding to keratin 8 and vimentin
    • Kazerounian S., Uitto J., Aho S. Unique role for the periplakin tail in intermediate filament association: Specific binding to keratin 8 and vimentin. Exp. Dermatol. 11:2002;428-438
    • (2002) Exp. Dermatol. , vol.11 , pp. 428-438
    • Kazerounian, S.1    Uitto, J.2    Aho, S.3
  • 142
    • 11944262997 scopus 로고    scopus 로고
    • Hemidesmosomes: Molecular organization and their importance for cell adhesion and disease
    • Starke K. Berlin: Springer-Verlag
    • Koster J., Borradori L., Sonnenberg A. Hemidesmosomes: Molecular organization and their importance for cell adhesion and disease. Starke K. "Handbook of Experimental Pharmacology" Vol. 165:2004a;243-280 Springer-Verlag, Berlin
    • (2004) "handbook of Experimental Pharmacology" , vol.165 , pp. 243-280
    • Koster, J.1    Borradori, L.2    Sonnenberg, A.3
  • 143
    • 0037439896 scopus 로고    scopus 로고
    • Analysis of the interactions between BP180, BP230, plectin, and the integrin alpha6beta4 important for hemidesmosome assembly
    • Koster J., Geerts D., Favre B., Borradori L., Sonnenberg A. Analysis of the interactions between BP180, BP230, plectin, and the integrin alpha6beta4 important for hemidesmosome assembly. J. Cell Sci. 116:2003;387-399
    • (2003) J. Cell Sci. , vol.116 , pp. 387-399
    • Koster, J.1    Geerts, D.2    Favre, B.3    Borradori, L.4    Sonnenberg, A.5
  • 144
    • 1542344031 scopus 로고    scopus 로고
    • Role of binding of plectin to the integrin beta4 subunit in the assembly of hemidesmosomes
    • Koster J., van Wilpe S., Kuikman I., Litjens S.H., Sonnenberg A. Role of binding of plectin to the integrin beta4 subunit in the assembly of hemidesmosomes. Mol. Biol. Cell. 15:2004b;1211-1223
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1211-1223
    • Koster, J.1    Van Wilpe, S.2    Kuikman, I.3    Litjens, S.H.4    Sonnenberg, A.5
  • 145
    • 0027987929 scopus 로고
    • Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins
    • Kouklis P.D., Hutton E., Fuchs E. Making a connection: Direct binding between keratin intermediate filaments and desmosomal proteins. J. Biol. Chem. 127:1994;1049-1060
    • (1994) J. Biol. Chem. , vol.127 , pp. 1049-1060
    • Kouklis, P.D.1    Hutton, E.2    Fuchs, E.3
  • 148
    • 0026008748 scopus 로고
    • Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: Correlation of thin filament length, nebulin size, and epitope profile
    • Kruger M., Wright J., Wang K. Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: Correlation of thin filament length, nebulin size, and epitope profile. J. Cell Biol. 115:1991;97-107
    • (1991) J. Cell Biol. , vol.115 , pp. 97-107
    • Kruger, M.1    Wright, J.2    Wang, K.3
  • 149
    • 0037192772 scopus 로고    scopus 로고
    • Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: Modulation by a keratin 1-like disease causing mutation
    • Ku N.O., Azhar S., Omary M.B. Keratin 8 phosphorylation by p38 kinase regulates cellular keratin filament reorganization: Modulation by a keratin 1-like disease causing mutation. J. Biol. Chem. 277:2002a;10775-10782
    • (2002) J. Biol. Chem. , vol.277 , pp. 10775-10782
    • Ku, N.O.1    Azhar, S.2    Omary, M.B.3
  • 151
    • 4143116817 scopus 로고    scopus 로고
    • Raf-1 activation disrupts its binding to keratins during cell stress
    • Ku N.O., Fu H., Omary M.B. Raf-1 activation disrupts its binding to keratins during cell stress. J. Cell Biol. 166:2004;479-485
    • (2004) J. Cell Biol. , vol.166 , pp. 479-485
    • Ku, N.O.1    Fu, H.2    Omary, M.B.3
  • 152
    • 0035942786 scopus 로고    scopus 로고
    • Keratin 8 mutations in patients with cryptogenic liver disease
    • Ku N.O., Gish R., Wright T.L., Omary M.B. Keratin 8 mutations in patients with cryptogenic liver disease. N. Engl. J. Med. 344:2001;1580-1587
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1580-1587
    • Ku, N.O.1    Gish, R.2    Wright, T.L.3    Omary, M.B.4
  • 153
    • 0032055050 scopus 로고    scopus 로고
    • Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins
    • Ku N.O., Liao J., Omary M.B. Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins. EMBO J. 17:1998;1892-1906
    • (1998) EMBO J. , vol.17 , pp. 1892-1906
    • Ku, N.O.1    Liao, J.2    Omary, M.B.3
  • 154
    • 0037007011 scopus 로고    scopus 로고
    • Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression
    • Ku N.O., Michie S., Resurreccion E.Z., Broome R.L., Omary M.B. Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression. Proc. Natl. Acad. Sci. USA. 99:2002b;4373-4378
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4373-4378
    • Ku, N.O.1    Michie, S.2    Resurreccion, E.Z.3    Broome, R.L.4    Omary, M.B.5
  • 156
    • 0037847551 scopus 로고    scopus 로고
    • Keratin mutation in transgenic mice predisposes to Fas but not TNF-induced apoptosis and massive liver injury
    • Ku N.O., Soetikno R.M., Omary M.B. Keratin mutation in transgenic mice predisposes to Fas but not TNF-induced apoptosis and massive liver injury. Hepatology. 37:2003b;1006-1014
    • (2003) Hepatology , vol.37 , pp. 1006-1014
    • Ku, N.O.1    Soetikno, R.M.2    Omary, M.B.3
  • 157
    • 0033002351 scopus 로고    scopus 로고
    • Profilaggrin requires both linker and filaggrin peptide sequences to form granules: Implications for profilaggrin processing in vivo
    • Kuechle M.K., Thulin C.D., Presland R.B., Dale B.A. Profilaggrin requires both linker and filaggrin peptide sequences to form granules: Implications for profilaggrin processing in vivo. J. Invest. Dermatol. 112:1999;843-852
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 843-852
    • Kuechle, M.K.1    Thulin, C.D.2    Presland, R.B.3    Dale, B.A.4
  • 158
    • 0032789411 scopus 로고    scopus 로고
    • Pmg-1 and pmg-2 constitute a novel family of KAP genes differentially expressed during skin and mammary gland development
    • Kuhn F., Lassing C., Range A., Mueller M., Hunziker T., Ziemiecki A., Andres A.C. Pmg-1 and pmg-2 constitute a novel family of KAP genes differentially expressed during skin and mammary gland development. Mech. Dev. 86:1999;193-196
    • (1999) Mech. Dev. , vol.86 , pp. 193-196
    • Kuhn, F.1    Lassing, C.2    Range, A.3    Mueller, M.4    Hunziker, T.5    Ziemiecki, A.6    Andres, A.C.7
  • 159
    • 0022596012 scopus 로고
    • Association of spectrin with desmin intermediate filaments
    • Langley R.C. Jr., Cohen C.M. Association of spectrin with desmin intermediate filaments. J. Cell Biochem. 30:1986;101-109
    • (1986) J. Cell Biochem. , vol.30 , pp. 101-109
    • Langley Jr., R.C.1    Cohen, C.M.2
  • 160
    • 0023497802 scopus 로고
    • Cell type-specific association between two types of spectrin and two types of intermediate filaments
    • Langley R.C. Jr., Cohen C.M. Cell type-specific association between two types of spectrin and two types of intermediate filaments. Cell Motil. Cytoskel. 8:1987;165-173
    • (1987) Cell Motil. Cytoskel. , vol.8 , pp. 165-173
    • Langley Jr., R.C.1    Cohen, C.M.2
  • 165
    • 0027195421 scopus 로고
    • The structure of human trichohyalin: Potential multiple roles as a functional EF-hand-like calcium-binding protein, a cornified cell envelope precursor, and an intermediate filament-associated (cross-linking) protein
    • Lee S.-C., Kim I.-G., Marekov L.N., O'Keefe E.J., Parry D.A.D., Steinert P.M. The structure of human trichohyalin: Potential multiple roles as a functional EF-hand-like calcium-binding protein, a cornified cell envelope precursor, and an intermediate filament-associated (cross-linking) protein. J. Biol. Chem. 268:1993;12164-12176
    • (1993) J. Biol. Chem. , vol.268 , pp. 12164-12176
    • Lee, S.-C.1    Kim, I.-G.2    Marekov, L.N.3    O'Keefe, E.J.4    Parry, D.A.D.5    Steinert, P.M.6
  • 166
    • 0036169110 scopus 로고    scopus 로고
    • Plakins: A family of versatile cytolinker proteins
    • Leung C.L., Green K.J., Liem R.K. Plakins: A family of versatile cytolinker proteins. Trends Cell Biol. 12:2002;37-45
    • (2002) Trends Cell Biol. , vol.12 , pp. 37-45
    • Leung, C.L.1    Green, K.J.2    Liem, R.K.3
  • 168
    • 0033535053 scopus 로고    scopus 로고
    • The intermediate filament protein peripherin is the specific interaction partner of mouse BPAG1-n (dystonin) in neurons
    • Leung C.L., Sun D., Liem R.K. The intermediate filament protein peripherin is the specific interaction partner of mouse BPAG1-n (dystonin) in neurons. J. Cell Biol. 144:1999;435-446
    • (1999) J. Cell Biol. , vol.144 , pp. 435-446
    • Leung, C.L.1    Sun, D.2    Liem, R.K.3
  • 169
    • 0035921424 scopus 로고    scopus 로고
    • The BPAG1 locus: Alternative splicing produces multiple isoforms with distinct cytoskeletal linker domains, including predominant isoforms in neurons and muscles
    • Leung C.L., Zheng M., Prater S.M., Liem R.K. The BPAG1 locus: Alternative splicing produces multiple isoforms with distinct cytoskeletal linker domains, including predominant isoforms in neurons and muscles. J. Cell Biol. 154:2001b;691-698
    • (2001) J. Cell Biol. , vol.154 , pp. 691-698
    • Leung, C.L.1    Zheng, M.2    Prater, S.M.3    Liem, R.K.4
  • 170
    • 0032540307 scopus 로고    scopus 로고
    • Kinesin is a candidate for cross-bridging microtubules and intermediate filaments. Selective binding of kinesin to detyrosinated tubulin and vimentin
