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Volumn 360, Issue 2, 2015, Pages 363-378

Molecular architecture and function of the hemidesmosome

Author keywords

Bullous pemphigoid antigen; Epidermolysis bullosa; Hemidesmosomes; Integrin; Plectin

Indexed keywords

MEMBRANE PROTEIN;

EID: 84939940392     PISSN: 0302766X     EISSN: 14320878     Source Type: Journal    
DOI: 10.1007/s00441-014-2061-z     Document Type: Review
Times cited : (88)

References (181)
  • 1
    • 34547757016 scopus 로고    scopus 로고
    • Conditional targeting of plectin in prenatal and adult mouse stratified epithelia causes keratinocyte fragility and lesional epidermal barrier defects
    • COI: 1:CAS:528:DC%2BD2sXpslChsb0%3D, PID: 17606998
    • Ackerl R, Walko G, Fuchs P, Fischer I, Schmuth M, Wiche G (2007) Conditional targeting of plectin in prenatal and adult mouse stratified epithelia causes keratinocyte fragility and lesional epidermal barrier defects. J Cell Sci 120:2435–2443
    • (2007) J Cell Sci , vol.120 , pp. 2435-2443
    • Ackerl, R.1    Walko, G.2    Fuchs, P.3    Fischer, I.4    Schmuth, M.5    Wiche, G.6
  • 2
    • 77954758155 scopus 로고    scopus 로고
    • PKC-delta and -eta, MEKK-1, MEK-6, MEK-3, and p38-delta are essential mediators of the response of normal human epidermal keratinocytes to differentiating agents
    • COI: 1:CAS:528:DC%2BC3cXovVCmtrw%3D, PID: 20445555
    • Adhikary G, Chew YC, Reece EA, Eckert RL (2010) PKC-delta and -eta, MEKK-1, MEK-6, MEK-3, and p38-delta are essential mediators of the response of normal human epidermal keratinocytes to differentiating agents. J Invest Dermatol 130:2017–2030
    • (2010) J Invest Dermatol , vol.130 , pp. 2017-2030
    • Adhikary, G.1    Chew, Y.C.2    Reece, E.A.3    Eckert, R.L.4
  • 3
    • 0035354189 scopus 로고    scopus 로고
    • Protein kinase Cdelta-mediated phosphorylation of alpha6beta4 is associated with reduced integrin localization to the hemidesmosome and decreased keratinocyte attachment
    • COI: 1:CAS:528:DC%2BD3MXktlWjsLY%3D, PID: 11389095
    • Alt A, Ohba M, Li L, Gartsbein M, Belanger A, Denning MF, Kuroki T, Yuspa SH, Tennenbaum T (2001) Protein kinase Cdelta-mediated phosphorylation of alpha6beta4 is associated with reduced integrin localization to the hemidesmosome and decreased keratinocyte attachment. Cancer Res 61:4591–4598
    • (2001) Cancer Res , vol.61 , pp. 4591-4598
    • Alt, A.1    Ohba, M.2    Li, L.3    Gartsbein, M.4    Belanger, A.5    Denning, M.F.6    Kuroki, T.7    Yuspa, S.H.8    Tennenbaum, T.9
  • 4
    • 78049333308 scopus 로고    scopus 로고
    • Adult epidermal Notch activity induces dermal accumulation of T cells and neural crest derivatives through upregulation of jagged 1
    • COI: 1:CAS:528:DC%2BC3cXhsFCntb7I, PID: 20940224
    • Ambler CA, Watt FM (2010) Adult epidermal Notch activity induces dermal accumulation of T cells and neural crest derivatives through upregulation of jagged 1. Development 137:3569–3579
    • (2010) Development , vol.137 , pp. 3569-3579
    • Ambler, C.A.1    Watt, F.M.2
  • 5
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • PID: 9389647
    • Andrä K, Lassmann H, Bittner R, Shorny S, Fässler R, Propst F, Wiche G (1997) Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture. Genes Dev 11:3143–3156
    • (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
  • 7
    • 84872200290 scopus 로고    scopus 로고
    • The laminin family
    • PID: 23263632
    • Aumailley M (2013) The laminin family. Cell Adh Migr 7:48–55
    • (2013) Cell Adh Migr , vol.7 , pp. 48-55
    • Aumailley, M.1
  • 8
    • 33751078603 scopus 로고    scopus 로고
    • Canonical notch signaling functions as a commitment switch in the epidermal lineage
    • COI: 1:CAS:528:DC%2BD28XhtFynu7fK, PID: 17079689
    • Blanpain C, Lowry WE, Pasolli HA, Fuchs E (2006) Canonical notch signaling functions as a commitment switch in the epidermal lineage. Genes Dev 20:3022–3035
    • (2006) Genes Dev , vol.20 , pp. 3022-3035
    • Blanpain, C.1    Lowry, W.E.2    Pasolli, H.A.3    Fuchs, E.4
  • 9
    • 0030773865 scopus 로고    scopus 로고
    • The localization of bullous pemphigoid antigen 180 (BP180) in hemidesmosomes is mediated by its cytoplasmic domain and seems to be regulated by the beta4 integrin subunit
    • COI: 1:CAS:528:DyaK2sXitFentbY%3D, PID: 9087447
    • Borradori L, Koch PJ, Niessen CM, Erkeland S, van Leusden MR, Sonnenberg A (1997) The localization of bullous pemphigoid antigen 180 (BP180) in hemidesmosomes is mediated by its cytoplasmic domain and seems to be regulated by the beta4 integrin subunit. J Cell Biol 136:1333–1347
    • (1997) J Cell Biol , vol.136 , pp. 1333-1347
    • Borradori, L.1    Koch, P.J.2    Niessen, C.M.3    Erkeland, S.4    van Leusden, M.R.5    Sonnenberg, A.6
  • 10
    • 84897055612 scopus 로고    scopus 로고
    • Plakins, a versatile family of cytolinkers: roles in skin integrity and in human diseases
    • COI: 1:CAS:528:DC%2BC3sXhvFGrtrzL, PID: 24352042
    • Bouameur JE, Favre B, Borradori L (2014a) Plakins, a versatile family of cytolinkers: roles in skin integrity and in human diseases. J Invest Dermatol 134:885–894
    • (2014) J Invest Dermatol , vol.134 , pp. 885-894
    • Bouameur, J.E.1    Favre, B.2    Borradori, L.3
  • 11
    • 84908570044 scopus 로고    scopus 로고
    • Interaction of Plectin with Keratins 5 and 14: Dependence on Several Plectin Domains and Keratin Quaternary Structure
    • COI: 1:CAS:528:DC%2BC2cXhtFehs7fF, PID: 24940650
    • Bouameur JE, Favre B, Fontao L, Lingasamy P, Begre N, Borradori L (2014b) Interaction of Plectin with Keratins 5 and 14: Dependence on Several Plectin Domains and Keratin Quaternary Structure. J Invest Dermatol 134:2776–2783
    • (2014) J Invest Dermatol , vol.134 , pp. 2776-2783
    • Bouameur, J.E.1    Favre, B.2    Fontao, L.3    Lingasamy, P.4    Begre, N.5    Borradori, L.6
  • 12
    • 84876521580 scopus 로고    scopus 로고
    • Skin basement membrane: the foundation of epidermal integrity–BM functions and diverse roles of bridging molecules nidogen and perlecan
    • Breitkreutz D, Koxholt I, Thiemann K, Nischt R (2013) Skin basement membrane: the foundation of epidermal integrity–BM functions and diverse roles of bridging molecules nidogen and perlecan. Biomed Res Intern 2013:179784
    • (2013) Biomed Res Intern , vol.2013 , pp. 179784
    • Breitkreutz, D.1    Koxholt, I.2    Thiemann, K.3    Nischt, R.4
  • 13
    • 0016711953 scopus 로고
    • The epidermal-dermal junction
    • COI: 1:STN:280:DyaE2M3ht1CgtQ%3D%3D, PID: 1097542
    • Briggaman RA, Wheeler CE Jr (1975) The epidermal-dermal junction. J Invest Dermatol 65:71–84
    • (1975) J Invest Dermatol , vol.65 , pp. 71-84
    • Briggaman, R.A.1    Wheeler, C.E.2
  • 14
    • 33645931350 scopus 로고    scopus 로고
    • High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV
    • COI: 1:CAS:528:DC%2BD28XjtFGjs7g%3D, PID: 16563355
    • Brittingham R, Uitto J, Fertala A (2006) High-affinity binding of the NC1 domain of collagen VII to laminin 5 and collagen IV. Biochem Biophys Res Commun 343:692–699
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 692-699
    • Brittingham, R.1    Uitto, J.2    Fertala, A.3
  • 15
    • 0029035706 scopus 로고
    • The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1
    • COI: 1:CAS:528:DyaK2MXms1Kjtbg%3D, PID: 7670468
    • Brown A, Bernier G, Mathieu M, Rossant J, Kothary R (1995) The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1. Nat Genet 10:301–306
    • (1995) Nat Genet , vol.10 , pp. 301-306
    • Brown, A.1    Bernier, G.2    Mathieu, M.3    Rossant, J.4    Kothary, R.5
  • 16
    • 70450267632 scopus 로고    scopus 로고
    • Dystrophic epidermolysis bullosa: pathogenesis and clinical features
    • COI: 1:CAS:528:DC%2BC3cXhsVSnsrw%3D, PID: 19945622
    • Bruckner-Tuderman L (2010) Dystrophic epidermolysis bullosa: pathogenesis and clinical features. Dermatol Clin 28:107–114
    • (2010) Dermatol Clin , vol.28 , pp. 107-114
    • Bruckner-Tuderman, L.1
  • 19
    • 0025679064 scopus 로고
    • Distinct functions for integrins alpha 3 beta 1 in focal adhesions and alpha 6 beta 4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosomes
    • COI: 1:STN:280:DyaK3M7gtVChtw%3D%3D, PID: 2269668
    • Carter WG, Kaur P, Gil SG, Gahr PJ, Wayner EA (1990) Distinct functions for integrins alpha 3 beta 1 in focal adhesions and alpha 6 beta 4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosomes. J Cell Biol 111:3141–3154
    • (1990) J Cell Biol , vol.111 , pp. 3141-3154
    • Carter, W.G.1    Kaur, P.2    Gil, S.G.3    Gahr, P.J.4    Wayner, E.A.5
  • 20
    • 84879796143 scopus 로고    scopus 로고
    • Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve
    • PID: 23748243
    • Castañón MJ, Walko G, Winter L, Wiche G (2013) Plectin-intermediate filament partnership in skin, skeletal muscle, and peripheral nerve. Histochem Cell Biol 140:33–53
    • (2013) Histochem Cell Biol , vol.140 , pp. 33-53
    • Castañón, M.J.1    Walko, G.2    Winter, L.3    Wiche, G.4
  • 21
    • 70450285355 scopus 로고    scopus 로고
    • Epidermolysis bullosa with pyloric atresia
    • COI: 1:CAS:528:DC%2BC3cXhsVSgu7s%3D, PID: 19945615
    • Chung HJ, Uitto J (2010a) Epidermolysis bullosa with pyloric atresia. Dermatol Clin 28:43–54
    • (2010) Dermatol Clin , vol.28 , pp. 43-54
    • Chung, H.J.1    Uitto, J.2
  • 22
    • 70450235277 scopus 로고    scopus 로고
    • Type VII collagen: the anchoring fibril protein at fault in dystrophic epidermolysis bullosa
