메뉴 건너뛰기




Volumn 45, Issue 2, 2011, Pages 202-220

Do cell junction protein mutations cause an airway phenotype in mice or humans?

Author keywords

Adherens proteins; Airway epithelia; Cell adhesion; Hemi desmosomes; Tight junction

Indexed keywords

INTEGRIN;

EID: 80051618750     PISSN: 10441549     EISSN: None     Source Type: Journal    
DOI: 10.1165/rcmb.2010-0498TR     Document Type: Review
Times cited : (6)

References (266)
  • 1
  • 3
    • 0033498876 scopus 로고    scopus 로고
    • Lung symptoms in pseudohypoaldosteronism type 1 are associated with deficiency of the alpha-subunit of the epithelial sodium channel
    • Schaedel C, Marthinsen L, Kristoffersson AC, Kornfalt R, Nilsson KO, Orlenius B, Holmberg L. Lung symptoms in pseudohypoaldosteronism type 1 are associated with deficiency of the alpha-subunit of the epithelial sodium channel. J Pediatr 1999;135:739-745. (Pubitemid 30180424)
    • (1999) Journal of Pediatrics , vol.135 , Issue.6 , pp. 739-745
    • Schaedel, C.1    Marthinsen, L.2    Kristoffersson, A.-C.3    Kornfalt, R.4    Nilsson, K.O.5    Orlenius, B.6    Holmberg, L.7
  • 5
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie CM, Anderson JM. Claudins and epithelial paracellular transport. Annu Rev Physiol 2006;68:403-429.
    • (2006) Annu Rev Physiol , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 8
    • 29144533473 scopus 로고    scopus 로고
    • Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells
    • DOI 10.1083/jcb.200510043
    • Ikenouchi J, Furuse M, Furuse K, Sasaki H, Tsukita S, Tsukita S. Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J Cell Biol 2005;171:939-945. (Pubitemid 41815826)
    • (2005) Journal of Cell Biology , vol.171 , Issue.6 , pp. 939-945
    • Ikenouchi, J.1    Furuse, M.2    Furuse, K.3    Sasaki, H.4    Tsukita, S.5    Tsukita, S.6
  • 12
    • 35348841509 scopus 로고    scopus 로고
    • Tight junctions/adherens junctions: Basic structure and function
    • DOI 10.1038/sj.jid.5700865, PII 5700865
    • Niessen CM. Tight junctions/adherens junctions: basic structure and function. J Invest Dermatol 2007;127:2525-2532. (Pubitemid 47585053)
    • (2007) Journal of Investigative Dermatology , vol.127 , Issue.11 , pp. 2525-2532
    • Niessen, C.M.1
  • 13
    • 34249785986 scopus 로고    scopus 로고
    • Functional effects of coxsackievirus and adenovirus receptor glycosylation on homophilic adhesion and adenoviral infection
    • DOI 10.1128/JVI.02562-06
    • Excoffon KJDA, Gansemer N, Traver G, Zabner J. Functional effects of Coxsackievirus and adenovirus receptor glycosylation on homophilic adhesion and adenoviral infection. J Virol 2007;81:5573-5578. (Pubitemid 46846997)
    • (2007) Journal of Virology , vol.81 , Issue.11 , pp. 5573-5578
    • Ashbourne, E.K.J.D.1    Gansemer, N.2    Traver, G.3    Zabner, J.4
  • 14
    • 0346025727 scopus 로고    scopus 로고
    • Junctional adhesion molecules (JAMs): More molecules with dual functions?
    • DOI 10.1242/jcs.00930
    • Ebnet K, Suzuki A, Ohno S, Vestweber D. Junctional adhesion molecules (JAMS): more molecules with dual functions? J Cell Sci 2004;117:19-29. (Pubitemid 38072117)
    • (2004) Journal of Cell Science , vol.117 , Issue.1 , pp. 19-29
    • Ebnet, K.1    Suzuki, A.2    Ohno, S.3    Vestweber, D.4
  • 19
    • 0035991944 scopus 로고    scopus 로고