    • Liao G., Gundersen G.G. Kinesin is a candidate for cross-bridging microtubules and intermediate filaments. Selective binding of kinesin to detyrosinated tubulin and vimentin. J. Biol. Chem. 273:1998;9797-9803
    • (1998) J. Biol. Chem. , vol.273 , pp. 9797-9803
    • Liao, G.1    Gundersen, G.G.2
  • 171
    • 0028931927 scopus 로고
    • The 70-kDa heat shock proteins associate with glandular intermediate filaments in an ATP-dependent manner
    • Liao J., Lowthert L.A., Ghori N., Omary M.B. The 70-kDa heat shock proteins associate with glandular intermediate filaments in an ATP-dependent manner. J. Biol. Chem. 270:1995;915-922
    • (1995) J. Biol. Chem. , vol.270 , pp. 915-922
    • Liao, J.1    Lowthert, L.A.2    Ghori, N.3    Omary, M.B.4
  • 172
    • 0029947282 scopus 로고    scopus 로고
    • 14-3-3 Proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor
    • Liao J., Omary M.B. 14-3-3 proteins associate with phosphorylated simple epithelial keratins during cell cycle progression and act as a solubility cofactor. J. Cell. Biol. 133:1996;345-357
    • (1996) J. Cell. Biol. , vol.133 , pp. 345-357
    • Liao, J.1    Omary, M.B.2
  • 173
    • 0030830633 scopus 로고    scopus 로고
    • Association of glucose-regulated protein (grp78) with human keratin 8
    • Liao J., Price D., Omary M.B. Association of glucose-regulated protein (grp78) with human keratin 8. FEBS Lett. 417:1997;316-320
    • (1997) FEBS Lett. , vol.417 , pp. 316-320
    • Liao, J.1    Price, D.2    Omary, M.B.3
  • 174
    • 0023369137 scopus 로고
    • An Epstein-Barr virus transforming protein associates with vimentin in lymphocytes
    • Liebowitz D., Kopan R., Fuchs E., Sample J., Kieff E. An Epstein-Barr virus transforming protein associates with vimentin in lymphocytes. Mol. Cell. Biol. 7:1987;2299-2308
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2299-2308
    • Liebowitz, D.1    Kopan, R.2    Fuchs, E.3    Sample, J.4    Kieff, E.5
  • 175
    • 0022245790 scopus 로고
    • Purification of the 300K intermediate filament-associated protein and its in vitro recombination with intermediate filaments
    • Lieska N., Yang H.-Y., Goldman R.D. Purification of the 300K intermediate filament-associated protein and its in vitro recombination with intermediate filaments. J. Biol. Chem. 101:1985;802-813
    • (1985) J. Biol. Chem. , vol.101 , pp. 802-813
    • Lieska, N.1    Yang, H.-Y.2    Goldman, R.D.3
  • 176
    • 0027511422 scopus 로고
    • Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells
    • Lin C.S., Park T., Chen Z.P., Leavitt J. Human plastin genes. Comparative gene structure, chromosome location, and differential expression in normal and neoplastic cells. J. Biol. Chem. 268:1993;2781-2792
    • (1993) J. Biol. Chem. , vol.268 , pp. 2781-2792
    • Lin, C.S.1    Park, T.2    Chen, Z.P.3    Leavitt, J.4
  • 177
    • 0028221820 scopus 로고
    • Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney
    • Lin C.S., Shen W., Chen Z.P., Tu Y.H., Matsudaira P. Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney. Mol. Cell. Biol. 14:1994;2457-2467
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2457-2467
    • Lin, C.S.1    Shen, W.2    Chen, Z.P.3    Tu, Y.H.4    Matsudaira, P.5
  • 178
    • 0029961661 scopus 로고    scopus 로고
    • Human plectin: Organization of the gene, sequence analysis, and chromosome localization (8q24)
    • Liu C.G., Maercker C., Castanon M.J., Hauptmann R., Wiche G. Human plectin: Organization of the gene, sequence analysis, and chromosome localization (8q24). Proc. Natl. Acad. Sci. 93:1996;4278-4283
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 4278-4283
    • Liu, C.G.1    Maercker, C.2    Castanon, M.J.3    Hauptmann, R.4    Wiche, G.5
  • 179
    • 0020478334 scopus 로고
    • Characterization of a phosphorylated form of the intermediate filament-aggregating protein filaggrin
    • Lonsdale-Eccles J.D., Teller D.C., Dale B.A. Characterization of a phosphorylated form of the intermediate filament-aggregating protein filaggrin. Biochemistry. 21:1982;5940-5948
    • (1982) Biochemistry , vol.21 , pp. 5940-5948
    • Lonsdale-Eccles, J.D.1    Teller, D.C.2    Dale, B.A.3
  • 180
    • 0034808105 scopus 로고    scopus 로고
    • Gene targeting of envoplakin, a cytoskeletal linker protein and precursor of the epidermal cornified envelope
    • Maatta A., DiColandrea T., Groot K., Watt F.M. Gene targeting of envoplakin, a cytoskeletal linker protein and precursor of the epidermal cornified envelope. Mol. Cell. Biol. 21:2001;7047-7053
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7047-7053
    • Maatta, A.1    Dicolandrea, T.2    Groot, K.3    Watt, F.M.4
  • 181
    • 0030923431 scopus 로고    scopus 로고
    • Association of calponin with desmin intermediate filaments
    • Mabuchi K., Li B., Ip W., Tao T. Association of calponin with desmin intermediate filaments. J. Biol. Chem. 272:1997;22662-22666
    • (1997) J. Biol. Chem. , vol.272 , pp. 22662-22666
    • Mabuchi, K.1    Li, B.2    Ip, W.3    Tao, T.4
  • 182
    • 0029982386 scopus 로고    scopus 로고
    • Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle
    • Mabuchi K., Li Y., Tao T., Wang C.L. Immunocytochemical localization of caldesmon and calponin in chicken gizzard smooth muscle. J. Muscle Res. Cell Motil. 17:1996;243-260
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 243-260
    • Mabuchi, K.1    Li, Y.2    Tao, T.3    Wang, C.L.4
  • 183
    • 0027254919 scopus 로고
    • The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis
    • Mack J.W., Steven A.C., Steinert P.M. The mechanism of interaction of filaggrin with intermediate filaments. The ionic zipper hypothesis. J. Mol. Biol. 232:1993;50-66
    • (1993) J. Mol. Biol. , vol.232 , pp. 50-66
    • MacK, J.W.1    Steven, A.C.2    Steinert, P.M.3
  • 184
    • 0031928124 scopus 로고    scopus 로고
    • The members of the plakin family of proteins recognized by paraneoplastic pemphigus antibodies include periplakin
    • Mahoney M.G., Aho S., Uitto J., Stanley J.R. The members of the plakin family of proteins recognized by paraneoplastic pemphigus antibodies include periplakin. J. Invest. Derm. 111:1998;308-313
    • (1998) J. Invest. Derm. , vol.111 , pp. 308-313
    • Mahoney, M.G.1    Aho, S.2    Uitto, J.3    Stanley, J.R.4
  • 185
    • 0028037537 scopus 로고
    • Existence of trichohyalin-keratohyalin hybrid granules: Co-localization of two major intermediate filament-associated proteins in non-follicular epithelia
    • Manabe M., O'Guin W.M. Existence of trichohyalin-keratohyalin hybrid granules: Co-localization of two major intermediate filament-associated proteins in non-follicular epithelia. Differentiation. 58:1994;65-75
    • (1994) Differentiation , vol.58 , pp. 65-75
    • Manabe, M.1    O'Guin, W.M.2
  • 186
    • 0025851310 scopus 로고
    • Interaction of filaggrin with keratin filaments during advanced stages of normal human epidermal differentiation and in ichthyosis vulgaris
    • Manabe M., Sanchez M., Sun T.T., Dale B.A. Interaction of filaggrin with keratin filaments during advanced stages of normal human epidermal differentiation and in ichthyosis vulgaris. Differentiation. 48:1991;43-50
    • (1991) Differentiation , vol.48 , pp. 43-50
    • Manabe, M.1    Sanchez, M.2    Sun, T.T.3    Dale, B.A.4
  • 187
    • 0021187624 scopus 로고
    • Immunoprecipitation of nonerythrocyte spectrin within live cells following microinjection of specific antibodies: Relation to cytoskeletal structures
    • Mangeat P.H., Burridge K. Immunoprecipitation of nonerythrocyte spectrin within live cells following microinjection of specific antibodies: Relation to cytoskeletal structures. J. Cell. Biol. 98:1984;1363-1377
    • (1984) J. Cell. Biol. , vol.98 , pp. 1363-1377
    • Mangeat, P.H.1    Burridge, K.2
  • 188
    • 85047681520 scopus 로고    scopus 로고
    • Keratin-mediated resistance to stress and apoptosis in simple epithelial cells in relation to health and disease
    • Marceau N., Loranger A., Gilbert S., Daigle N., Champetier S. Keratin-mediated resistance to stress and apoptosis in simple epithelial cells in relation to health and disease. Biochem. Cell Biol. 79:2001;543-555
    • (2001) Biochem. Cell Biol. , vol.79 , pp. 543-555
    • Marceau, N.1    Loranger, A.2    Gilbert, S.3    Daigle, N.4    Champetier, S.5
  • 189
    • 0032504164 scopus 로고    scopus 로고
    • Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope
    • Marekov L.N., Steinert P.M. Ceramides are bound to structural proteins of the human foreskin epidermal cornified cell envelope. J. Biol. Chem. 273:1998;17763-17770
    • (1998) J. Biol. Chem. , vol.273 , pp. 17763-17770
    • Marekov, L.N.1    Steinert, P.M.2
  • 192
    • 0035808418 scopus 로고    scopus 로고
    • The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments
    • McElhinny A.S., Kolmerer B., Fowler V.M., Labeit S., Gregorio C.C. The N-terminal end of nebulin interacts with tropomodulin at the pointed ends of the thin filaments. J. Biol. Chem. 276:2001;583-592
    • (2001) J. Biol. Chem. , vol.276 , pp. 583-592
    • McElhinny, A.S.1    Kolmerer, B.2    Fowler, V.M.3    Labeit, S.4    Gregorio, C.C.5
  • 194
    • 0034923678 scopus 로고    scopus 로고