    • COI: 1:CAS:528:DC%2BC3cXhsVSnsr8%3D, PID: 19945621
    • Chung HJ, Uitto J (2010b) Type VII collagen: the anchoring fibril protein at fault in dystrophic epidermolysis bullosa. Dermatol Clin 28:93–105
    • (2010) Dermatol Clin , vol.28 , pp. 93-105
    • Chung, H.J.1    Uitto, J.2
  • 23
    • 0034709651 scopus 로고    scopus 로고
    • The 300-kDa intermediate filament-associated protein (IFAP300) is a hamster plectin ortholog
    • COI: 1:CAS:528:DC%2BD3cXkt1Kmsrw%3D, PID: 10873583
    • Clubb BH, Chou YH, Herrmann H, Svitkina TM, Borisy GG, Goldman RD (2000) The 300-kDa intermediate filament-associated protein (IFAP300) is a hamster plectin ortholog. Biochem Biophys Res Commun 273:183–187
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 183-187
    • Clubb, B.H.1    Chou, Y.H.2    Herrmann, H.3    Svitkina, T.M.4    Borisy, G.G.5    Goldman, R.D.6
  • 24
    • 0027499510 scopus 로고
    • Chromosomal localization of mouse bullous pemphigoid antigens. BPAG1 and BPAG2: identification of a new region of homology between mouse and human chromosomes
    • COI: 1:CAS:528:DyaK3sXhvVCru7w%3D, PID: 8432531
    • Copeland NG, Gilbert DJ, Li K, Sawamura D, Giudice GJ, Chu ML, Jenkins NA, Uitto J (1993) Chromosomal localization of mouse bullous pemphigoid antigens. BPAG1 and BPAG2: identification of a new region of homology between mouse and human chromosomes. Genomics 15:180–181
    • (1993) Genomics , vol.15 , pp. 180-181
    • Copeland, N.G.1    Gilbert, D.J.2    Li, K.3    Sawamura, D.4    Giudice, G.J.5    Chu, M.L.6    Jenkins, N.A.7    Uitto, J.8
  • 26
    • 67349092209 scopus 로고    scopus 로고
    • Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes
    • PID: 19242489
    • de Pereda JM, Lillo MP, Sonnenberg A (2009a) Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes. EMBO J 28:1180–1190
    • (2009) EMBO J , vol.28 , pp. 1180-1190
    • de Pereda, J.M.1    Lillo, M.P.2    Sonnenberg, A.3
  • 27
  • 28
    • 0025053990 scopus 로고
    • Isolation of a human epidermal cDNA corresponding to the 180-kD autoantigen recognized by bullous pemphigoid and herpes gestationis sera. Immunolocalization of this protein to the hemidesmosome
    • COI: 1:CAS:528:DyaK3cXmtV2rsrs%3D, PID: 1698819
    • Diaz LA, Ratrie H 3rd, Saunders WS, Futamura S, Squiquera HL, Anhalt GJ, Giudice GJ (1990) Isolation of a human epidermal cDNA corresponding to the 180-kD autoantigen recognized by bullous pemphigoid and herpes gestationis sera. Immunolocalization of this protein to the hemidesmosome. J Clin Invest 86:1088–1094
    • (1990) J Clin Invest , vol.86 , pp. 1088-1094
    • Diaz, L.A.1    Ratrie, H.2    Saunders, W.S.3    Futamura, S.4    Squiquera, H.L.5    Anhalt, G.J.6    Giudice, G.J.7
  • 29
    • 0029666420 scopus 로고    scopus 로고
    • Beta4 integrin is required for hemidesmosome formation, cell adhesion and cell survival
    • COI: 1:CAS:528:DyaK28XktlKju7c%3D, PID: 8707838
    • Dowling J, Yu QC, Fuchs E (1996) Beta4 integrin is required for hemidesmosome formation, cell adhesion and cell survival. J Cell Biol 134:559–572
    • (1996) J Cell Biol , vol.134 , pp. 559-572
    • Dowling, J.1    Yu, Q.C.2    Fuchs, E.3
  • 30
    • 0029092515 scopus 로고
    • Expression pattern of the bullous pemphigoid-180 antigen in normal and neoplastic epithelia
    • COI: 1:STN:280:DyaK287kt1Gltg%3D%3D, PID: 8546992
    • Fairley JA, Heintz PW, Neuburg M, Diaz LA, Giudice GJ (1995) Expression pattern of the bullous pemphigoid-180 antigen in normal and neoplastic epithelia. Br J Dermatol 133:385–391
    • (1995) Br J Dermatol , vol.133 , pp. 385-391
    • Fairley, J.A.1    Heintz, P.W.2    Neuburg, M.3    Diaz, L.A.4    Giudice, G.J.5
  • 31
    • 68949094493 scopus 로고    scopus 로고
    • Extracutaneous manifestations and complications of inherited epidermolysis bullosa: Part I. Epithelial associated tissues
    • PID: 19700010
    • Fine JD, Mellerio JE (2009a) Extracutaneous manifestations and complications of inherited epidermolysis bullosa: Part I. Epithelial associated tissues. J Am Acad Dermatol 61:367–384
    • (2009) J Am Acad Dermatol , vol.61 , pp. 367-384
    • Fine, J.D.1    Mellerio, J.E.2
  • 32
    • 68949145390 scopus 로고    scopus 로고
    • Extracutaneous manifestations and complications of inherited epidermolysis bullosa: Part II. Other organs
    • PID: 19700011
    • Fine JD, Mellerio JE (2009b) Extracutaneous manifestations and complications of inherited epidermolysis bullosa: Part II. Other organs. J Am Acad Dermatol 61:387–402
    • (2009) J Am Acad Dermatol , vol.61 , pp. 387-402
    • Fine, J.D.1    Mellerio, J.E.2
  • 34
    • 0023645941 scopus 로고
    • Structure and hydrodynamic properties of plectin molecules
    • COI: 1:CAS:528:DyaL1cXovF2rsA%3D%3D, PID: 3430617
    • Foisner R, Wiche G (1987) Structure and hydrodynamic properties of plectin molecules. J Mol Biol 198:515–531
    • (1987) J Mol Biol , vol.198 , pp. 515-531
    • Foisner, R.1    Wiche, G.2
  • 35
    • 0033179106 scopus 로고    scopus 로고
    • Regulation of the type II hemidesmosomal plaque assembly in intestinal epithelial cells
    • COI: 1:CAS:528:DyaK1MXksFSjsbs%3D, PID: 10413585
    • Fontao L, Stutzmann J, Gendry P, Launay JF (1999) Regulation of the type II hemidesmosomal plaque assembly in intestinal epithelial cells. Exp Cell Res 250:298–312
    • (1999) Exp Cell Res , vol.250 , pp. 298-312
    • Fontao, L.1    Stutzmann, J.2    Gendry, P.3    Launay, J.F.4
  • 36
    • 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
    • COI: 1:CAS:528:DC%2BD3MXkslWktb4%3D, PID: 11493642
    • Fontao L, Geerts D, Kuikman I, Koster J, Kramer D, Sonnenberg A (2001) 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 114:2065–2076
    • (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
  • 37
    • 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
    • COI: 1:CAS:528:DC%2BD3sXktFKiu7Y%3D, PID: 12802069
    • Fontao L, Favre B, Riou S, Geerts D, Jaunin F, Saurat JH, Green KJ, Sonnenberg A, Borradori L (2003) 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 14:1978–1992
    • (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
  • 39
    • 78549232337 scopus 로고    scopus 로고
    • EGF-induced MAPK signaling inhibits hemidesmosome formation through phosphorylation of the integrin {beta}4
    • COI: 1:CAS:528:DC%2BC3cXhsVCrt73O, PID: 20870721
    • Frijns E, Sachs N, Kreft M, Wilhelmsen K, Sonnenberg A (2010) EGF-induced MAPK signaling inhibits hemidesmosome formation through phosphorylation of the integrin {beta}4. J Biol Chem 285:37650–37662
    • (2010) J Biol Chem , vol.285 , pp. 37650-37662
    • Frijns, E.1    Sachs, N.2    Kreft, M.3    Wilhelmsen, K.4    Sonnenberg, A.5
  • 40
    • 84859726094 scopus 로고    scopus 로고
    • Phosphorylation of threonine 1736 in the C-terminal tail of integrin beta4 contributes to hemidesmosome disassembly
    • COI: 1:CAS:528:DC%2BC38XlvFSqurs%3D, PID: 22357621
    • Frijns E, Kuikman I, Litjens S, Raspe M, Jalink K, Ports M, Wilhelmsen K, Sonnenberg A (2012) Phosphorylation of threonine 1736 in the C-terminal tail of integrin beta4 contributes to hemidesmosome disassembly. Mol Biol Cell 23:1475–1485
    • (2012) Mol Biol Cell , vol.23 , pp. 1475-1485
    • Frijns, E.1    Kuikman, I.2    Litjens, S.3    Raspe, M.4    Jalink, K.5    Ports, M.6    Wilhelmsen, K.7    Sonnenberg, A.8
  • 41
    • 0042913170 scopus 로고    scopus 로고
    • Evidence that Myc activation depletes the epidermal stem cell compartment by modulating adhesive interactions with the local microenvironment
    • COI: 1:CAS:528:DC%2BD3sXltFart7Y%3D, PID: 12736221
    • Frye M, Gardner C, Li ER, Arnold I, Watt FM (2003) Evidence that Myc activation depletes the epidermal stem cell compartment by modulating adhesive interactions with the local microenvironment. Development 130:2793–2808
    • (2003) Development , vol.130 , pp. 2793-2808
    • Frye, M.1    Gardner, C.2    Li, E.R.3    Arnold, I.4    Watt, F.M.5
  • 42
    • 0036245242 scopus 로고    scopus 로고
    • Getting under the skin of epidermal morphogenesis
    • COI: 1:CAS:528:DC%2BD38Xit1Cks7o%3D, PID: 11972157
    • Fuchs E, Raghavan S (2002) Getting under the skin of epidermal morphogenesis. Nat Rev Genet 3:199–209
    • (2002) Nat Rev Genet , vol.3 , pp. 199-209
    • Fuchs, E.1    Raghavan, S.2
  • 43
    • 0344462732 scopus 로고    scopus 로고
    • Unusual 5' transcript complexity of plectin isoforms: novel tissue-specific exons modulate actin binding activity
    • COI: 1:CAS:528:DyaK1MXnvFKrur8%3D, PID: 10556294
    • Fuchs P, Zörer M, Rezniczek GA, Spazierer D, Oehler S, Castañón MJ, Hauptmann R, Wiche G (1999) Unusual 5' transcript complexity of plectin isoforms: novel tissue-specific exons modulate actin binding activity. Hum Mol Genet 8:2461–2472
    • (1999) Hum Mol Genet , vol.8 , pp. 2461-2472
    • Fuchs, P.1    Zörer, M.2    Rezniczek, G.A.3    Spazierer, D.4    Oehler, S.5    Castañón, M.J.6    Hauptmann, R.7    Wiche, G.8
  • 45
    • 0029970098 scopus 로고    scopus 로고
    • Defective expression of plectin/HD1 in epidermolysis bullosa simplex with muscular dystrophy
    • COI: 1:CAS:528:DyaK28XjtFChtrc%3D, PID: 8636409
    • Gache Y, Chavanas S, Lacour JP, Wiche G, Owaribe K, Meneguzzi G, Ortonne JP (1996) Defective expression of plectin/HD1 in epidermolysis bullosa simplex with muscular dystrophy. J Clin Invest 97:2289–2298
    • (1996) J Clin Invest , vol.97 , pp. 2289-2298
    • Gache, Y.1    Chavanas, S.2    Lacour, J.P.3    Wiche, G.4    Owaribe, K.5    Meneguzzi, G.6    Ortonne, J.P.7
  • 46