    • Desmosomes: Structure and function in normal and diseased epidermis
    • McMillan J.R., Shimizu H. Desmosomes: Structure and function in normal and diseased epidermis. J. Dermatol. 28:2001;291-298
    • (2001) J. Dermatol. , vol.28 , pp. 291-298
    • McMillan, J.R.1    Shimizu, H.2
  • 195
    • 0030856050 scopus 로고    scopus 로고
    • Two hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type specific intermediate filaments
    • Meng J.-J., Bornslaeger E.A., Green K.J., Steinert P.M., Ip W. Two hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type specific intermediate filaments. J. Biol. Chem. 272:1997;21495-21503
    • (1997) J. Biol. Chem. , vol.272 , pp. 21495-21503
    • Meng, J.-J.1    Bornslaeger, E.A.2    Green, K.J.3    Steinert, P.M.4    Ip, W.5
  • 196
    • 0141529737 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of plakoglobin causes contrary effects on its association with desmosomes and adherens junction components and modulates beta-catenin-mediated transcription
    • Miravet S., Piedra J., Castano J., Raurell I., Franci C., Dunach M., Garcia de Herreros A. Tyrosine phosphorylation of plakoglobin causes contrary effects on its association with desmosomes and adherens junction components and modulates beta-catenin-mediated transcription. Mol. Cell. Biol. 23:2003;7391-7402
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7391-7402
    • Miravet, S.1    Piedra, J.2    Castano, J.3    Raurell, I.4    Franci, C.5    Dunach, M.6    Garcia De Herreros, A.7
  • 200
    • 0027521276 scopus 로고
    • 33-kDa peptides prepared from chicken gizzard smooth muscle bundle both actin and desmin filaments in vitro
    • Nakagawa H., Ishihara M., Ohashi K. 33-kDa peptides prepared from chicken gizzard smooth muscle bundle both actin and desmin filaments in vitro. J. Biochem. (Tokyo). 114:1993;623-626
    • (1993) J. Biochem. (Tokyo) , vol.114 , pp. 623-626
    • Nakagawa, H.1    Ishihara, M.2    Ohashi, K.3
  • 201
    • 0026468443 scopus 로고
    • Human T cell L-plastin bundles actin filaments in a calcium-dependent manner
    • Namba Y., Ito M., Zu Y., Shigesada K., Maruyama K. Human T cell L-plastin bundles actin filaments in a calcium-dependent manner. J. Biochem. (Tokyo). 112:1992;503-507
    • (1992) J. Biochem. (Tokyo) , vol.112 , pp. 503-507
    • Namba, Y.1    Ito, M.2    Zu, Y.3    Shigesada, K.4    Maruyama, K.5
  • 202
    • 85012419750 scopus 로고
    • Beta-Internexin, a ubiquitous intermediate filament-associated protein
    • Napolitano E.W., Pachter J.S., Chin S.S., Liem R.K. beta-Internexin, a ubiquitous intermediate filament-associated protein. J. Cell Biol. 101:1985;1323-1331
    • (1985) J. Cell Biol. , vol.101 , pp. 1323-1331
    • Napolitano, E.W.1    Pachter, J.S.2    Chin, S.S.3    Liem, R.K.4
  • 203
    • 1542347695 scopus 로고    scopus 로고
    • Convergence of Wnt, beta-catenin, and cadherin pathways
    • Nelson W.J., Nusse R. Convergence of Wnt, beta-catenin, and cadherin pathways. Science. 303:2004;1483-1487
    • (2004) Science , vol.303 , pp. 1483-1487
    • Nelson, W.J.1    Nusse, R.2
  • 204
    • 0035794230 scopus 로고    scopus 로고
    • Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle
    • Newey S.E., Howman E.V., Ponting C.P., Benson M.A., Nawrotzki R., Loh N.Y., Davies K.E., Blake D.J. Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle. J. Biol. Chem. 276:2001;6645-6655
    • (2001) J. Biol. Chem. , vol.276 , pp. 6645-6655
    • Newey, S.E.1    Howman, E.V.2    Ponting, C.P.3    Benson, M.A.4    Nawrotzki, R.5    Loh, N.Y.6    Davies, K.E.7    Blake, D.J.8
  • 206
    • 0028176579 scopus 로고
    • Chaperone activity of alpha-crystallins modulates intermediate filament assembly
    • Nicholl I.D., Quinlan R.A. Chaperone activity of alpha-crystallins modulates intermediate filament assembly. EMBO J. 13:1994;945-953
    • (1994) EMBO J. , vol.13 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 208
    • 10144233447 scopus 로고    scopus 로고
    • Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions
    • Nikolic B., MacNulty E., Mir B., Wiche G. Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions. J. Cell Biol. 134:1996;1455-1467
    • (1996) J. Cell Biol. , vol.134 , pp. 1455-1467
    • Nikolic, B.1    MacNulty, E.2    Mir, B.3    Wiche, G.4
  • 209
    • 0025371590 scopus 로고
    • Do thin filaments of smooth muscle contain calponin? a new method for the preparation
    • Nishida W., Abe M., Takahashi K., Hiwada K. Do thin filaments of smooth muscle contain calponin? A new method for the preparation. FEBS Lett. 268:1990;165-168
    • (1990) FEBS Lett. , vol.268 , pp. 165-168
    • Nishida, W.1    Abe, M.2    Takahashi, K.3    Hiwada, K.4
  • 212
    • 0028265170 scopus 로고
    • Calponin is localised in both the contractile apparatus and the cytoskeleton of smooth muscle cells
    • North A.J., Gimona M., Cross R.A., Small J.V. Calponin is localised in both the contractile apparatus and the cytoskeleton of smooth muscle cells. J. Cell Sci. 107:1994;437-444
    • (1994) J. Cell Sci. , vol.107 , pp. 437-444
    • North, A.J.1    Gimona, M.2    Cross, R.A.3    Small, J.V.4
  • 213
    • 0026503017 scopus 로고
    • Interaction of trichohyalin with intermediate filaments: Three immunologically defined stages of trichohyalin maturation
    • O'Guin W.M., Sun T.T., Manabe M. Interaction of trichohyalin with intermediate filaments: Three immunologically defined stages of trichohyalin maturation. J. Invest. Dermatol. 98:1992;24-32
    • (1992) J. Invest. Dermatol. , vol.98 , pp. 24-32
    • O'Guin, W.M.1    Sun, T.T.2    Manabe, M.3
  • 214
    • 0024371499 scopus 로고
    • Desmoplakin I and desmoplakin II: Purification and characterization
    • O'Keefe E.J., Erickson H.P., Bennett V. Desmoplakin I and desmoplakin II: Purification and characterization. J. Biol. Chem. 264:1989;8310-8318
    • (1989) J. Biol. Chem. , vol.264 , pp. 8310-8318
    • O'Keefe, E.J.1    Erickson, H.P.2    Bennett, V.3
  • 217
    • 0037155162 scopus 로고    scopus 로고
    • Novel alternative splicings of BPAG1 (bullous pemphigoid antigen 1) including the domain structure closely related to MACF (microtubule actin cross-linking factor)
    • Okumura M., Yamakawa H., Ohara O., Owaribe K. Novel alternative splicings of BPAG1 (bullous pemphigoid antigen 1) including the domain structure closely related to MACF (microtubule actin cross-linking factor). J. Biol. Chem. 277:2002;6682-6687
    • (2002) J. Biol. Chem. , vol.277 , pp. 6682-6687
    • Okumura, M.1    Yamakawa, H.2    Ohara, O.3    Owaribe, K.4
  • 218
    • 0034160011 scopus 로고    scopus 로고
    • Integrin signalling: A new Cas(t) of characters enters the stage
    • O'Neill G.M., Fashena S.J., Golemis E.A. Integrin signalling: A new Cas(t) of characters enters the stage. Trends Cell Biol. 10:2000;111-119
    • (2000) Trends Cell Biol. , vol.10 , pp. 111-119
    • O'Neill, G.M.1    Fashena, S.J.2    Golemis, E.A.3
  • 219
    • 0036097410 scopus 로고    scopus 로고
    • Apoptosis and keratin intermediate filaments
    • Oshima R.G. Apoptosis and keratin intermediate filaments. Cell Death Differ. 9:2002;486-492
    • (2002) Cell Death Differ. , vol.9 , pp. 486-492
    • Oshima, R.G.1
  • 220
    • 2442605590 scopus 로고    scopus 로고
    • Plectin-RACK1 (receptor for activated C kinase 1) scaffolding: A novel mechanism to regulate protein kinase C activity
    • Osmanagic-Myers S., Wiche G. Plectin-RACK1 (receptor for activated C kinase 1) scaffolding: A novel mechanism to regulate protein kinase C activity. J. Biol. Chem. 279:2004;18701-18710
    • (2004) J. Biol. Chem. , vol.279 , pp. 18701-18710
    • Osmanagic-Myers, S.1    Wiche, G.2
  • 221
    • 0029836931 scopus 로고    scopus 로고
    • Characterization of pinin, a novel protein associated with the desmosome-intermediate filament complex
    • Ouyang P., Sugrue S.P. Characterization of pinin, a novel protein associated with the desmosome-intermediate filament complex. J. Biol. Chem. 135:1996;1027-1042
    • (1996) J. Biol. Chem. , vol.135 , pp. 1027-1042
    • Ouyang, P.1    Sugrue, S.P.2
  • 222
    • 0030804192 scopus 로고    scopus 로고
    • Cloning and analysis of cDNA encoding murine pinin
    • Ouyang P., Zhen Y.Y., Sugrue S.P. Cloning and analysis of cDNA encoding murine pinin. Gene. 197:1997;115-120
    • (1997) Gene , vol.197 , pp. 115-120
    • Ouyang, P.1    Zhen, Y.Y.2    Sugrue, S.P.3
  • 224
    • 21544441484 scopus 로고    scopus 로고
    • Roles of plakoglobin end domains in desmosome assembly
    • Palka H.L., Green K.J. Roles of plakoglobin end domains in desmosome assembly. J. Cell Sci. 110:1997;2359-2371
    • (1997) J. Cell Sci. , vol.110 , pp. 2359-2371
    • Palka, H.L.1    Green, K.J.2
  • 226
    • 0034791125 scopus 로고    scopus 로고
    • Inhibition of protein kinase B (PKB) and PKCzeta mediates keratin K10-induced cell cycle arrest
    • Paramio J.M., Segrelles C., Ruiz S., Jorcano J.L. Inhibition of protein kinase B (PKB) and PKCzeta mediates keratin K10-induced cell cycle arrest. Mol. Cell. Biol. 21:2001;7449-7459
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7449-7459
    • Paramio, J.M.1    Segrelles, C.2    Ruiz, S.3    Jorcano, J.L.4
  • 227
    • 0010935732 scopus 로고
    • A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma
    • 1081-1012.