    • 0029744414 scopus 로고    scopus 로고
    • Functional Re-expression of laminin-5 in laminin-gamma2-deficient human keratinocytes modifies cell morphology, motility, and adhesion
    • COI: 1:CAS:528:DyaK28XkslCju7g%3D, PID: 8702488
    • Gagnoux-Palacios L, Vailly J, Durand-Clement M, Wagner E, Ortonne JP, Meneguzzi G (1996) Functional Re-expression of laminin-5 in laminin-gamma2-deficient human keratinocytes modifies cell morphology, motility, and adhesion. J Biol Chem 271:18437–18444
    • (1996) J Biol Chem , vol.271 , pp. 18437-18444
    • Gagnoux-Palacios, L.1    Vailly, J.2    Durand-Clement, M.3    Wagner, E.4    Ortonne, J.P.5    Meneguzzi, G.6
  • 47
    • 0030718613 scopus 로고    scopus 로고
    • Hemidesmosome assembly assessed by expression of a wild-type integrin beta 4 cDNA in junctional epidermolysis bullosa keratinocytes
    • COI: 1:STN:280:DyaK1c%2FltFahug%3D%3D, PID: 9389789
    • Gagnoux-Palacios L, Gache Y, Ortonne JP, Meneguzzi G (1997) Hemidesmosome assembly assessed by expression of a wild-type integrin beta 4 cDNA in junctional epidermolysis bullosa keratinocytes. Lab Invest 77:459–468
    • (1997) Lab Invest , vol.77 , pp. 459-468
    • Gagnoux-Palacios, L.1    Gache, Y.2    Ortonne, J.P.3    Meneguzzi, G.4
  • 48
    • 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
    • PID: 12791251
    • García-Alvarez B, Bobkov A, Sonnenberg A, de Pereda JM (2003) Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4. Structure 11:615–625
    • (2003) Structure , vol.11 , pp. 615-625
    • García-Alvarez, B.1    Bobkov, A.2    Sonnenberg, A.3    de Pereda, J.M.4
  • 50
    • 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
    • COI: 1:CAS:528:DyaK1MXmslCqsL8%3D, PID: 10525545
    • Geerts D, Fontao L, Nievers MG, Schaapveld RQ, Purkis PE, Wheeler GN, Lane EB, Leigh IM, Sonnenberg A (1999) Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding. J Cell Biol 147:417–434
    • (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
  • 51
    • 0029908558 scopus 로고    scopus 로고
    • Absence of integrin alpha 6 leads to epidermolysis bullosa and neonatal death in mice
    • COI: 1:STN:280:DyaK283lvFGksg%3D%3D, PID: 8673141
    • Georges-Labouesse E, Messaddeq N, Yehia G, Cadalbert L, Dierich A, Le Meur M (1996) Absence of integrin alpha 6 leads to epidermolysis bullosa and neonatal death in mice. Nat Genet 13:370–373
    • (1996) Nat Genet , vol.13 , pp. 370-373
    • Georges-Labouesse, E.1    Messaddeq, N.2    Yehia, G.3    Cadalbert, L.4    Dierich, A.5    Le Meur, M.6
  • 52
    • 63049113014 scopus 로고    scopus 로고
    • Phosphorylation of a novel site on the {beta}4 integrin at the trailing edge of migrating cells promotes hemidesmosome disassembly
    • COI: 1:CAS:528:DC%2BD1MXht1Sktbg%3D, PID: 19005215
    • Germain EC, Santos TM, Rabinovitz I (2009) Phosphorylation of a novel site on the {beta}4 integrin at the trailing edge of migrating cells promotes hemidesmosome disassembly. Mol Biol Cell 20:56–67
    • (2009) Mol Biol Cell , vol.20 , pp. 56-67
    • Germain, E.C.1    Santos, T.M.2    Rabinovitz, I.3
  • 53
    • 0036854284 scopus 로고    scopus 로고
    • Dynamics of the alpha6beta4 integrin in keratinocytes
    • COI: 1:CAS:528:DC%2BD38XpsVaitL8%3D, PID: 12429829
    • Geuijen CA, Sonnenberg A (2002) Dynamics of the alpha6beta4 integrin in keratinocytes. Mol Biol Cell 13:3845–3858
    • (2002) Mol Biol Cell , vol.13 , pp. 3845-3858
    • Geuijen, C.A.1    Sonnenberg, A.2
  • 54
    • 0026779495 scopus 로고
    • Proteolytic processing of endogenous and recombinant beta 4 integrin subunit
    • COI: 1:CAS:528:DyaK38XkvVOgtLs%3D, PID: 1500432
    • Giancotti FG, Stepp MA, Suzuki S, Engvall E, Ruoslahti E (1992) Proteolytic processing of endogenous and recombinant beta 4 integrin subunit. J Cell Biol 118:951–959
    • (1992) J Cell Biol , vol.118 , pp. 951-959
    • Giancotti, F.G.1    Stepp, M.A.2    Suzuki, S.3    Engvall, E.4    Ruoslahti, E.5
  • 55
    • 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
    • COI: 1:CAS:528:DyaK38XksVejsbs%3D, PID: 1390446
    • Green KJ, Virata ML, Elgart GW, Stanley JR, Parry DA (1992) 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 14:145–153
    • (1992) Int J Biol Macromol , vol.14 , pp. 145-153
    • Green, K.J.1    Virata, M.L.2    Elgart, G.W.3    Stanley, J.R.4    Parry, D.A.5
  • 57
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • COI: 1:CAS:528:DyaK2MXlt1Kisrs%3D, PID: 7736575
    • Guo L, Degenstein L, Dowling J, Yu QC, Wollmann R, Perman B, Fuchs E (1995) Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell 81:233–243
    • (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
  • 58
    • 70450237245 scopus 로고    scopus 로고
    • Collagen XVII
    • COI: 1:CAS:528:DC%2BC3cXhsVSgu7k%3D, PID: 19945617
    • Has C, Kern JS (2010) Collagen XVII. Dermatol Clin 28:61–66
    • (2010) Dermatol Clin , vol.28 , pp. 61-66
    • Has, C.1    Kern, J.S.2
  • 59
    • 0031568883 scopus 로고    scopus 로고
    • Assignment of SFA-1 (PETA-3), a member of the transmembrane 4 superfamily, to human chromosome 11p15.5 by fluorescence in situ hybridization
    • COI: 1:CAS:528:DyaK2sXhtlSksbs%3D, PID: 9070943
    • Hasegawa H, Kishimoto K, Yanagisawa K, Terasaki H, Shimadzu M, Fujita S (1997) Assignment of SFA-1 (PETA-3), a member of the transmembrane 4 superfamily, to human chromosome 11p15.5 by fluorescence in situ hybridization. Genomics 40:193–196
    • (1997) Genomics , vol.40 , pp. 193-196
    • Hasegawa, H.1    Kishimoto, K.2    Yanagisawa, K.3    Terasaki, H.4    Shimadzu, M.5    Fujita, S.6
  • 60
    • 0023126564 scopus 로고
    • Plectin and IFAP-300 K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin
    • COI: 1:CAS:528:DyaL2sXpvVejsA%3D%3D, PID: 3027087
    • Herrmann H, Wiche G (1987) Plectin and IFAP-300 K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin. J Biol Chem 262:1320–1325
    • (1987) J Biol Chem , vol.262 , pp. 1320-1325
    • Herrmann, H.1    Wiche, G.2
  • 61
    • 0026577999 scopus 로고
    • Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes
    • COI: 1:CAS:528:DyaK38Xks1Ois70%3D, PID: 1541639
    • Hieda Y, Nishizawa Y, Uematsu J, Owaribe K (1992) Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes. J Cell Biol 116:1497–1506
    • (1992) J Cell Biol , vol.116 , pp. 1497-1506
    • Hieda, Y.1    Nishizawa, Y.2    Uematsu, J.3    Owaribe, K.4
  • 62
    • 0029890331 scopus 로고    scopus 로고
    • Demonstration of the molecular shape of BP180, a 180-kDa bullous pemphigoid antigen and its potential for trimer formation
    • COI: 1:CAS:528:DyaK28XjsVOjsrk%3D, PID: 8662839
    • Hirako Y, Usukura J, Nishizawa Y, Owaribe K (1996) Demonstration of the molecular shape of BP180, a 180-kDa bullous pemphigoid antigen and its potential for trimer formation. J Biol Chem 271:13739–13745
    • (1996) J Biol Chem , vol.271 , pp. 13739-13745
    • Hirako, Y.1    Usukura, J.2    Nishizawa, Y.3    Owaribe, K.4
  • 63
    • 2642513682 scopus 로고    scopus 로고
    • Extracellular cleavage of bullous pemphigoid antigen 180/type XVII collagen and its involvement in hemidesmosomal disassembly
    • COI: 1:CAS:528:DC%2BD3sXjsVamtrw%3D, PID: 12761182
    • Hirako Y, Yoshino K, Zillikens D, Owaribe K (2003) Extracellular cleavage of bullous pemphigoid antigen 180/type XVII collagen and its involvement in hemidesmosomal disassembly. J Biochem 133:197–206
    • (2003) J Biochem , vol.133 , pp. 197-206
    • Hirako, Y.1    Yoshino, K.2    Zillikens, D.3    Owaribe, K.4
  • 64
    • 0025117579 scopus 로고
    • Cloning and sequence analysis of beta-4 cDNA: an integrin subunit that contains a unique 118 kd cytoplasmic domain
    • COI: 1:CAS:528:DyaK3cXksFensLg%3D, PID: 2311578
    • Hogervorst F, Kuikman I, von dem Borne AE, Sonnenberg A (1990) Cloning and sequence analysis of beta-4 cDNA: an integrin subunit that contains a unique 118 kd cytoplasmic domain. EMBO J 9:765–770
    • (1990) EMBO J , vol.9 , pp. 765-770
    • Hogervorst, F.1    Kuikman, I.2    von dem Borne, A.E.3    Sonnenberg, A.4
  • 65
    • 0025908468 scopus 로고
    • Molecular cloning of the human alpha 6 integrin subunit. Alternative splicing of alpha 6 mRNA and chromosomal localization of the alpha 6 and beta 4 genes
    • COI: 1:CAS:528:DyaK38XhsVGju78%3D, PID: 2070796
    • Hogervorst F, Kuikman I, van Kessel AG, Sonnenberg A (1991) Molecular cloning of the human alpha 6 integrin subunit. Alternative splicing of alpha 6 mRNA and chromosomal localization of the alpha 6 and beta 4 genes. Eur J Biochem 199:425–433
    • (1991) Eur J Biochem , vol.199 , pp. 425-433
    • Hogervorst, F.1    Kuikman, I.2    van Kessel, A.G.3    Sonnenberg, A.4
  • 66
    • 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
    • COI: 1:CAS:528:DC%2BD3cXosFyisQ%3D%3D, PID: 10637308
    • Hopkinson SB, Jones JC (2000) 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 11:277–286
    • (2000) Mol Biol Cell , vol.11 , pp. 277-286
    • Hopkinson, S.B.1    Jones, J.C.2
  • 67
    • 0029005210 scopus 로고
    • Molecular genetic studies of a human epidermal autoantigen (the 180-kD bullous pemphigoid antigen/BP180): identification of functionally important sequences within the BP180 molecule and evidence for an interaction between BP180 and alpha 6 integrin
    • COI: 1:CAS:528:DyaK2MXmsFWhu74%3D, PID: 7790367
    • Hopkinson SB, Baker SE, Jones JC (1995) Molecular genetic studies of a human epidermal autoantigen (the 180-kD bullous pemphigoid antigen/BP180): identification of functionally important sequences within the BP180 molecule and evidence for an interaction between BP180 and alpha 6 integrin. J Cell Biol 130:117–125