    • Pardo J.V., Siliciano J.D., Craig S.W. A vinculin-containing cortical lattice in skeletal muscle: Transverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma. Proc. Natl. Acad. Sci. 80:1983;. 1081-1012.
    • (1983) Proc. Natl. Acad. Sci. , vol.80
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 228
    • 0034998031 scopus 로고    scopus 로고
    • Proprotein convertase expression and localization in epidermis: Evidence for multiple roles and substrates
    • Pearton D.J., Nirunsuksiri W., Rehemtulla A., Lewis S.P., Presland R.B., Dale B.A. Proprotein convertase expression and localization in epidermis: Evidence for multiple roles and substrates. Exp. Dermatol. 10:2001;193-203
    • (2001) Exp. Dermatol. , vol.10 , pp. 193-203
    • Pearton, D.J.1    Nirunsuksiri, W.2    Rehemtulla, A.3    Lewis, S.P.4    Presland, R.B.5    Dale, B.A.6
  • 229
    • 0026661360 scopus 로고
    • The vertebrate adhesive junction proteins b-catenin and plakoglobin and the Drosophila segment polarity gene armadillo form a multigene family with similar properties
    • Peifer M., McCrea P.D., Green K.J., Wieschaus E., Gumbiner B.M. The vertebrate adhesive junction proteins b-catenin and plakoglobin and the Drosophila segment polarity gene armadillo form a multigene family with similar properties. J. Biol. Chem. 118:1992;681-691
    • (1992) J. Biol. Chem. , vol.118 , pp. 681-691
    • Peifer, M.1    McCrea, P.D.2    Green, K.J.3    Wieschaus, E.4    Gumbiner, B.M.5
  • 232
    • 0000843475 scopus 로고    scopus 로고
    • The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro
    • Perng M.D., Muchowski P.J., van Den I.P., Wu G.J., Hutcheson A.M., Clark J.I., Quinlan R.A. The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro. J. Biol. Chem. 274:1999b;33235-33243
    • (1999) J. Biol. Chem. , vol.274 , pp. 33235-33243
    • Perng, M.D.1    Muchowski, P.J.2    Van Den, I.P.3    Wu, G.J.4    Hutcheson, A.M.5    Clark, J.I.6    Quinlan, R.A.7
  • 233
    • 0036479311 scopus 로고    scopus 로고
    • Association of syncoilin and desmin: Linking intermediate filament proteins to the dystrophin-associated protein complex
    • Poon E., Howman E.V., Newey S.E., Davies K.E. Association of syncoilin and desmin: Linking intermediate filament proteins to the dystrophin-associated protein complex. J. Biol. Chem. 277:2002;3433-3439
    • (2002) J. Biol. Chem. , vol.277 , pp. 3433-3439
    • Poon, E.1    Howman, E.V.2    Newey, S.E.3    Davies, K.E.4
  • 234
    • 0030636267 scopus 로고    scopus 로고
    • The role of keratin proteins and their genes in the growth, structure and properties of hair
    • P. Jollès, H. Zahn, & H. Höcker. Boston: Basel; Birkhäuser Verlag
    • Powell B.C., Rogers G.E. The role of keratin proteins and their genes in the growth, structure and properties of hair. Jollès P., Zahn H., Höcker H. "Formation and structure of human hair" 1997;59-148 Basel; Birkhäuser Verlag, Boston
    • (1997) "formation and Structure of Human Hair" , pp. 59-148
    • Powell, B.C.1    Rogers, G.E.2
  • 235
    • 0034474025 scopus 로고    scopus 로고
    • Fast transport of neurofilament protein along microtubules in squid axoplasm
    • Prahlad V., Helfand B.T., Langford G.M., Vale R.D., Goldman R.D. Fast transport of neurofilament protein along microtubules in squid axoplasm. J. Cell Sci. 113:2000;3939-3946
    • (2000) J. Cell Sci. , vol.113 , pp. 3939-3946
    • Prahlad, V.1    Helfand, B.T.2    Langford, G.M.3    Vale, R.D.4    Goldman, R.D.5
  • 236
    • 0028896390 scopus 로고
    • Characterization of two distinct calcium-binding sites in the amino-terminus of human profilaggrin
    • Presland R.B., Bassuk J.A., Kimball J.R., Dale B.A. Characterization of two distinct calcium-binding sites in the amino-terminus of human profilaggrin. J. Invest. Dermatol. 104:1995;218-223
    • (1995) J. Invest. Dermatol. , vol.104 , pp. 218-223
    • Presland, R.B.1    Bassuk, J.A.2    Kimball, J.R.3    Dale, B.A.4
  • 237
    • 0034533621 scopus 로고    scopus 로고
    • Epithelial structural proteins of the skin and oral cavity: Function in health and disease
    • Presland R.B., Dale B.A. Epithelial structural proteins of the skin and oral cavity: Function in health and disease. Crit. Rev. Oral Biol. Med. 11:2000;383-408
    • (2000) Crit. Rev. Oral Biol. Med. , vol.11 , pp. 383-408
    • Presland, R.B.1    Dale, B.A.2
  • 238
    • 0027058170 scopus 로고
    • Characterization of the human epidermal profilaggrin gene. Genomic organization and identification of an S-100-like calcium binding domain at the amino terminus
    • Presland R.B., Haydock P.V., Fleckman P., Nirunsuksiri W., Dale B.A. Characterization of the human epidermal profilaggrin gene. Genomic organization and identification of an S-100-like calcium binding domain at the amino terminus. J. Biol. Chem. 267:1992;23772-23781
    • (1992) J. Biol. Chem. , vol.267 , pp. 23772-23781
    • Presland, R.B.1    Haydock, P.V.2    Fleckman, P.3    Nirunsuksiri, W.4    Dale, B.A.5
  • 239
    • 0035499865 scopus 로고    scopus 로고
    • Regulated expression of human filaggrin in keratinocytes results in cytoskeletal disruption, loss of cell-cell adhesion, and cell cycle arrest
    • Presland R.B., Kuechle M.K., Lewis S.P., Fleckman P., Dale B.A. Regulated expression of human filaggrin in keratinocytes results in cytoskeletal disruption, loss of cell-cell adhesion, and cell cycle arrest. Exp. Cell Res. 270:2001;199-213
    • (2001) Exp. Cell Res. , vol.270 , pp. 199-213
    • Presland, R.B.1    Kuechle, M.K.2    Lewis, S.P.3    Fleckman, P.4    Dale, B.A.5
  • 240
    • 0018474781 scopus 로고
    • Intermediate filaments connect Z-discs in adult chicken muscle
    • Price M., Sanger J.W. Intermediate filaments connect Z-discs in adult chicken muscle. J. Exp. Zool. 208:1979;263-269
    • (1979) J. Exp. Zool. , vol.208 , pp. 263-269
    • Price, M.1    Sanger, J.W.2
  • 241
    • 0029798270 scopus 로고    scopus 로고
    • Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy
    • Pulkkinen L., Smith F.J.D., Shimizu H., Murata S., Yaoita H., Hachisuka H., Nishikawa T., McLean W.H.I., Uitto J. Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy. Hum. Molec. Gent. 5:1996;1539-1546
    • (1996) Hum. Molec. Gent. , vol.5 , pp. 1539-1546
    • Pulkkinen, L.1    Smith, F.J.D.2    Shimizu, H.3    Murata, S.4    Yaoita, H.5    Hachisuka, H.6    Nishikawa, T.7    McLean, W.H.I.8    Uitto, J.9
  • 242
    • 0019051839 scopus 로고
    • High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments
    • Pytela R., Wiche G. High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments. Proc. Natl. Acad. Sci. USA. 77:1980;4808-4812
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4808-4812
    • Pytela, R.1    Wiche, G.2
  • 243
    • 0031941135 scopus 로고    scopus 로고
    • Association of neurofilament proteins with neuronal Cdk5 activator
    • Qi Z., Tang D., Zhu X., Fujita D.J., Wang J.H. Association of neurofilament proteins with neuronal Cdk5 activator. J. Biol. Chem. 273:1998;2329-2335
    • (1998) J. Biol. Chem. , vol.273 , pp. 2329-2335
    • Qi, Z.1    Tang, D.2    Zhu, X.3    Fujita, D.J.4    Wang, J.H.5
  • 246
  • 247
    • 0028818854 scopus 로고
    • Characterization of profilaggrin endoproteinase 1. A regulated cytoplasmic endoproteinase of epidermis
    • Resing K.A., Thulin C., Whiting K., al-Alawi N., Mostad S. Characterization of profilaggrin endoproteinase 1. A regulated cytoplasmic endoproteinase of epidermis. J. Biol. Chem. 270:1995;28193-28198
    • (1995) J. Biol. Chem. , vol.270 , pp. 28193-28198
    • Resing, K.A.1    Thulin, C.2    Whiting, K.3    Al-Alawi, N.4    Mostad, S.5
  • 248
    • 0344668724 scopus 로고    scopus 로고
    • Plectin 5′-transcript diversity: Short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms
    • Rezniczek G.A., Abrahamsberg C., Fuchs P., Spazierer D., Wiche G. Plectin 5′-transcript diversity: Short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms. Hum. Mol. Genet. 12:2003;3181-3194
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3181-3194
    • Rezniczek, G.A.1    Abrahamsberg, C.2    Fuchs, P.3    Spazierer, D.4    Wiche, G.5
  • 249
    • 0032489678 scopus 로고    scopus 로고
    • Linking integrin α6β4-based cell adhesion to the intermediate filament cytoskeleton: Direct interaction between the β4 subunit and plectin at multiple molecular sites
    • Rezniczek G.A., Pereda J.M.d., Reipert S., Wiche G. Linking integrin α6β4-based cell adhesion to the intermediate filament cytoskeleton: Direct interaction between the β4 subunit and plectin at multiple molecular sites. J. Biol. Chem. 141:1998;209-225
    • (1998) J. Biol. Chem. , vol.141 , pp. 209-225
    • Rezniczek, G.A.1    D. M., P.J.2    Reipert, S.3    Wiche, G.4
  • 250
    • 0027323058 scopus 로고
    • Organization and expression of hair follicle genes
    • Rogers G.E., Powell B.C. Organization and expression of hair follicle genes. J. Invest. Dermatol. 101:1993;50S-55S
    • (1993) J. Invest. Dermatol. , vol.101
    • Rogers, G.E.1    Powell, B.C.2
  • 251
    • 1642575258 scopus 로고    scopus 로고
    • Hair keratin associated proteins: Characterization of a second high sulfur KAP gene domain on human chromosome 21
    • Rogers M.A., Langbein L., Winter H., Beckmann I., Praetzel S., Schweizer J. Hair keratin associated proteins: Characterization of a second high sulfur KAP gene domain on human chromosome 21. J. Invest. Dermatol. 122:2004;147-158
    • (2004) J. Invest. Dermatol. , vol.122 , pp. 147-158
    • Rogers, M.A.1    Langbein, L.2    Winter, H.3    Beckmann, I.4    Praetzel, S.5    Schweizer, J.6
  • 252
    • 2242419081 scopus 로고    scopus 로고
    • Characterization of a first domain of human high glycine-tyrosine and high sulfur keratin-associated protein (KAP) genes on chromosome 21q22.1
    • Rogers M.A., Langbein L., Winter H., Ehmann C., Praetzel S., Schweizer J. Characterization of a first domain of human high glycine-tyrosine and high sulfur keratin-associated protein (KAP) genes on chromosome 21q22.1. J. Biol. Chem. 277:2002;48993-49002
    • (2002) J. Biol. Chem. , vol.277 , pp. 48993-49002
    • Rogers, M.A.1    Langbein, L.2    Winter, H.3    Ehmann, C.4    Praetzel, S.5    Schweizer, J.6
  • 254
    • 0141641125 scopus 로고    scopus 로고
    • Maintaining epithelial integrity: A function for gigantic spectraplakin isoforms in adherens junctions
    • Roper K., Brown N.H. Maintaining epithelial integrity: A function for gigantic spectraplakin isoforms in adherens junctions. J. Cell Biol. 162:2003;1305-1315
    • (2003) J. Cell Biol. , vol.162 , pp. 1305-1315
    • Roper, K.1    Brown, N.H.2
  • 255
    • 0037112997 scopus 로고    scopus 로고
    • The 'spectraplakins': Cytoskeletal giants with characteristics of both spectrin and plakin families
    • Roper K., Gregory S.L., Brown N.H. The 'spectraplakins': Cytoskeletal giants with characteristics of both spectrin and plakin families. J. Cell Sci. 115:2002;4215-4225
    • (2002) J. Cell Sci. , vol.115 , pp. 4215-4225
    • Roper, K.1    Gregory, S.L.2    Brown, N.H.3
  • 256
    • 0022549612 scopus 로고
    • Trichohyalin, an intermediate filament-associated protein of the hair follicle
    • Rothnagel J.A., Rogers G.E. Trichohyalin, an intermediate filament-associated protein of the hair follicle. J. Cell Biol. 102:1986;1419-1429
    • (1986) J. Cell Biol. , vol.102 , pp. 1419-1429
    • Rothnagel, J.A.1    Rogers, G.E.2
  • 257
    • 0031417774 scopus 로고    scopus 로고
    • Periplakin, a novel component of cornified envelopes and desmosomes that belongs to the plakin family and forms complexes with envoplakin
    • Ruhrberg C., Hajibagheri M.A.N., Parry D.A.D., Watt F.M. Periplakin, a novel component of cornified envelopes and desmosomes that belongs to the plakin family and forms complexes with envoplakin. J. Biol. Chem. 139:1997;1835-1849
    • (1997) J. Biol. Chem. , vol.139 , pp. 1835-1849
    • Ruhrberg, C.1    Hajibagheri, M.A.N.2    Parry, D.A.D.3    Watt, F.M.4
  • 258
    • 0029741672 scopus 로고    scopus 로고
    • Envoplakin, a novel precursor of the cornified envelope that has homology to desmoplakin
    • Ruhrberg C., Hajibagheri M.A.N., Simon M., Dooley T.P., Watt F.M. Envoplakin, a novel precursor of the cornified envelope that has homology to desmoplakin. J. Biol. Chem. 134:1996;715-729
    • (1996) J. Biol. Chem. , vol.134 , pp. 715-729
    • Ruhrberg, C.1    Hajibagheri, M.A.N.2    Simon, M.3    Dooley, T.P.4    Watt, F.M.5
  • 259
    • 0030795164 scopus 로고    scopus 로고
    • The plakin family: Versatile organisers of cytoskeletal architecture
    • Ruhrberg C., Watt F.M. The plakin family: Versatile organisers of cytoskeletal architecture. Curr. Opin. Genet. Devel. 7:1997;392-397
    • (1997) Curr. Opin. Genet. Devel. , vol.7 , pp. 392-397
    • Ruhrberg, C.1    Watt, F.M.2
  • 261
    • 0037630407 scopus 로고    scopus 로고
    • Impaired NF-kappa B activation and increased production of tumor necrosis factor alpha in transgenic mice expressing keratin K10 in the basal layer of the epidermis
    • Santos M., Perez P., Segrelles C., Ruiz S., Jorcano J.L., Paramio J.M. Impaired NF-kappa B activation and increased production of tumor necrosis factor alpha in transgenic mice expressing keratin K10 in the basal layer of the epidermis. J. Biol. Chem. 278:2003;13422-13430
    • (2003) J. Biol. Chem. , vol.278 , pp. 13422-13430
    • Santos, M.1    Perez, P.2    Segrelles, C.3    Ruiz, S.4    Jorcano, J.L.5    Paramio, J.M.6
  • 262
    • 0026744762 scopus 로고
    • A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells
    • Sarria A.J., Panini S.R., Evans R.M. A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells. J. Biol. Chem. 267:1992;19455-19463
    • (1992) J. Biol. Chem. , vol.267 , pp. 19455-19463
    • Sarria, A.J.1    Panini, S.R.2    Evans, R.M.3
  • 263
    • 0026052915 scopus 로고
    • Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains
    • Sawamura D., Li K., Chu M.-L., Uitto J. Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains. J. Biol. Chem. 266:1991;17784-17790
    • (1991) J. Biol. Chem. , vol.266 , pp. 17784-17790
    • Sawamura, D.1    Li, K.2    Chu, M.-L.3    Uitto, J.4
  • 264
    • 0025604399 scopus 로고
    • Bullous pemphigoid antigen (BPAG1): CDNA cloning and mapping of the gene to the short arm of human chromosome 6
    • Sawamura D., Nomura K., Sugita Y., Mattei M.G., Chu M.L., Knowlton R., Uitto J. Bullous pemphigoid antigen (BPAG1): cDNA cloning and mapping of the gene to the short arm of human chromosome 6. Genomics. 8:1990;722-726
    • (1990) Genomics , vol.8 , pp. 722-726
    • Sawamura, D.1    Nomura, K.2    Sugita, Y.3    Mattei, M.G.4    Chu, M.L.5    Knowlton, R.6    Uitto, J.7
  • 266
    • 0027491462 scopus 로고
    • Complexus adhaerentes, a new group of desmoplakin-containing junctions in endothelial cells: The syndesmos connecting retrothelial cells of lymph nodes
    • Schmelz M., Franke W.W. Complexus adhaerentes, a new group of desmoplakin-containing junctions in endothelial cells: The syndesmos connecting retrothelial cells of lymph nodes. Eur. J. Cell Biol. 61:1993;274-289
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 274-289
    • Schmelz, M.1    Franke, W.W.2
  • 267
    • 0342424740 scopus 로고    scopus 로고
    • Association of plectin with Z-discs is a prerequisite for the formation of the intermyofibrillar desmin cytoskeleton
    • Schröder R., Furst D.O., Klasen C., Reimann J., Herrmann H., van der Ven P.F. Association of plectin with Z-discs is a prerequisite for the formation of the intermyofibrillar desmin cytoskeleton. Lab. Invest. 80:2000;455-464
    • (2000) Lab. Invest. , vol.80 , pp. 455-464
    • Schröder, R.1    Furst, D.O.2    Klasen, C.3    Reimann, J.4    Herrmann, H.5    Van Der Ven, P.F.6
  • 269
    • 0035055799 scopus 로고    scopus 로고
    • Protein 4.1 in forebrain postsynaptic density preparations: Enrichment of 4.1 gene products and detection of 4.1R binding proteins