    • (1995) J Cell Biol , vol.130 , pp. 117-125
    • Hopkinson, S.B.1    Baker, S.E.2    Jones, J.C.3
  • 68
    • 0032447962 scopus 로고    scopus 로고
    • Interaction of BP180 (type XVII collagen) and alpha6 integrin is necessary for stabilization of hemidesmosome structure
    • COI: 1:CAS:528:DyaK1cXnvFyisbk%3D, PID: 9856810
    • Hopkinson SB, Findlay K, deHart GW, Jones JC (1998) Interaction of BP180 (type XVII collagen) and alpha6 integrin is necessary for stabilization of hemidesmosome structure. J Invest Dermatol 111:1015–1022
    • (1998) J Invest Dermatol , vol.111 , pp. 1015-1022
    • Hopkinson, S.B.1    Findlay, K.2    deHart, G.W.3    Jones, J.C.4
  • 71
    • 0035197616 scopus 로고    scopus 로고
    • Plectin repeats and modules: strategic cysteines and their presumed impact on cytolinker functions
    • COI: 1:CAS:528:DC%2BD38XksFyjtQ%3D%3D, PID: 11746222
    • Janda L, Damborský J, Rezniczek GA, Wiche G (2001) Plectin repeats and modules: strategic cysteines and their presumed impact on cytolinker functions. Bioessays 23:1064–1069
    • (2001) Bioessays , vol.23 , pp. 1064-1069
    • Janda, L.1    Damborský, J.2    Rezniczek, G.A.3    Wiche, G.4
  • 72
    • 33644522372 scopus 로고    scopus 로고
    • New roles for integrins in squamous-cell carcinoma
    • COI: 1:CAS:528:DC%2BD28Xhsleltrc%3D, PID: 16498442
    • Janes SM, Watt FM (2006) New roles for integrins in squamous-cell carcinoma. Nat Rev Cancer 6:175–183
    • (2006) Nat Rev Cancer , vol.6 , pp. 175-183
    • Janes, S.M.1    Watt, F.M.2
  • 73
    • 0033050072 scopus 로고    scopus 로고
    • Hereditary skin diseases of hemidesmosomes
    • COI: 1:CAS:528:DyaK1MXjtFWqt7o%3D, PID: 10379703
    • Jonkman MF (1999) Hereditary skin diseases of hemidesmosomes. J Dermatol Sci 20:103–121
    • (1999) J Dermatol Sci , vol.20 , pp. 103-121
    • Jonkman, M.F.1
  • 74
    • 84930271915 scopus 로고    scopus 로고
    • Recessive Epidermolysis Bullosa Simplex due to plectin 1a deficiency causes only skin blisters
    • abstract 534
    • Jonkman MF, Lemmink HH (2012) Recessive Epidermolysis Bullosa Simplex due to plectin 1a deficiency causes only skin blisters. J Invest Dermatol 132:S94, abstract 534
    • (2012) J Invest Dermatol , vol.132 , pp. 94
    • Jonkman, M.F.1    Lemmink, H.H.2
  • 75
    • 2542428252 scopus 로고    scopus 로고
    • Co-assembly of envoplakin and periplakin into oligomers and Ca(2+)-dependent vesicle binding: implications for cornified cell
    • COI: 1:CAS:528:DC%2BD2cXjvF2ru7w%3D, PID: 15033990
    • Kalinin AE, Idler WW, Marekov LN, McPhie P, Bowers B, Steinert PM, Steven AC (2004) Co-assembly of envoplakin and periplakin into oligomers and Ca(2+)-dependent vesicle binding: implications for cornified cell. J Biol Chem 279:22773–22780
    • (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
  • 76
    • 4944239350 scopus 로고    scopus 로고
    • CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin
    • PID: 15265795
    • Karamatic Crew V, Burton N, Kagan A, Green CA, Levene C, Flinter F, Brady RL, Daniels G, Anstee DJ (2004) CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin. Blood 104:2217–2223
    • (2004) Blood , vol.104 , pp. 2217-2223
    • Karamatic Crew, V.1    Burton, N.2    Kagan, A.3    Green, C.A.4    Levene, C.5    Flinter, F.6    Brady, R.L.7    Daniels, G.8    Anstee, D.J.9
  • 77
    • 84866563101 scopus 로고    scopus 로고
    • The calcium/calcineurin pathway promotes hemidesmosome stability through inhibition of beta4 integrin phosphorylation
    • COI: 1:CAS:528:DC%2BC38XhtlyqsrrJ, PID: 22865863
    • Kashyap T, Rabinovitz I (2012) The calcium/calcineurin pathway promotes hemidesmosome stability through inhibition of beta4 integrin phosphorylation. J Biol Chem 287:32440–32449
    • (2012) J Biol Chem , vol.287 , pp. 32440-32449
    • Kashyap, T.1    Rabinovitz, I.2
  • 78
    • 80053355409 scopus 로고    scopus 로고
    • Role of beta4 integrin phosphorylation in human invasive squamous cell carcinoma: regulation of hemidesmosome stability modulates cell migration
    • COI: 1:CAS:528:DC%2BC3MXht1Ghu7zP, PID: 21769085
    • Kashyap T, Germain E, Roche M, Lyle S, Rabinovitz I (2011) Role of beta4 integrin phosphorylation in human invasive squamous cell carcinoma: regulation of hemidesmosome stability modulates cell migration. Lab Invest 91:1414–1426
    • (2011) Lab Invest , vol.91 , pp. 1414-1426
    • Kashyap, T.1    Germain, E.2    Roche, M.3    Lyle, S.4    Rabinovitz, I.5
  • 79
    • 0037144837 scopus 로고    scopus 로고
    • An extracellular site on tetraspanin CD151 determines alpha 3 and alpha 6 integrin-dependent cellular morphology
    • COI: 1:CAS:528:DC%2BD38Xns1equrs%3D, PID: 12356873
    • Kazarov AR, Yang X, Stipp CS, Sehgal B, Hemler ME (2002) An extracellular site on tetraspanin CD151 determines alpha 3 and alpha 6 integrin-dependent cellular morphology. J Cell Biol 158:1299–1309
    • (2002) J Cell Biol , vol.158 , pp. 1299-1309
    • Kazarov, A.R.1    Yang, X.2    Stipp, C.S.3    Sehgal, B.4    Hemler, M.E.5
  • 80
    • 0013865428 scopus 로고
    • Fine structure of desmosomes, hemidesmosomes, and an adepidermal globular layer in developing newt epidermis
    • COI: 1:STN:280:DyaF28%2FmslOlsw%3D%3D, PID: 5901500
    • Kelly DE (1966) Fine structure of desmosomes, hemidesmosomes, and an adepidermal globular layer in developing newt epidermis. J Cell Biol 28:51–72
    • (1966) J Cell Biol , vol.28 , pp. 51-72
    • Kelly, D.E.1
  • 81
    • 79960296684 scopus 로고    scopus 로고
    • Molecular mechanisms of phenotypic variability in junctional epidermolysis bullosa
    • COI: 1:CAS:528:DC%2BC3MXhtVaksLjL, PID: 21357940
    • Kiritsi D, Kern JS, Schumann H, Kohlhase J, Has C, Bruckner-Tuderman L (2011) Molecular mechanisms of phenotypic variability in junctional epidermolysis bullosa. J Med Genet 48:450–457
    • (2011) J Med Genet , vol.48 , pp. 450-457
    • Kiritsi, D.1    Kern, J.S.2    Schumann, H.3    Kohlhase, J.4    Has, C.5    Bruckner-Tuderman, L.6
  • 82
    • 84872191021 scopus 로고    scopus 로고
    • Laminin 332 in junctional epidermolysis bullosa
    • PID: 23076207
    • Kiritsi D, Has C, Bruckner-Tuderman L (2013) Laminin 332 in junctional epidermolysis bullosa. Cell Adh Migr 7:135–141
    • (2013) Cell Adh Migr , vol.7 , pp. 135-141
    • Kiritsi, D.1    Has, C.2    Bruckner-Tuderman, L.3
  • 83
    • 0026497939 scopus 로고
    • Phorbol ester- and calcium-induced reorganization of 180-kDa bullous pemphigoid antigen on the ventral surface of cultured human keratinocytes as studied by immunofluorescence and immunoelectron microscopy
    • COI: 1:CAS:528:DyaK3sXhvF2msw%3D%3D, PID: 1426040
    • Kitajima Y, Owaribe K, Nishizawa Y, Jokura Y, Yaoita H (1992) Phorbol ester- and calcium-induced reorganization of 180-kDa bullous pemphigoid antigen on the ventral surface of cultured human keratinocytes as studied by immunofluorescence and immunoelectron microscopy. Exp Cell Res 203:17–24
    • (1992) Exp Cell Res , vol.203 , pp. 17-24
    • Kitajima, Y.1    Owaribe, K.2    Nishizawa, Y.3    Jokura, Y.4    Yaoita, H.5
  • 84
    • 0032857374 scopus 로고    scopus 로고
    • Transmembrane signaling for adhesive regulation of desmosomes and hemidesmosomes, and for cell-cell datachment induced by pemphigus IgG in cultured keratinocytes: involvement of protein kinase C
    • COI: 1:CAS:528:DyaK1MXntFSrs7k%3D, PID: 10536988
    • Kitajima Y, Aoyama Y, Seishima M (1999) Transmembrane signaling for adhesive regulation of desmosomes and hemidesmosomes, and for cell-cell datachment induced by pemphigus IgG in cultured keratinocytes: involvement of protein kinase C. J Investig Dermatol Symp Proc 4:137–144
    • (1999) J Investig Dermatol Symp Proc , vol.4 , pp. 137-144
    • Kitajima, Y.1    Aoyama, Y.2    Seishima, M.3
  • 86
    • 67650561186 scopus 로고    scopus 로고
    • Plectin isoform-dependent regulation of keratin-integrin alpha6beta4 anchorage via Ca2+/calmodulin
    • COI: 1:CAS:528:DC%2BD1MXnslegu70%3D, PID: 19419971
    • Kostan J, Gregor M, Walko G, Wiche G (2009) Plectin isoform-dependent regulation of keratin-integrin alpha6beta4 anchorage via Ca2+/calmodulin. J Biol Chem 284:18525–18536
    • (2009) J Biol Chem , vol.284 , pp. 18525-18536
    • Kostan, J.1    Gregor, M.2    Walko, G.3    Wiche, G.4
  • 87
    • 0035670672 scopus 로고    scopus 로고
    • Two different mutations in the cytoplasmic domain of the integrin beta 4 subunit in nonlethal forms of epidermolysis bullosa prevent interaction of beta 4 with plectin
    • COI: 1:CAS:528:DC%2BD38XjtVagsA%3D%3D, PID: 11886501
    • Koster J, Kuikman I, Kreft M, Sonnenberg A (2001) Two different mutations in the cytoplasmic domain of the integrin beta 4 subunit in nonlethal forms of epidermolysis bullosa prevent interaction of beta 4 with plectin. J Invest Dermatol 117:1405–1411
    • (2001) J Invest Dermatol , vol.117 , pp. 1405-1411
    • Koster, J.1    Kuikman, I.2    Kreft, M.3    Sonnenberg, A.4
  • 88
    • 0037439896 scopus 로고    scopus 로고
    • Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly
    • COI: 1:CAS:528:DC%2BD3sXpvVKmtg%3D%3D, PID: 12482924
    • Koster J, Geerts D, Favre B, Borradori L, Sonnenberg A (2003) Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly. J Cell Sci 116:387–399
    • (2003) J Cell Sci , vol.116 , pp. 387-399
    • Koster, J.1    Geerts, D.2    Favre, B.3    Borradori, L.4    Sonnenberg, A.5
  • 89
    • 1542344031 scopus 로고    scopus 로고
    • Role of binding of plectin to the integrin beta4 subunit in the assembly of hemidesmosomes
    • COI: 1:CAS:528:DC%2BD2cXitlGgsrs%3D, PID: 14668477
    • Koster J, van Wilpe S, Kuikman I, Litjens SH, Sonnenberg A (2004) Role of binding of plectin to the integrin beta4 subunit in the assembly of hemidesmosomes. Mol Biol Cell 15:1211–1223
    • (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
  • 90
    • 0026327822 scopus 로고
    • Genomic organization of collagenous domains and chromosomal assignment of human 180-kDa bullous pemphigoid antigen-2, a novel collagen of stratified squamous epithelium
    • COI: 1:CAS:528:DyaK38XltVGntLw%3D, PID: 1748679
    • Li KH, Sawamura D, Giudice GJ, Diaz LA, Mattei MG, Chu ML, Uitto J (1991) Genomic organization of collagenous domains and chromosomal assignment of human 180-kDa bullous pemphigoid antigen-2, a novel collagen of stratified squamous epithelium. J Biol Chem 266:24064–24069
    • (1991) J Biol Chem , vol.266 , pp. 24064-24069
    • Li, K.H.1    Sawamura, D.2    Giudice, G.J.3    Diaz, L.A.4    Mattei, M.G.5    Chu, M.L.6    Uitto, J.7
  • 91
    • 0027477628 scopus 로고
    • Cloning of type XVII collagen. Complementary and genomic DNA sequences of mouse 180-kilodalton bullous pemphigoid antigen (BPAG2) predict an interrupted collagenous domain, a transmembrane segment, and unusual features in the 5'-end of the gene and the 3'-untranslated region of the mRNA
    • COI: 1:CAS:528:DyaK3sXkt1Khs7g%3D, PID: 8473327
    • Li K, Tamai K, Tan EM, Uitto J (1993) Cloning of type XVII collagen. Complementary and genomic DNA sequences of mouse 180-kilodalton bullous pemphigoid antigen (BPAG2) predict an interrupted collagenous domain, a transmembrane segment, and unusual features in the 5'-end of the gene and the 3'-untranslated region of the mRNA. J Biol Chem 268:8825–8834
    • (1993) J Biol Chem , vol.268 , pp. 8825-8834
    • Li, K.1    Tamai, K.2    Tan, E.M.3    Uitto, J.4
  • 93
    • 27644496163 scopus 로고    scopus 로고
    • Mobilization and activation of a signaling competent alpha6beta4integrin underlies its contribution to carcinoma progression
    • COI: 1:CAS:528:DC%2BD2MXhtFKht73P, PID: 16258729
    • Lipscomb EA, Mercurio AM (2005) Mobilization and activation of a signaling competent alpha6beta4integrin underlies its contribution to carcinoma progression. Cancer Metastasis Rev 24:413–423
    • (2005) Cancer Metastasis Rev , vol.24 , pp. 413-423
    • Lipscomb, E.A.1    Mercurio, A.M.2
  • 94
    • 33745947286 scopus 로고    scopus 로고
    • Current insights into the formation and breakdown of hemidesmosomes
    • COI: 1:CAS:528:DC%2BD28XntFWrtLo%3D, PID: 16757171
    • Litjens SH, de Pereda JM, Sonnenberg A (2006) Current insights into the formation and breakdown of hemidesmosomes. Trends Cell Biol 16:376–383
    • (2006) Trends Cell Biol , vol.16 , pp. 376-383
    • Litjens, S.H.1    de Pereda, J.M.2    Sonnenberg, A.3
  • 95
    • 0029961661 scopus 로고    scopus 로고
    • Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24)
    • COI: 1:CAS:528:DyaK28XivVKqsb8%3D, PID: 8633055
    • Liu CG, Maercker C, Castañón MJ, Hauptmann R, Wiche G (1996) Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24). Proc Natl Acad Sci U S A 93:4278–4283
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 4278-4283
    • Liu, C.G.1    Maercker, C.2    Castañón, M.J.3    Hauptmann, R.4    Wiche, G.5
  • 97
    • 0030947554 scopus 로고    scopus 로고
    • The tetraspanin superfamily: molecular facilitators
    • COI: 1:CAS:528:DyaK2sXjvFahsLY%3D, PID: 9194523
    • Maecker HT, Todd SC, Levy S (1997) The tetraspanin superfamily: molecular facilitators. FASEB J 11:428–442
    • (1997) FASEB J , vol.11 , pp. 428-442
    • Maecker, H.T.1    Todd, S.C.2    Levy, S.3
  • 98
    • 0029115343 scopus 로고
    • Signal transduction by the alpha 6 beta 4 integrin: distinct beta 4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes
    • COI: 1:CAS:528:DyaK2MXovVektrs%3D, PID: 7556090
    • Mainiero F, Pepe A, Wary KK, Spinardi L, Mohammadi M, Schlessinger J, Giancotti FG (1995) Signal transduction by the alpha 6 beta 4 integrin: distinct beta 4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes. EMBO J 14:4470–4481
    • (1995) EMBO J , vol.14 , pp. 4470-4481
    • Mainiero, F.1    Pepe, A.2    Wary, K.K.3    Spinardi, L.4    Mohammadi, M.5    Schlessinger, J.6    Giancotti, F.G.7
  • 99
    • 0029666451 scopus 로고    scopus 로고
    • The intracellular functions of alpha6beta4 integrin are regulated by EGF
    • COI: 1:CAS:528:DyaK28XktVGjs7k%3D, PID: 8698818
    • Mainiero F, Pepe A, Yeon M, Ren Y, Giancotti FG (1996) The intracellular functions of alpha6beta4 integrin are regulated by EGF. J Cell Biol 134:241–253
    • (1996) J Cell Biol , vol.134 , pp. 241-253
    • Mainiero, F.1    Pepe, A.2    Yeon, M.3    Ren, Y.4    Giancotti, F.G.5
  • 100
    • 50849108513 scopus 로고    scopus 로고
    • Regulation of hemidesmosome disassembly by growth factor receptors
    • COI: 1:CAS:528:DC%2BD1cXhtVyks7vI, PID: 18583123
    • Margadant C, Frijns E, Wilhelmsen K, Sonnenberg A (2008) Regulation of hemidesmosome disassembly by growth factor receptors. Curr Opin Cell Biol 20:589–596
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 589-596
    • Margadant, C.1    Frijns, E.2    Wilhelmsen, K.3    Sonnenberg, A.4
  • 101
    • 78649867535 scopus 로고    scopus 로고
    • Unique and redundant functions of integrins in the epidermis
    • COI: 1:CAS:528:DC%2BC3cXhsVWqu73P, PID: 20624931
    • Margadant C, Charafeddine RA, Sonnenberg A (2010) Unique and redundant functions of integrins in the epidermis. FASEB J 24:4133–4152
    • (2010) FASEB J , vol.24 , pp. 4133-4152
    • Margadant, C.1    Charafeddine, R.A.2    Sonnenberg, A.3
  • 102
    • 0026640262 scopus 로고
    • The anchoring filament protein kalinin is synthesized and secreted as a high molecular weight precursor
    • COI: 1:CAS:528:DyaK38XkvVOgtrk%3D, PID: 1517226
    • Marinkovich MP, Lunstrum GP, Burgeson RE (1992) The anchoring filament protein kalinin is synthesized and secreted as a high molecular weight precursor. J Biol Chem 267:17900–17906
    • (1992) J Biol Chem , vol.267 , pp. 17900-17906
    • Marinkovich, M.P.1    Lunstrum, G.P.2    Burgeson, R.E.3
  • 103
    • 84889294341 scopus 로고    scopus 로고
    • EGF-R signaling through Fyn kinase disrupts the function of integrin alpha6beta4 at hemidesmosomes: role in epithelial cell migration and carcinoma invasion
    • COI: 1:CAS:528:DC%2BD3MXotVSrtr0%3D, PID: 11684709
    • Mariotti A, Kedeshian PA, Dans M, Curatola AM, Gagnoux-Palacios L, Giancotti FG (2001) EGF-R signaling through Fyn kinase disrupts the function of integrin alpha6beta4 at hemidesmosomes: role in epithelial cell migration and carcinoma invasion. J Cell Biol 155:447–458
    • (2001) J Cell Biol , vol.155 , pp. 447-458
    • Mariotti, A.1    Kedeshian, P.A.2    Dans, M.3    Curatola, A.M.4    Gagnoux-Palacios, L.5    Giancotti, F.G.6
  • 105
    • 0030798040 scopus 로고    scopus 로고
    • The extracellular domain of BPAG2 localizes to anchoring filaments and its carboxyl terminus extends to the lamina densa of normal human epidermal basement membrane
    • COI: 1:CAS:528:DyaK2sXltlKjuro%3D, PID: 9242508
    • Masunaga T, Shimizu H, Yee C, Borradori L, Lazarova Z, Nishikawa T, Yancey KB (1997) The extracellular domain of BPAG2 localizes to anchoring filaments and its carboxyl terminus extends to the lamina densa of normal human epidermal basement membrane. J Invest Dermatol 109:200–206
    • (1997) J Invest Dermatol , vol.109 , pp. 200-206
    • Masunaga, T.1    Shimizu, H.2    Yee, C.3    Borradori, L.4    Lazarova, Z.5    Nishikawa, T.6    Yancey, K.B.7
  • 106
    • 0031930179 scopus 로고    scopus 로고
    • Hemidesmosomes show abnormal association with the keratin filament network in junctional forms of epidermolysis bullosa
    • COI: 1:STN:280:DyaK1c7hslWisw%3D%3D, PID: 9457907
    • McMillan JR, McGrath JA, Tidman MJ, Eady RA (1998) Hemidesmosomes show abnormal association with the keratin filament network in junctional forms of epidermolysis bullosa. J Invest Dermatol 110:132–137
    • (1998) J Invest Dermatol , vol.110 , pp. 132-137
    • McMillan, J.R.1    McGrath, J.A.2    Tidman, M.J.3    Eady, R.A.4
  • 107
    • 0037406396 scopus 로고    scopus 로고
    • Epidermal basement membrane zone components: ultrastructural distribution and molecular interactions
    • COI: 1:CAS:528:DC%2BD3sXjtlWktr4%3D, PID: 12727020
    • McMillan JR, Akiyama M, Shimizu H (2003) Epidermal basement membrane zone components: ultrastructural distribution and molecular interactions. J Dermatol Sci 31:169–177
    • (2003) J Dermatol Sci , vol.31 , pp. 169-177
    • McMillan, J.R.1    Akiyama, M.2    Shimizu, H.3
  • 109
    • 0141887524 scopus 로고    scopus 로고
    • Targeted inactivation of murine laminin gamma2-chain gene recapitulates human junctional epidermolysis bullosa
    • COI: 1:CAS:528:DC%2BD3sXotFOjtbw%3D, PID: 14632187
    • Meng X, Klement JF, Leperi DA, Birk DE, Sasaki T, Timpl R, Uitto J, Pulkkinen L (2003) Targeted inactivation of murine laminin gamma2-chain gene recapitulates human junctional epidermolysis bullosa. J Invest Dermatol 121:720–731
    • (2003) J Invest Dermatol , vol.121 , pp. 720-731
    • Meng, X.1    Klement, J.F.2    Leperi, D.A.3    Birk, D.E.4    Sasaki, T.5    Timpl, R.6    Uitto, J.7    Pulkkinen, L.8
  • 110
    • 35648976145 scopus 로고    scopus 로고
    • Intrinsic signaling functions of the beta4 integrin intracellular domain