    • Scott C., Keating L., Bellamy M., Baines A.J. Protein 4.1 in forebrain postsynaptic density preparations: Enrichment of 4.1 gene products and detection of 4.1R binding proteins. Eur. J. Biochem. 268:2001;1084-1094
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1084-1094
    • Scott, C.1    Keating, L.2    Bellamy, M.3    Baines, A.J.4
  • 270
    • 0022585350 scopus 로고
    • Filaggrin breakdown to water binding compounds during development of the rat stratum corneum is controlled by the water activity of the environment
    • Scott I.R., Harding C.R. Filaggrin breakdown to water binding compounds during development of the rat stratum corneum is controlled by the water activity of the environment. Dev. Biol. 115:1986;84-92
    • (1986) Dev. Biol. , vol.115 , pp. 84-92
    • Scott, I.R.1    Harding, C.R.2
  • 271
    • 0026442554 scopus 로고
    • Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers
    • Seifert G.J., Lawson D., Wiche G. Immunolocalization of the intermediate filament-associated protein plectin at focal contacts and actin stress fibers. Eur. J. Cell Biol. 59:1992;138-147
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 138-147
    • Seifert, G.J.1    Lawson, D.2    Wiche, G.3
  • 272
    • 2442675099 scopus 로고    scopus 로고
    • Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin
    • Sevcik J., Urbanikova L., Kost'an J., Janda L., Wiche G. Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin. Eur. J. Biochem. 271:2004;1873-1884
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1873-1884
    • Sevcik, J.1    Urbanikova, L.2    Kost'An, J.3    Janda, L.4    Wiche, G.5
  • 273
    • 0033783031 scopus 로고    scopus 로고
    • Bidirectional translocation of neurofilaments along microtubules mediated in part by dynein/dynactin
    • Shah J.V., Flanagan L.A., Janmey P.A., Leterrier J.F. Bidirectional translocation of neurofilaments along microtubules mediated in part by dynein/dynactin. Mol. Biol. Cell. 11:2000;3495-3508
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3495-3508
    • Shah, J.V.1    Flanagan, L.A.2    Janmey, P.A.3    Leterrier, J.F.4
  • 274
    • 0034433639 scopus 로고    scopus 로고
    • Microtubule motors, phosphorylation and axonal transport of neurofilaments
    • Shea T.B. Microtubule motors, phosphorylation and axonal transport of neurofilaments. J. Neurocytol. 29:2000;873-887
    • (2000) J. Neurocytol. , vol.29 , pp. 873-887
    • Shea, T.B.1
  • 275
    • 0034685789 scopus 로고    scopus 로고
    • Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus
    • Shi J., Sugrue S.P. Dissection of protein linkage between keratins and pinin, a protein with dual location at desmosome-intermediate filament complex and in the nucleus. J. Biol. Chem. 275:2000;14910-14915
    • (2000) J. Biol. Chem. , vol.275 , pp. 14910-14915
    • Shi, J.1    Sugrue, S.P.2
  • 276
    • 0021132365 scopus 로고
    • Participation of membrane-associated proteins in the formation of the cross-linked envelope of the keratinocyte
    • Simon M., Green H. Participation of membrane-associated proteins in the formation of the cross-linked envelope of the keratinocyte. Cell. 36:1984;827-834
    • (1984) Cell , vol.36 , pp. 827-834
    • Simon, M.1    Green, H.2
  • 279
    • 0028178390 scopus 로고
    • IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions
    • Skalli O., Jones J.C.R., Gagescu R., Goldman R.D. IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions. J. Biol. Chem. 125:1994;159-170
    • (1994) J. Biol. Chem. , vol.125 , pp. 159-170
    • Skalli, O.1    Jones, J.C.R.2    Gagescu, R.3    Goldman, R.D.4
  • 280
    • 0016291431 scopus 로고
    • Chemical characterization of isolated epidermal desmosomes
    • Skerrow C.J., Matoltsy A.G. Chemical characterization of isolated epidermal desmosomes. J. Biol. Chem. 63:1974;524-530
    • (1974) J. Biol. Chem. , vol.63 , pp. 524-530
    • Skerrow, C.J.1    Matoltsy, A.G.2
  • 281
    • 0029360691 scopus 로고
    • Structure-function relationships in smooth muscle: The missing links
    • Small J.V. Structure-function relationships in smooth muscle: The missing links. Bioessays. 17:1995;785-792
    • (1995) Bioessays , vol.17 , pp. 785-792
    • Small, J.V.1
  • 283
    • 0032446186 scopus 로고    scopus 로고
    • The cytoskeleton of the vertebrate smooth muscle cell
    • Small J.V., Gimona M. The cytoskeleton of the vertebrate smooth muscle cell. Acta Physiol. Scand. 164:1998;341-348
    • (1998) Acta Physiol. Scand. , vol.164 , pp. 341-348
    • Small, J.V.1    Gimona, M.2
  • 284
    • 0032100705 scopus 로고    scopus 로고
    • Defining the interactions between intermediate filaments and desmosomes
    • Smith E.A., Fuchs E. Defining the interactions between intermediate filaments and desmosomes. J. Biol. Chem. 141:1998;1229-1241
    • (1998) J. Biol. Chem. , vol.141 , pp. 1229-1241
    • Smith, E.A.1    Fuchs, E.2
  • 285
    • 0041355342 scopus 로고    scopus 로고
    • Epiplakin gene analysis in mouse reveals a single exon encoding a 725-kDa protein with expression restricted to epithelial tissues
    • Spazierer D., Fuchs P., Proll V., Janda L., Oehler S., Fischer I., Hauptmann R., Wiche G. Epiplakin gene analysis in mouse reveals a single exon encoding a 725-kDa protein with expression restricted to epithelial tissues. J. Biol. Chem. 278:2003;31657-31666
    • (2003) J. Biol. Chem. , vol.278 , pp. 31657-31666
    • Spazierer, D.1    Fuchs, P.2    Proll, V.3    Janda, L.4    Oehler, S.5    Fischer, I.6    Hauptmann, R.7    Wiche, G.8
  • 286
    • 0019417455 scopus 로고
    • Characterization of bullous pemphigoid antigen: A unique basement membrane protein of stratified squamous epithelia
    • Stanley J.R., Hawley-Nelson P., Yuspa S.H., Shevach E.M., Katz S.I. Characterization of bullous pemphigoid antigen: A unique basement membrane protein of stratified squamous epithelia. Cell. 24:1981;897-903
    • (1981) Cell , vol.24 , pp. 897-903
    • Stanley, J.R.1    Hawley-Nelson, P.2    Yuspa, S.H.3    Shevach, E.M.4    Katz, S.I.5
  • 287
    • 0027428693 scopus 로고
    • Functional analysis of desmoplakin domains: Specification of the interaction with keratin versus vimentin intermediate filament networks
    • Stappenbeck T.S., Bornslaeger E.A., Corcoran C.M., Luu H.H., Virata M.L.A., Green K.J. Functional analysis of desmoplakin domains: Specification of the interaction with keratin versus vimentin intermediate filament networks. J. Biol. Chem. 123:1993;691-705
    • (1993) J. Biol. Chem. , vol.123 , pp. 691-705
    • Stappenbeck, T.S.1    Bornslaeger, E.A.2    Corcoran, C.M.3    Luu, H.H.4    Virata, M.L.A.5    Green, K.J.6
  • 288
    • 0026511055 scopus 로고
    • The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells
    • Stappenbeck T.S., Green K.J. The desmoplakin carboxyl terminus coaligns with and specifically disrupts intermediate filament networks when expressed in cultured cells. J. Biol. Chem. 116:1992;1197-1209
    • (1992) J. Biol. Chem. , vol.116 , pp. 1197-1209
    • Stappenbeck, T.S.1    Green, K.J.2
  • 289
    • 0028028177 scopus 로고
    • Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks
    • Stappenbeck T.S., Lamb J.A., Corcoran C.M., Green K.J. Phosphorylation of the desmoplakin COOH terminus negatively regulates its interaction with keratin intermediate filament networks. J. Biol. Chem. 269:1994;29351-29354
    • (1994) J. Biol. Chem. , vol.269 , pp. 29351-29354
    • Stappenbeck, T.S.1    Lamb, J.A.2    Corcoran, C.M.3    Green, K.J.4
  • 291
    • 0033515454 scopus 로고    scopus 로고
    • A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a type VI intermediate filament protein. Limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV alpha-internexin
    • Steinert P.M., Chou Y.H., Prahlad V., Parry D.A.D., Marekov L.N., Wu K.C., Jang S.I., Goldman R.D. A high molecular weight intermediate filament-associated protein in BHK-21 cells is nestin, a type VI intermediate filament protein. Limited co-assembly in vitro to form heteropolymers with type III vimentin and type IV alpha-internexin. J. Biol. Chem. 274:1999;9881-9890