    • COI: 1:CAS:528:DC%2BD2sXhtFagurzF, PID: 17711859
    • Merdek KD, Yang X, Taglienti CA, Shaw LM, Mercurio AM (2007) Intrinsic signaling functions of the beta4 integrin intracellular domain. J Biol Chem 282:30322–30330
    • (2007) J Biol Chem , vol.282 , pp. 30322-30330
    • Merdek, K.D.1    Yang, X.2    Taglienti, C.A.3    Shaw, L.M.4    Mercurio, A.M.5
  • 114
    • 0029990621 scopus 로고    scopus 로고
    • Deficiency of the integrin beta 4 subunit in junctional epidermolysis bullosa with pyloric atresia: consequences for hemidesmosome formation and adhesion properties
    • COI: 1:CAS:528:DyaK28XksFCksLw%3D, PID: 8832392
    • Niessen CM, van der Raaij-Helmer MH, Hulsman EH, van der Neut R, Jonkman MF, Sonnenberg A (1996) Deficiency of the integrin beta 4 subunit in junctional epidermolysis bullosa with pyloric atresia: consequences for hemidesmosome formation and adhesion properties. J Cell Sci 109:1695–1706
    • (1996) J Cell Sci , vol.109 , pp. 1695-1706
    • Niessen, C.M.1    van der Raaij-Helmer, M.H.2    Hulsman, E.H.3    van der Neut, R.4    Jonkman, M.F.5    Sonnenberg, A.6
  • 115
    • 10144233447 scopus 로고    scopus 로고
    • Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplas— mic plectin-vimentin network junctions
    • Nikolic B, Mac Nulty E, Mir B, Wiche G (1996) Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplas— mic plectin-vimentin network junctions. J Cell Biol 134:1455–1467
    • (1996) J Cell Biol , vol.134 , pp. 1455-1467
    • Nikolic, B.1    Mac Nulty, E.2    Mir, B.3    Wiche, G.4
  • 117
    • 80052475666 scopus 로고    scopus 로고
    • Bruckner-Tuderman L(2011) Dynamic interactions of epidermal collagen XVII with theextracellular matrix. Laminin 332 as a major binding partner
    • Nishie W, Kiritsi D, Nyström A, Hofmann SC, Bruckner-Tuderman L(2011) Dynamic interactions of epidermal collagen XVII with theextracellular matrix. Laminin 332 as a major binding partner. AmJ Pathol 179:829–837
    • AmJ Pathol , vol.179 , pp. 829-837
    • Nishie, W.1    Kiritsi, D.2    Nyström, A.3    Hofmann, S.C.4
  • 119
    • 0033395566 scopus 로고    scopus 로고
    • Identification of the hemidesmosomal 500 kDa protein (HD1) as plectin
    • COI: 1:CAS:528:DC%2BD3cXmt1aksw%3D%3D, PID: 10578067
    • Okumura M, Uematsu J, Hirako Y, Nishizawa Y, Shimizu H, Kido N, Owaribe K (1999) Identification of the hemidesmosomal 500 kDa protein (HD1) as plectin. J Biochem 126:1144–1150
    • (1999) J Biochem , vol.126 , pp. 1144-1150
    • Okumura, M.1    Uematsu, J.2    Hirako, Y.3    Nishizawa, Y.4    Shimizu, H.5    Kido, N.6    Owaribe, K.7
  • 121
    • 33747163300 scopus 로고    scopus 로고
    • Plectin-controlled keratin cytoarchitecture affects MAP kinases involved in cellular stress response and migration
    • COI: 1:CAS:528:DC%2BD28XosVKgt7Y%3D, PID: 16908671
    • Osmanagic-Myers S, Gregor M, Walko G, Burgstaller G, Reipert S, Wiche G (2006) Plectin-controlled keratin cytoarchitecture affects MAP kinases involved in cellular stress response and migration. J Cell Biol 174:557–568
    • (2006) J Cell Biol , vol.174 , pp. 557-568
    • Osmanagic-Myers, S.1    Gregor, M.2    Walko, G.3    Burgstaller, G.4    Reipert, S.5    Wiche, G.6
  • 122
    • 0025615956 scopus 로고
    • The hemidesmosomal plaque. I. Characterization of a major constituent protein as a differentiation marker for certain forms of epithelia
    • COI: 1:CAS:528:DyaK3MXhvValsL4%3D, PID: 2090522
    • Owaribe K, Kartenbeck J, Stumpp S, Magin TM, Krieg T, Diaz LA, Franke WW (1990) The hemidesmosomal plaque. I. Characterization of a major constituent protein as a differentiation marker for certain forms of epithelia. Differentiation 45:207–220
    • (1990) Differentiation , vol.45 , pp. 207-220
    • Owaribe, K.1    Kartenbeck, J.2    Stumpp, S.3    Magin, T.M.4    Krieg, T.5    Diaz, L.A.6    Franke, W.W.7
  • 124
    • 0028283214 scopus 로고
    • Proteolytic cleavage of the integrin beta 4 subunit
    • COI: 1:STN:280:DyaK2c3ivFWltA%3D%3D, PID: 8174638
    • Potts AJ, Croall DE, Hemler ME (1994) Proteolytic cleavage of the integrin beta 4 subunit. Exp Cell Res 212:2–9
    • (1994) Exp Cell Res , vol.212 , pp. 2-9
    • Potts, A.J.1    Croall, D.E.2    Hemler, M.E.3
  • 125
    • 0032962217 scopus 로고    scopus 로고
    • Mutation analysis and molecular genetics of epidermolysis bullosa
    • COI: 1:CAS:528:DyaK1MXjsV2it7s%3D, PID: 10367729
    • Pulkkinen L, Uitto J (1999) Mutation analysis and molecular genetics of epidermolysis bullosa. Matrix Biol 18:29–42
    • (1999) Matrix Biol , vol.18 , pp. 29-42
    • Pulkkinen, L.1    Uitto, J.2
  • 126
    • 2942628076 scopus 로고    scopus 로고
    • Protein kinase C-alpha phosphorylation of specific serines in the connecting segment of the beta 4 integrin regulates the dynamics of type II hemidesmosomes
    • COI: 1:CAS:528:DC%2BD2cXjvFChtLo%3D, PID: 15121854
    • Rabinovitz I, Tsomo L, Mercurio AM (2004) Protein kinase C-alpha phosphorylation of specific serines in the connecting segment of the beta 4 integrin regulates the dynamics of type II hemidesmosomes. Mol Cell Biol 24:4351–4360
    • (2004) Mol Cell Biol , vol.24 , pp. 4351-4360
    • Rabinovitz, I.1    Tsomo, L.2    Mercurio, A.M.3
  • 127
    • 16844373398 scopus 로고    scopus 로고
    • Keratinocytes display normal proliferation, survival and differentiation in conditional beta4-integrin knockout mice
    • COI: 1:CAS:528:DC%2BD2MXjs12mtrc%3D, PID: 15731010
    • Raymond K, Kreft M, Janssen H, Calafat J, Sonnenberg A (2005) Keratinocytes display normal proliferation, survival and differentiation in conditional beta4-integrin knockout mice. J Cell Sci 118:1045–1060
    • (2005) J Cell Sci , vol.118 , pp. 1045-1060
    • Raymond, K.1    Kreft, M.2    Janssen, H.3    Calafat, J.4    Sonnenberg, A.5
  • 128
    • 4043090575 scopus 로고    scopus 로고
    • High-pressure cryoimmobilization of murine skin reveals novel structural features and prevents extraction artifacts
    • PID: 15217362
    • Reipert S, Fischer I, Wiche G (2004) High-pressure cryoimmobilization of murine skin reveals novel structural features and prevents extraction artifacts. Exp Dermatol 13:419–425
    • (2004) Exp Dermatol , vol.13 , pp. 419-425
    • Reipert, S.1    Fischer, I.2    Wiche, G.3
  • 130
    • 0032489678 scopus 로고    scopus 로고
    • Linking integrin alpha6beta4-based cell adhesion to the intermediate filament cytoskeleton: direct interaction between the beta4 subunit and plectin at multiple molecular sites
    • COI: 1:CAS:528:DyaK1cXis1ejs7s%3D, PID: 9531560
    • Rezniczek GA, de Pereda JM, Reipert S, Wiche G (1998) Linking integrin alpha6beta4-based cell adhesion to the intermediate filament cytoskeleton: direct interaction between the beta4 subunit and plectin at multiple molecular sites. J Cell Biol 141:209–225
    • (1998) J Cell Biol , vol.141 , pp. 209-225
    • Rezniczek, G.A.1    de Pereda, J.M.2    Reipert, S.3    Wiche, G.4
  • 131
    • 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
    • COI: 1:CAS:528:DC%2BD3sXptVSntLs%3D, PID: 14559777
    • Rezniczek GA, Abrahamsberg C, Fuchs P, Spazierer D, Wiche G (2003) Plectin 5'-transcript diversity: short alternative sequences determine stability of gene products, initiation of translation and subcellular localization of isoforms. Hum Mol Genet 12:3181–94
    • (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
  • 132
    • 70450263531 scopus 로고    scopus 로고
    • Plectin gene defects lead to various forms of epidermolysis bullosa simplex
    • COI: 1:CAS:528:DC%2BC3cXhsVSgu7o%3D, PID: 19945614
    • Rezniczek GA, Walko G, Wiche G (2010) Plectin gene defects lead to various forms of epidermolysis bullosa simplex. Dermatol Clin 28:33–41
    • (2010) Dermatol Clin , vol.28 , pp. 33-41
    • Rezniczek, G.A.1    Walko, G.2    Wiche, G.3
  • 133
    • 0028294842 scopus 로고
    • Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other epithelial cells and has a different requirement for integrin receptors
    • COI: 1:CAS:528:DyaK2cXitFersb4%3D, PID: 8138572
    • Rousselle P, Aumailley M (1994) Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other epithelial cells and has a different requirement for integrin receptors. J Cell Biol 125:205–214
    • (1994) J Cell Biol , vol.125 , pp. 205-214
    • Rousselle, P.1    Aumailley, M.2
  • 134
    • 84872188147 scopus 로고    scopus 로고
    • Laminin 332 processing impacts cellular behavior
    • PID: 23263634
    • Rousselle P, Beck K (2013) Laminin 332 processing impacts cellular behavior. Cell Adh Migr 7:122–134
    • (2013) Cell Adh Migr , vol.7 , pp. 122-134
    • Rousselle, P.1    Beck, K.2
  • 136
    • 0033553883 scopus 로고    scopus 로고
    • Targeted disruption of the LAMA3 gene in mice reveals abnormalities in survival and late stage differentiation of epithelial cells
    • COI: 1:CAS:528:DyaK1MXjvVKiu70%3D, PID: 10366601
    • Ryan MC, Lee K, Miyashita Y, Carter WG (1999) Targeted disruption of the LAMA3 gene in mice reveals abnormalities in survival and late stage differentiation of epithelial cells. J Cell Biol 145:1309–1323
    • (1999) J Cell Biol , vol.145 , pp. 1309-1323
    • Ryan, M.C.1    Lee, K.2    Miyashita, Y.3    Carter, W.G.4
  • 137
    • 0042679580 scopus 로고    scopus 로고
    • The MSP receptor regulates alpha6beta4 and alpha3beta1 integrins via 14-3-3 proteins in keratinocyte migration
    • COI: 1:CAS:528:DC%2BD3sXmvVCit7c%3D, PID: 12919677
    • Santoro MM, Gaudino G, Marchisio PC (2003) The MSP receptor regulates alpha6beta4 and alpha3beta1 integrins via 14-3-3 proteins in keratinocyte migration. Dev Cell 5:257–271
    • (2003) Dev Cell , vol.5 , pp. 257-271
    • Santoro, M.M.1    Gaudino, G.2    Marchisio, P.C.3
  • 138
    • 0025604399 scopus 로고
    • Bullous pemphigoid antigen (BPAG1): cDNA cloning and mapping of the gene to the short arm of human chromosome 6
    • COI: 1:CAS:528:DyaK3MXksVejsrk%3D, PID: 2276744
    • Sawamura D, Nomura K, Sugita Y, Mattei MG, Chu ML, Knowlton R, Uitto J (1990) Bullous pemphigoid antigen (BPAG1): cDNA cloning and mapping of the gene to the short arm of human chromosome 6. Genomics 8:722–726
    • (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
  • 139
    • 0032514156 scopus 로고    scopus 로고
    • Hemidesmosome formation is initiated by the beta4 integrin subunit, requires complex formation of beta4 and HD1/plectin, and involves a direct interaction between beta4 and the bullous pemphigoid antigen 180
    • COI: 1:CAS:528:DyaK1cXkslWhtr0%3D, PID: 9660880
    • Schaapveld RQ, Borradori L, Geerts D, van Leusden MR, Kuikman I, Nievers MG, Niessen CM, Steenbergen RD, Snijders PJ, Sonnenberg A (1998) Hemidesmosome formation is initiated by the beta4 integrin subunit, requires complex formation of beta4 and HD1/plectin, and involves a direct interaction between beta4 and the bullous pemphigoid antigen 180. J Cell Biol 142:271–284
    • (1998) J Cell Biol , vol.142 , pp. 271-284
    • Schaapveld, R.Q.1    Borradori, L.2    Geerts, D.3    van Leusden, M.R.4    Kuikman, I.5    Nievers, M.G.6    Niessen, C.M.7    Steenbergen, R.D.8    Snijders, P.J.9    Sonnenberg, A.10
  • 141
    • 2442675099 scopus 로고    scopus 로고
    • Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin
    • PID: 15128297
    • Sevcík J, Urbániková L, Kost'an J, Janda L, Wiche G (2004) Actin-binding domain of mouse plectin. Crystal structure and binding to vimentin. Eur J Biochem 271:1873–1884
    • (2004) Eur J Biochem , vol.271 , pp. 1873-1884
    • Sevcík, J.1    Urbániková, L.2    Kost'an, J.3    Janda, L.4    Wiche, G.5
  • 143
    • 79958859497 scopus 로고    scopus 로고
    • Ultrastructure and molecular pathogenesis of epidermolysis bullosa
    • PID: 21679868
    • Shinkuma S, McMillan JR, Shimizu H (2011) Ultrastructure and molecular pathogenesis of epidermolysis bullosa. Clin Dermatol 29:412–419
    • (2011) Clin Dermatol , vol.29 , pp. 412-419
    • Shinkuma, S.1    McMillan, J.R.2    Shimizu, H.3
  • 144
    • 0030975429 scopus 로고    scopus 로고
    • Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin
    • COI: 1:CAS:528:DyaK2sXislamt70%3D, PID: 9111230
    • Sincock PM, Mayrhofer G, Ashman LK (1997) Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and alpha5beta1 integrin. J Histochem Cytochem 45:515–525
    • (1997) J Histochem Cytochem , vol.45 , pp. 515-525
    • Sincock, P.M.1    Mayrhofer, G.2    Ashman, L.K.3
  • 145
    • 0028178390 scopus 로고
    • IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions
    • COI: 1:CAS:528:DyaK2cXis1Kntro%3D, PID: 8138568
    • Skalli O, Jones JC, Gagescu R, Goldman RD (1994) IFAP 300 is common to desmosomes and hemidesmosomes and is a possible linker of intermediate filaments to these junctions. J Cell Biol 125:159–170
    • (1994) J Cell Biol , vol.125 , pp. 159-170
    • Skalli, O.1    Jones, J.C.2    Gagescu, R.3    Goldman, R.D.4
  • 148
    • 0028944247 scopus 로고
    • A recombinant tail-less integrin beta 4 subunit disrupts hemidesmosomes, but does not suppress alpha 6 beta 4-mediated cell adhesion to laminins
    • COI: 1:CAS:528:DyaK2MXkvFCis7s%3D, PID: 7721947
    • Spinardi L, Einheber S, Cullen T, Milner TA, Giancotti FG (1995) A recombinant tail-less integrin beta 4 subunit disrupts hemidesmosomes, but does not suppress alpha 6 beta 4-mediated cell adhesion to laminins. J Cell Biol 129:473–487
    • (1995) J Cell Biol , vol.129 , pp. 473-487
    • Spinardi, L.1    Einheber, S.2    Cullen, T.3    Milner, T.A.4    Giancotti, F.G.5
  • 149
    • 0024272151 scopus 로고
    • Isolation of complementary DNA for bullous pemphigoid antigen by use of patients' autoantibodies
    • COI: 1:CAS:528:DyaL1MXntVentg%3D%3D, PID: 2461961
    • Stanley JR, Tanaka T, Mueller S, Klaus-Kovtun V, Roop D (1988) Isolation of complementary DNA for bullous pemphigoid antigen by use of patients' autoantibodies. J Clin Invest 82:1864–1870
    • (1988) J Clin Invest , vol.82 , pp. 1864-1870
    • Stanley, J.R.1    Tanaka, T.2    Mueller, S.3    Klaus-Kovtun, V.4    Roop, D.5
  • 150
    • 0034003558 scopus 로고    scopus 로고
    • Dose-dependent linkage, assembly inhibition and disassembly of vimentin and cytokeratin 5/14 filaments through plectin's intermediate filament-binding domain
    • PID: 10639335
    • Steinböck FA, Nikolic B, Coulombe PA, Fuchs E, Traub P, Wiche G (2000) Dose-dependent linkage, assembly inhibition and disassembly of vimentin and cytokeratin 5/14 filaments through plectin's intermediate filament-binding domain. J Cell Sci 113:483–491
    • (2000) J Cell Sci , vol.113 , pp. 483-491
    • Steinböck, F.A.1    Nikolic, B.2    Coulombe, P.A.3    Fuchs, E.4    Traub, P.5    Wiche, G.6
  • 151
    • 0034658462 scopus 로고    scopus 로고
    • The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes
    • COI: 1:CAS:528:DC%2BD3cXjtlKns7Y%3D, PID: 10811835
    • Sterk LM, Geuijen CA, Oomen LC, Calafat J, Janssen H, Sonnenberg A (2000) The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes. J Cell Biol 149:969–982
    • (2000) J Cell Biol , vol.149 , pp. 969-982
    • Sterk, L.M.1    Geuijen, C.A.2    Oomen, L.C.3    Calafat, J.4    Janssen, H.5    Sonnenberg, A.6
  • 152
    • 65249130582 scopus 로고    scopus 로고
    • Integrin beta 4 in neural cells
    • COI: 1:CAS:528:DC%2BD1MXhtlKkug%3D%3D
    • Su L, Lv X, Miao J (2008) Integrin beta 4 in neural cells. Neuromol Med 10:316–321
    • (2008) Neuromol Med , vol.10 , pp. 316-321
    • Su, L.1    Lv, X.2    Miao, J.3
  • 153
    • 84862603775 scopus 로고    scopus 로고
    • Spectraplakins: master orchestrators of cytoskeletal dynamics
    • COI: 1:CAS:528:DC%2BC38XnsVSrtbo%3D, PID: 22584905
    • Suozzi KC, Wu X, Fuchs E (2012) Spectraplakins: master orchestrators of cytoskeletal dynamics. J Cell Biol 197:465–475
    • (2012) J Cell Biol , vol.197 , pp. 465-475
    • Suozzi, K.C.1    Wu, X.2    Fuchs, E.3
  • 154
    • 0025020280 scopus 로고
    • Amino acid sequence of a novel integrin beta 4 subunit and primary expression of the mRNA in epithelial cells
    • COI: 1:CAS:528:DyaK3cXlt1Ogu7g%3D, PID: 2311577
    • Suzuki S, Naitoh Y (1990) Amino acid sequence of a novel integrin beta 4 subunit and primary expression of the mRNA in epithelial cells. EMBO J 9:757–763
    • (1990) EMBO J , vol.9 , pp. 757-763
    • Suzuki, S.1    Naitoh, Y.2
  • 155
    • 0025149542 scopus 로고
    • Epithelial integrin alpha 6 beta 4: complete primary structure of alpha 6 and variant forms of beta 4
    • COI: 1:CAS:528:DyaK3MXhtlyhs7g%3D, PID: 1976638
    • Tamura RN, Rozzo C, Starr L, Chambers J, Reichardt LF, Cooper HM, Quaranta V (1990) Epithelial integrin alpha 6 beta 4: complete primary structure of alpha 6 and variant forms of beta 4. J Cell Biol 111:1593–1604
    • (1990) J Cell Biol , vol.111 , pp. 1593-1604
    • Tamura, R.N.1    Rozzo, C.2    Starr, L.3    Chambers, J.4    Reichardt, L.F.5    Cooper, H.M.6    Quaranta, V.7
  • 156
    • 0029986491 scopus 로고    scopus 로고
    • Structural analysis of the predicted coiled-coil rod domain of the cytoplasmic bullous pemphigoid antigen (BPAG1). Empirical localization of the N-terminal globular domain-rod boundary
    • COI: 1:CAS:528:DyaK28XisFSlsL4%3D, PID: 8621649
    • Tang HY, Chaffotte AF, Thacher SM (1996) Structural analysis of the predicted coiled-coil rod domain of the cytoplasmic bullous pemphigoid antigen (BPAG1). Empirical localization of the N-terminal globular domain-rod boundary. J Biol Chem 271:9716–9722
    • (1996) J Biol Chem , vol.271 , pp. 9716-9722
    • Tang, H.Y.1    Chaffotte, A.F.2    Thacher, S.M.3
  • 157
    • 2442701762 scopus 로고    scopus 로고
    • Keratinocytes from patients lacking collagen XVII display a migratory phenotype
    • COI: 1:CAS:528:DC%2BD2cXltFyms7c%3D, PID: 15161638
    • Tasanen K, Tunggal L, Chometon G, Bruckner-Tuderman L, Aumailley M (2004) Keratinocytes from patients lacking collagen XVII display a migratory phenotype. Am J Pathol 164:2027–2038
    • (2004) Am J Pathol , vol.164 , pp. 2027-2038
    • Tasanen, K.1    Tunggal, L.2    Chometon, G.3    Bruckner-Tuderman, L.4    Aumailley, M.5
  • 158
    • 0029823622 scopus 로고    scopus 로고
    • Selective changes in laminin adhesion and alpha 6 beta 4 integrin regulation are associated with the initial steps in keratinocyte maturation
    • COI: 1:CAS:528:DyaK28XivFKgt78%3D, PID: 8732671
    • Tennenbaum T, Li L, Belanger AJ, De Luca LM, Yuspa SH (1996) Selective changes in laminin adhesion and alpha 6 beta 4 integrin regulation are associated with the initial steps in keratinocyte maturation. Cell Growth Differ 7:615–628
    • (1996) Cell Growth Differ , vol.7 , pp. 615-628
    • Tennenbaum, T.1    Li, L.2    Belanger, A.J.3    De Luca, L.M.4    Yuspa, S.H.5
  • 159
    • 0021721975 scopus 로고
    • Ultrastructural morphometry of normal human dermal-epidermal junction. The influence of age, sex, and body region on laminar and nonlaminar components
    • COI: 1:STN:280:DyaL2M%2Fls1CmsA%3D%3D, PID: 6209345