    • (1999) J. Biol. Chem. , vol.274 , pp. 9881-9890
    • Steinert, P.M.1    Chou, Y.H.2    Prahlad, V.3    Parry, D.A.D.4    Marekov, L.N.5    Wu, K.C.6    Jang, S.I.7    Goldman, R.D.8
  • 292
    • 0029050246 scopus 로고
    • The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope
    • Steinert P.M., Marekov L.N. The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope. J. Biol. Chem. 270:1995;17702-17711
    • (1995) J. Biol. Chem. , vol.270 , pp. 17702-17711
    • Steinert, P.M.1    Marekov, L.N.2
  • 293
    • 0032757460 scopus 로고    scopus 로고
    • Initiation of assembly of the cell envelope barrier structure of stratified squamous epithelia
    • Steinert P.M., Marekov L.N. Initiation of assembly of the cell envelope barrier structure of stratified squamous epithelia. Mol. Biol. Cell. 10:1999;4247-4261
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4247-4261
    • Steinert, P.M.1    Marekov, L.N.2
  • 294
    • 0142103315 scopus 로고    scopus 로고
    • Trichohyalin mechanically strengthens the hair follicle: Multiple cross-bridging roles in the inner root sheath
    • Steinert P.M., Parry D.A.D., Marekov L.N. Trichohyalin mechanically strengthens the hair follicle: Multiple cross-bridging roles in the inner root sheath. J. Biol. Chem. 278:2003;41409-41419
    • (2003) J. Biol. Chem. , vol.278 , pp. 41409-41419
    • Steinert, P.M.1    Parry, D.A.D.2    Marekov, L.N.3
  • 295
    • 9444239263 scopus 로고    scopus 로고
    • The endo-lysosomal sorting machinery interacts wtih the intermediate filament cytoskeleton
    • Styers M.L., Salazar G., Love R., Peden A.A., Kowalczyk A.P., Faundez V. The endo-lysosomal sorting machinery interacts wtih the intermediate filament cytoskeleton. Mol. Biol. Cell. 15:2004;5369-5382
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5369-5382
    • Styers, M.L.1    Salazar, G.2    Love, R.3    Peden, A.A.4    Kowalczyk, A.P.5    Faundez, V.6
  • 296
    • 0035147233 scopus 로고    scopus 로고
    • Characterization of the microtubule binding domain of microtubule actin crosslinking factor (MACF): Identification of a novel group of microtubule-associated proteins
    • Sun D., Leung C.L., Liem R.K. Characterization of the microtubule binding domain of microtubule actin crosslinking factor (MACF): Identification of a novel group of microtubule-associated proteins. J. Cell Sci. 114:2001;161-172
    • (2001) J. Cell Sci. , vol.114 , pp. 161-172
    • Sun, D.1    Leung, C.L.2    Liem, R.K.3
  • 298
    • 0029805514 scopus 로고    scopus 로고
    • Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton
    • Svitkina T.M., Verkhovsky A.B., Borisy G.G. Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. J. Biol. Chem. 135:1996;991-1007
    • (1996) J. Biol. Chem. , vol.135 , pp. 991-1007
    • Svitkina, T.M.1    Verkhovsky, A.B.2    Borisy, G.G.3
  • 299
    • 0030784777 scopus 로고    scopus 로고
    • The fate of trichohyalin. Sequential post-translational modifications by peptidyl-arginine deiminase and transglutaminases
    • Tarcsa E., Marekov L.N., Andreoli J., Idler W.W., Candi E., Chung S.I., Steinert P.M. The fate of trichohyalin. Sequential post-translational modifications by peptidyl-arginine deiminase and transglutaminases. J. Biol. Chem. 272:1997;27893-27901
    • (1997) J. Biol. Chem. , vol.272 , pp. 27893-27901
    • Tarcsa, E.1    Marekov, L.N.2    Andreoli, J.3    Idler, W.W.4    Candi, E.5    Chung, S.I.6    Steinert, P.M.7
  • 300
    • 0029824853 scopus 로고    scopus 로고
    • Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin
    • Tarcsa E., Marekov L.N., Mei G., Melino G., Lee S.C., Steinert P.M. Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. J. Biol. Chem. 271:1996;30709-30716
    • (1996) J. Biol. Chem. , vol.271 , pp. 30709-30716
    • Tarcsa, E.1    Marekov, L.N.2    Mei, G.3    Melino, G.4    Lee, S.C.5    Steinert, P.M.6
  • 301
    • 0029014894 scopus 로고
    • Identification of the amino terminus of human filaggrin using differential LC/MS techniques: Implications for profilaggrin processing
    • Thulin C.D., Walsh K.A. Identification of the amino terminus of human filaggrin using differential LC/MS techniques: Implications for profilaggrin processing. Biochemistry. 34:1995;8687-8692
    • (1995) Biochemistry , vol.34 , pp. 8687-8692
    • Thulin, C.D.1    Walsh, K.A.2
  • 304
    • 0023284867 scopus 로고
    • Efficient interaction of nonpolar lipids with intermediate filaments of the vimentin type
    • Traub P., Perides G., Kuhn S., Scherbarth A. Efficient interaction of nonpolar lipids with intermediate filaments of the vimentin type. Eur. J. Cell Biol. 43:1987;55-64
    • (1987) Eur. J. Cell Biol. , vol.43 , pp. 55-64
    • Traub, P.1    Perides, G.2    Kuhn, S.3    Scherbarth, A.4
  • 305
    • 0022397820 scopus 로고
    • Tenacious binding of lipids to vimentin during its isolation and purification from Ehrlich ascites tumor cells
    • Traub P., Perides G., Scherbarth A., Traub U. Tenacious binding of lipids to vimentin during its isolation and purification from Ehrlich ascites tumor cells. FEBS Lett. 193:1985;217-221
    • (1985) FEBS Lett. , vol.193 , pp. 217-221
    • Traub, P.1    Perides, G.2    Scherbarth, A.3    Traub, U.4
  • 306
    • 0027468175 scopus 로고
    • Contributions of cytoplasmic domains of desmosomal cadherins to desmosome assembly and intermediate filament anchorage
    • Troyanovsky S.M., Eshkind L.G., Troyanovsky R.B., Leube R.E., Franke W.W. Contributions of cytoplasmic domains of desmosomal cadherins to desmosome assembly and intermediate filament anchorage. Cell. 72:1993;561-574
    • (1993) Cell , vol.72 , pp. 561-574
    • Troyanovsky, S.M.1    Eshkind, L.G.2    Troyanovsky, R.B.3    Leube, R.E.4    Franke, W.W.5
  • 307
    • 0022371564 scopus 로고
    • Desmocalmin: A calmodulin-binding high molecular weight protein isolated from desmosomes
    • Tsukita S., Tsukita S. Desmocalmin: A calmodulin-binding high molecular weight protein isolated from desmosomes. J. Biol. Chem. 101:1985;2070-2080
    • (1985) J. Biol. Chem. , vol.101 , pp. 2070-2080
    • Tsukita, S.1    Tsukita, S.2
  • 308
    • 0347513188 scopus 로고    scopus 로고
    • The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress
    • Tsuruta D., Jones J.C. The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress. J. Cell Sci. 116:2003;4977-4984
    • (2003) J. Cell Sci. , vol.116 , pp. 4977-4984
    • Tsuruta, D.1    Jones, J.C.2
  • 309
    • 0034703024 scopus 로고    scopus 로고
    • Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo
    • Tzivion G., Luo Z.J., Avruch J. Calyculin A-induced vimentin phosphorylation sequesters 14-3-3 and displaces other 14-3-3 partners in vivo. J. Biol. Chem. 275:2000;29772-29778
    • (2000) J. Biol. Chem. , vol.275 , pp. 29772-29778
    • Tzivion, G.1    Luo, Z.J.2    Avruch, J.3
  • 315
    • 0033776708 scopus 로고    scopus 로고
    • Rapid movement of axonal neurofilaments interrupted by prolonged pauses
    • Wang L., Ho C.L., Sun D., Liem R.K., Brown A. Rapid movement of axonal neurofilaments interrupted by prolonged pauses. Nat. Cell Biol. 2:2000;137-141
    • (2000) Nat. Cell Biol. , vol.2 , pp. 137-141
    • Wang, L.1    Ho, C.L.2    Sun, D.3    Liem, R.K.4    Brown, A.5
  • 316
    • 0030565430 scopus 로고    scopus 로고
    • Interaction of smooth muscle calponin and desmin
    • Wang P., Gusev N.B. Interaction of smooth muscle calponin and desmin. FEBS Lett. 392:1996;255-258
    • (1996) FEBS Lett. , vol.392 , pp. 255-258
    • Wang, P.1    Gusev, N.B.2
  • 317
    • 0036538199 scopus 로고    scopus 로고
    • F-actin serves as a template for cytokeratin organization in cell free extracts
    • Weber K.L., Bement W.M. F-actin serves as a template for cytokeratin organization in cell free extracts. J. Cell Sci. 115:2002;1373-1382
    • (2002) J. Cell Sci. , vol.115 , pp. 1373-1382
    • Weber, K.L.1    Bement, W.M.2