    • Tidman MJ, Eady RA (1984) Ultrastructural morphometry of normal human dermal-epidermal junction. The influence of age, sex, and body region on laminar and nonlaminar components. J Invest Dermatol 83:448–453
    • (1984) J Invest Dermatol , vol.83 , pp. 448-453
    • Tidman, M.J.1    Eady, R.A.2
  • 160
    • 0022631878 scopus 로고
    • Hemidesmosome heterogeneity in junctional epidermolysis bullosa revealed by morphometric analysis
    • COI: 1:STN:280:DyaL28zgsF2nsw%3D%3D, PID: 3745934
    • Tidman MJ, Eady RA (1986) Hemidesmosome heterogeneity in junctional epidermolysis bullosa revealed by morphometric analysis. J Invest Dermatol 86:51–56
    • (1986) J Invest Dermatol , vol.86 , pp. 51-56
    • Tidman, M.J.1    Eady, R.A.2
  • 161
    • 0035977147 scopus 로고    scopus 로고
    • A signaling adapter function for alpha6beta4 integrin in the control of HGF-dependent invasive growth
    • COI: 1:CAS:528:DC%2BD3MXptVaqtrk%3D, PID: 11733063
    • Trusolino L, Bertotti A, Comoglio PM (2001) A signaling adapter function for alpha6beta4 integrin in the control of HGF-dependent invasive growth. Cell 107:643–654
    • (2001) Cell , vol.107 , pp. 643-654
    • Trusolino, L.1    Bertotti, A.2    Comoglio, P.M.3
  • 162
    • 0037308755 scopus 로고    scopus 로고
    • Hemidesmosome protein dynamics in live epithelial cells
    • COI: 1:CAS:528:DC%2BD3sXhs1yqu7c%3D
    • Tsuruta D, Hopkinson SB, Jones JC (2003) Hemidesmosome protein dynamics in live epithelial cells. Cell Mot Cytoskeleton 54:122–134
    • (2003) Cell Mot Cytoskeleton , vol.54 , pp. 122-134
    • Tsuruta, D.1    Hopkinson, S.B.2    Jones, J.C.3
  • 163
    • 0028197645 scopus 로고
    • Demonstration of type II hemidesmosomes in a mammary gland epithelial cell line, BMGE-H
    • COI: 1:CAS:528:DyaK2cXitFegsb8%3D, PID: 8056759
    • Uematsu J, Nishizawa Y, Sonnenberg A, Owaribe K (1994) Demonstration of type II hemidesmosomes in a mammary gland epithelial cell line, BMGE-H. J Biochem 115:469–476
    • (1994) J Biochem , vol.115 , pp. 469-476
    • Uematsu, J.1    Nishizawa, Y.2    Sonnenberg, A.3    Owaribe, K.4
  • 164
    • 79952104090 scopus 로고    scopus 로고
    • Type XVII collagen (BP180) can function as a cell-matrix adhesion molecule via binding to laminin 332
    • PID: 21034821
    • Van den Bergh F, Eliason SL, Giudice GJ (2011) Type XVII collagen (BP180) can function as a cell-matrix adhesion molecule via binding to laminin 332. Matrix Biol 30:100–108
    • (2011) Matrix Biol , vol.30 , pp. 100-108
    • Van den Bergh, F.1    Eliason, S.L.2    Giudice, G.J.3
  • 165
    • 0030015434 scopus 로고    scopus 로고
    • Epithelial detachment due to absence of hemidesmosomes in integrin beta 4 null mice
    • PID: 8673140
    • van der Neut R, Krimpenfort P, Calafat J, Niessen CM, Sonnenberg A (1996) Epithelial detachment due to absence of hemidesmosomes in integrin beta 4 null mice. Nat Genet 13:366–369
    • (1996) Nat Genet , vol.13 , pp. 366-369
    • van der Neut, R.1    Krimpenfort, P.2    Calafat, J.3    Niessen, C.M.4    Sonnenberg, A.5
  • 166
    • 56149121572 scopus 로고    scopus 로고
    • Conditional deletion of the Itgb4 integrin gene in Schwann cells leads to delayed peripheral nerve regeneration
    • PID: 18971471
    • Van der Zee CE, Kreft M, Beckers G, Kuipers A, Sonnenberg A (2008) Conditional deletion of the Itgb4 integrin gene in Schwann cells leads to delayed peripheral nerve regeneration. J Neurosci 28:11292–11303
    • (2008) J Neurosci , vol.28 , pp. 11292-11303
    • Van der Zee, C.E.1    Kreft, M.2    Beckers, G.3    Kuipers, A.4    Sonnenberg, A.5
  • 167
    • 0030934096 scopus 로고    scopus 로고
    • Rapid disruption of an astrocyte interaction with the extracellular matrix mediated by integrin alpha 6 beta 4 during focal cerebral ischemia/reperfusion
    • COI: 1:CAS:528:DyaK2sXislyhsLw%3D, PID: 9099208
    • Wagner S, Tagaya M, Koziol JA, Quaranta V, del Zoppo GJ (1997) Rapid disruption of an astrocyte interaction with the extracellular matrix mediated by integrin alpha 6 beta 4 during focal cerebral ischemia/reperfusion. Stroke 28:858–865
    • (1997) Stroke , vol.28 , pp. 858-865
    • Wagner, S.1    Tagaya, M.2    Koziol, J.A.3    Quaranta, V.4    del Zoppo, G.J.5
  • 169
    • 84872358776 scopus 로고    scopus 로고
    • The vWFA2 domain of type VII collagen is responsible for collagen binding
    • COI: 1:CAS:528:DC%2BC3sXhvFamuw%3D%3D, PID: 23237810
    • Wegener H, Leineweber S, Seeger K (2013) The vWFA2 domain of type VII collagen is responsible for collagen binding. Biochem Biophys Res Commun 430:449–453
    • (2013) Biochem Biophys Res Commun , vol.430 , pp. 449-453
    • Wegener, H.1    Leineweber, S.2    Seeger, K.3
  • 170
    • 84876298788 scopus 로고    scopus 로고
    • Endothelial beta4 integrin is predominantly expressed in arterioles, where it promotes vascular remodeling in the hypoxic brain
    • COI: 1:CAS:528:DC%2BC3sXlslalsb8%3D, PID: 23471230
    • Welser-Alves JV, Boroujerdi A, Tigges U, Wrabetz L, Feltri ML, Milner R (2013) Endothelial beta4 integrin is predominantly expressed in arterioles, where it promotes vascular remodeling in the hypoxic brain. Arterioscler Thromb Vasc Biol 33:943–953
    • (2013) Arterioscler Thromb Vasc Biol , vol.33 , pp. 943-953
    • Welser-Alves, J.V.1    Boroujerdi, A.2    Tigges, U.3    Wrabetz, L.4    Feltri, M.L.5    Milner, R.6
  • 171
    • 84992236576 scopus 로고    scopus 로고
    • Plectin isoforms as organizers of intermediate filament cytoarchitecture
    • PID: 21866256
    • Wiche G, Winter L (2011) Plectin isoforms as organizers of intermediate filament cytoarchitecture. Bioarchitecture 1:14–20
    • (2011) Bioarchitecture , vol.1 , pp. 14-20
    • Wiche, G.1    Winter, L.2
  • 172
    • 0020612365 scopus 로고
    • Occurrence and immunolocalization of plectin in tissues
    • COI: 1:CAS:528:DyaL3sXltlOht7g%3D, PID: 6350322
    • Wiche G, Krepler R, Artlieb U, Pytela R, Denk H (1983) Occurrence and immunolocalization of plectin in tissues. J Cell Biol 97:887–901
    • (1983) J Cell Biol , vol.97 , pp. 887-901
    • Wiche, G.1    Krepler, R.2    Artlieb, U.3    Pytela, R.4    Denk, H.5
  • 173
    • 0021749865 scopus 로고
    • Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes
    • COI: 1:CAS:528:DyaL2cXmt1Onurc%3D, PID: 6386498
    • Wiche G, Krepler R, Artlieb U, Pytela R, Aberer W (1984) Identification of plectin in different human cell types and immunolocalization at epithelial basal cell surface membranes. Exp Cell Res 155:43–49
    • (1984) Exp Cell Res , vol.155 , pp. 43-49
    • Wiche, G.1    Krepler, R.2    Artlieb, U.3    Pytela, R.4    Aberer, W.5
  • 174
    • 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
    • COI: 1:CAS:528:DyaK38Xht1entLw%3D, PID: 2050743
    • Wiche G, Becker B, Luber K, Weitzer G, Castañón MJ, Hauptmann R, Stratowa C, Stewart M (1991) 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 Cell Biol 114:83–99
    • (1991) J Cell Biol , vol.114 , pp. 83-99
    • Wiche, G.1    Becker, B.2    Luber, K.3    Weitzer, G.4    Castañón, M.J.5    Hauptmann, R.6    Stratowa, C.7    Stewart, M.8
  • 175
    • 33645837225 scopus 로고    scopus 로고
    • Multiple functions of the integrin alpha6beta4 in epidermal homeostasis and tumorigenesis
    • COI: 1:CAS:528:DC%2BD28Xjs1Slsb8%3D, PID: 16581764
    • Wilhelmsen K, Litjens SH, Sonnenberg A (2006) Multiple functions of the integrin alpha6beta4 in epidermal homeostasis and tumorigenesis. Mol Cell Biol 26:2877–2886
    • (2006) Mol Cell Biol , vol.26 , pp. 2877-2886
    • Wilhelmsen, K.1    Litjens, S.H.2    Sonnenberg, A.3
  • 176
    • 34548477663 scopus 로고    scopus 로고
    • Serine phosphorylation of the integrin beta4 subunit is necessary for epidermal growth factor receptor induced hemidesmosome disruption
    • COI: 1:CAS:528:DC%2BD2sXhtVWnt7bK, PID: 17615294
    • Wilhelmsen K, Litjens SH, Kuikman I, Margadant C, van Rheenen J, Sonnenberg A (2007) Serine phosphorylation of the integrin beta4 subunit is necessary for epidermal growth factor receptor induced hemidesmosome disruption. Mol Biol Cell 18:3512–3522
    • (2007) Mol Biol Cell , vol.18 , pp. 3512-3522
    • Wilhelmsen, K.1    Litjens, S.H.2    Kuikman, I.3    Margadant, C.4    van Rheenen, J.5    Sonnenberg, A.6
  • 177
    • 84872350268 scopus 로고    scopus 로고
    • The many faces of plectin and plectinopathies: pathology and mechanisms
    • COI: 1:CAS:528:DC%2BC3sXktVyrtg%3D%3D, PID: 22864774
    • Winter L, Wiche G (2013) The many faces of plectin and plectinopathies: pathology and mechanisms. Acta Neuropathol 125:77–93
    • (2013) Acta Neuropathol , vol.125 , pp. 77-93
    • Winter, L.1    Wiche, G.2
  • 178
    • 33744763348 scopus 로고    scopus 로고
    • A critical role for tetraspanin CD151 in alpha3beta1 and alpha6beta4 integrin-dependent tumor cell functions on laminin-5
    • COI: 1:CAS:528:DC%2BD28XlvVCis7w%3D, PID: 16571677
    • Winterwood NE, Varzavand A, Meland MN, Ashman LK, Stipp CS (2006) A critical role for tetraspanin CD151 in alpha3beta1 and alpha6beta4 integrin-dependent tumor cell functions on laminin-5. Mol Biol Cell 17:2707–2721
    • (2006) Mol Biol Cell , vol.17 , pp. 2707-2721
    • Winterwood, N.E.1    Varzavand, A.2    Meland, M.N.3    Ashman, L.K.4    Stipp, C.S.5
  • 181
    • 57749169272 scopus 로고    scopus 로고
    • Tetraspanins: push and pull in suppressing and promoting metastasis
    • PID: 19078974
    • Zoller M (2009) Tetraspanins: push and pull in suppressing and promoting metastasis. Nat Rev Cancer 9:40–55
    • (2009) Nat Rev Cancer , vol.9 , pp. 40-55
    • Zoller, M.1


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