  • 318
    • 0021988001 scopus 로고
    • Bullous pemphigoid antigen localization suggests an intracellular association with hemidesmosomes
    • Westgate G.E., Weaver A.C., Couchman J.R. Bullous pemphigoid antigen localization suggests an intracellular association with hemidesmosomes. J. Invest. Dermatol. 84:1985;218-224
    • (1985) J. Invest. Dermatol. , vol.84 , pp. 218-224
    • Westgate, G.E.1    Weaver, A.C.2    Couchman, J.R.3
  • 319
    • 0024329341 scopus 로고
    • Plectin: General overview and appraisal of its potential role as a subunit protein of the cytomatrix
    • Wiche G. Plectin: General overview and appraisal of its potential role as a subunit protein of the cytomatrix. Crit. Rev. Biochem. Mol. Biol. 24:1989;41-67
    • (1989) Crit. Rev. Biochem. Mol. Biol. , vol.24 , pp. 41-67
    • Wiche, G.1
  • 320
    • 0031663054 scopus 로고    scopus 로고
    • Role of plectin in cytoskeleton organization and dynamics
    • Wiche G. Role of plectin in cytoskeleton organization and dynamics. J. Cell Sci. 111:1998;2477-2486
    • (1998) J. Cell Sci. , vol.111 , pp. 2477-2486
    • Wiche, G.1
  • 321
    • 0026014584 scopus 로고
    • Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil
    • Wiche G., Becker B., Luber K., Weitzer G., Castanon M.J., Hauptmann R., Stratowa C., Stewart M. Cloning and sequencing of rat plectin indicates a 466-kD polypeptide chain with a three-domain structure based on a central alpha-helical coiled coil. J. Biol. Chem. 114:1991;83-99
    • (1991) J. Biol. Chem. , vol.114 , pp. 83-99
    • Wiche, G.1    Becker, B.2    Luber, K.3    Weitzer, G.4    Castanon, M.J.5    Hauptmann, R.6    Stratowa, C.7    Stewart, M.8
  • 322
    • 0020329482 scopus 로고
    • Plectin: A high-molecular-weight cytoskeletal polypeptide component that copurifies with intermediate filaments of the vimentin type
    • Wiche G., Herrmann H., Leichtfried F., Pytela R. Plectin: A high-molecular-weight cytoskeletal polypeptide component that copurifies with intermediate filaments of the vimentin type. Cold Spring Harb. Symp. Quant. Biol. 46:1982;475-482
    • (1982) Cold Spring Harb. Symp. Quant. Biol. , vol.46 , pp. 475-482
    • Wiche, G.1    Herrmann, H.2    Leichtfried, F.3    Pytela, R.4
  • 323
    • 0021749865 scopus 로고
    • Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes
    • Wiche G., Krepler R., Artlieb U., Pytela R., Aberer W. Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes. Exp. Cell Res. 155:1984;43-49
    • (1984) Exp. Cell Res. , vol.155 , pp. 43-49
    • Wiche, G.1    Krepler, R.2    Artlieb, U.3    Pytela, R.4    Aberer, W.5
  • 325
    • 0032831465 scopus 로고    scopus 로고
    • The PKD1 gene product, "polycystin-1," is a tyrosine-phosphorylated protein that colocalizes with alpha2beta1-integrin in focal clusters in adherent renal epithelia
    • Wilson P.D., Geng L., Li X., Burrow C.R. The PKD1 gene product, "polycystin-1," is a tyrosine-phosphorylated protein that colocalizes with alpha2beta1-integrin in focal clusters in adherent renal epithelia. Lab. Invest. 79:1999;1311-1323
    • (1999) Lab. Invest. , vol.79 , pp. 1311-1323
    • Wilson, P.D.1    Geng, L.2    Li, X.3    Burrow, C.R.4
  • 328
    • 3242671425 scopus 로고    scopus 로고
    • The mouse synemin gene encodes three intermediate filament proteins generated by alternative exon usage and different open reading frames
    • Xue Z.G., Cheraud Y., Brocheriou V., Izmiryan A., Titeux M., Paulin D., Li Z. The mouse synemin gene encodes three intermediate filament proteins generated by alternative exon usage and different open reading frames. Exp. Cell Res. 298:2004;431-444
    • (2004) Exp. Cell Res. , vol.298 , pp. 431-444
    • Xue, Z.G.1    Cheraud, Y.2    Brocheriou, V.3    Izmiryan, A.4    Titeux, M.5    Paulin, D.6    Li, Z.7
  • 329
    • 0034030749 scopus 로고    scopus 로고
    • Phospho-dependent association of neurofilament proteins with kinesin in situ
    • Yabe J.T., Jung C., Chan W.K., Shea T.B. Phospho-dependent association of neurofilament proteins with kinesin in situ. Cell Motil. Cytoskeleton. 45:2000;249-262
    • (2000) Cell Motil. Cytoskeleton , vol.45 , pp. 249-262
    • Yabe, J.T.1    Jung, C.2    Chan, W.K.3    Shea, T.B.4
  • 330
    • 0032694199 scopus 로고    scopus 로고
    • Kinesin-mediated transport of neurofilament protein oligomers in growing axons
    • Yabe J.T., Pimenta A., Shea T.B. Kinesin-mediated transport of neurofilament protein oligomers in growing axons. J. Cell Sci. 112:(Pt 21):1999;3799-3814
    • (1999) J. Cell Sci. , vol.112 , Issue.21 PART , pp. 3799-3814
    • Yabe, J.T.1    Pimenta, A.2    Shea, T.B.3
  • 332
    • 0021947315 scopus 로고
    • A 300,000 MW intermediate filament-associated protein in baby hamster kidney (BHK-21) cells
    • Yang H.-Y., Lieska N., Goldman A., Goldman B. A 300,000 MW intermediate filament-associated protein in baby hamster kidney (BHK-21) cells. J. Biol. Chem. 100:1985;620-631
    • (1985) J. Biol. Chem. , vol.100 , pp. 620-631
    • Yang, H.-Y.1    Lieska, N.2    Goldman, A.3    Goldman, B.4
  • 334
    • 0030598838 scopus 로고    scopus 로고
    • An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments
    • Yang Y., Dowling J., Yu Q.-C., Kouklis P., Cleveland D.W., Fuchs E. An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments. Cell. 86:1996;655-665
    • (1996) Cell , vol.86 , pp. 655-665
    • Yang, Y.1    Dowling, J.2    Yu, Q.-C.3    Kouklis, P.4    Cleveland, D.W.5    Fuchs, E.6
  • 335
    • 0035972146 scopus 로고    scopus 로고
    • Insights into the dynamic properties of keratin intermediate filaments in living epithelial cells
    • Yoon K.H., Yoon M., Moir R.D., Khuon S., Flitney F.W., Goldman R.D. Insights into the dynamic properties of keratin intermediate filaments in living epithelial cells. J. Cell Biol. 153:2001;503-516
    • (2001) J. Cell Biol. , vol.153 , pp. 503-516
    • Yoon, K.H.1    Yoon, M.2    Moir, R.D.3    Khuon, S.4    Flitney, F.W.5    Goldman, R.D.6
  • 336
    • 0032487443 scopus 로고    scopus 로고
    • Motile properties of vimentin intermediate filament networks in living cells
    • Yoon M., Moir R.D., Prahlad V., Goldman R.D. Motile properties of vimentin intermediate filament networks in living cells. J. Cell Biol. 143:1998;147-157
    • (1998) J. Cell Biol. , vol.143 , pp. 147-157
    • Yoon, M.1    Moir, R.D.2    Prahlad, V.3    Goldman, R.D.4
  • 337
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir E., Geiger B. Molecular complexity and dynamics of cell-matrix adhesions. J. Cell Sci. 114:2001;3583-3590
    • (2001) J. Cell Sci. , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 338
    • 1842584782 scopus 로고    scopus 로고
    • Proteins that bind A-type lamins: Integrating isolated clues
    • Zastrow M.S., Vlcek S., Wilson K.L. Proteins that bind A-type lamins: Integrating isolated clues. J. Cell Sci. 117:2004;979-987
    • (2004) J. Cell Sci. , vol.117 , pp. 979-987
    • Zastrow, M.S.1    Vlcek, S.2    Wilson, K.L.3
  • 339
    • 0033843879 scopus 로고    scopus 로고
    • Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies
    • Zatloukal K., Stumptner C., Lehner M., Denk H., Baribault H., Eshkind L.G., Franke W.W. Cytokeratin 8 protects from hepatotoxicity, and its ratio to cytokeratin 18 determines the ability of hepatocytes to form Mallory bodies. Am. J. Pathol. 156:2000;1263-1274
    • (2000) Am. J. Pathol. , vol.156 , pp. 1263-1274
    • Zatloukal, K.1    Stumptner, C.2    Lehner, M.3    Denk, H.4    Baribault, H.5    Eshkind, L.G.6    Franke, W.W.7
  • 340
    • 0033788835 scopus 로고    scopus 로고
    • Plakoglobin and β-catenin: Protein interactions, regulation and biological roles
    • Zhurinsky J., Shtutman M., Ben-Ze'ev A. Plakoglobin and β-catenin: Protein interactions, regulation and biological roles. J. Cell Sci. 113:2000;3127-3139
    • (2000) J. Cell Sci. , vol.113 , pp. 3127-3139
    • Zhurinsky, J.1    Shtutman, M.2    Ben-Ze'Ev, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.