    • Desmosomal adhesion: Structural basis, molecular mechanism and regulation (review)
    • DOI 10.1080/09687680210132476
    • Garrod DR, Merritt AJ, Nie Z. Desmosomal adhesion: structural basis, molecular mechanism and regulation. Mol Membr Biol 2002;19:81-94. (review). (Pubitemid 34753312)
    • (2002) Molecular Membrane Biology , vol.19 , Issue.2 , pp. 81-94
    • Garrod, D.R.1    Merritt, A.J.2    Nie, Z.3
  • 22
    • 0030006606 scopus 로고    scopus 로고
    • Desmosomes and hemidesmosomes: Structure and function of molecular components
    • Green KJ, Jones JC. Desmosomes and hemidesmosomes: structure and function of molecular components. FASEB J 1996;10:871-881. (Pubitemid 26186121)
    • (1996) FASEB Journal , vol.10 , Issue.8 , pp. 871-881
    • Green, K.J.1    Jones, J.C.R.2
  • 23
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge K, Fath K, Kelly T, Nuckolls G, Turner C. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu Rev Cell Biol 1988;4:487-525. (Pubitemid 19139264)
    • (1988) Annual Review of Cell Biology , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 24
    • 0036461064 scopus 로고    scopus 로고
    • Laminin 5 mutations in junctional epidermolysis bullosa: Molecular basis of Herlitz vs non-Herlitz phenotypes
    • DOI 10.1007/s00439-001-0630-1
    • Nakano A, Chao S-C, Pulkkinen L, Murrell D, Bruckner-Tuderman L, Pfendner E, Uitto J. Laminin 5 mutations in junctional epidermolysis bullosa: molecular basis of Herlitz vs. non-Herlitz phenotypes. Hum Genet 2002;110:41-51. (Pubitemid 36067416)
    • (2002) Human Genetics , vol.110 , Issue.1 , pp. 41-51
    • Nakano, A.1    Chao, S.-C.2    Pulkkinen, L.3    Murrell, D.4    Bruckner-Tuderman, L.5    Pfendner, E.6    Uitto, J.7
  • 25
    • 0025214541 scopus 로고
    • Point mutations impairing cell surface expression of the common beta subunit (CD18) in a patient with leukocyte adhesion molecule (Leu-CAM) deficiency
    • Arnaout MA, Dana N, Gupta SK, Tenen DG, Fathallah DM. Point mutations impairing cell surface expression of the common beta subunit (cd18) in a patient with leukocyte adhesion molecule (leucam) deficiency. J Clin Invest 1990;85:977-981. (Pubitemid 20087506)
    • (1990) Journal of Clinical Investigation , vol.85 , Issue.3 , pp. 977-981
    • Arnaout, M.A.1    Dana, N.2    Gupta, S.K.3    Tenen, D.G.4    Fathallah, D.M.5
  • 26
    • 0025284549 scopus 로고
    • Distinct mutations in two patients with leukocyte adhesion deficiency and their functional correlates
    • DOI 10.1084/jem.172.1.335
    • Wardlaw AJ, Hibbs ML, Stacker SA, Springer TA. Distinct mutations in two patients with leukocyte adhesion deficiency and their functional correlates. J Exp Med 1990;172:335-345. (Pubitemid 20217275)
    • (1990) Journal of Experimental Medicine , vol.172 , Issue.1 , pp. 335-345
    • Wardlaw, A.J.1    Hibbs, M.L.2    Stacker, S.A.3    Springer, T.A.4
  • 27
    • 0034233562 scopus 로고    scopus 로고
    • In vivo functions of integrins: Lessons from null mutations in mice
    • DOI 10.1016/S0945-053X(00)00065-2, PII S0945053X00000652
    • Sheppard D. In vivo functions of integrins: lessons from null mutations in mice. Matrix Biol 2000;19:203-209. (Pubitemid 30601753)
    • (2000) Matrix Biology , vol.19 , Issue.3 , pp. 203-209
    • Sheppard, D.1
  • 28
    • 0037662109 scopus 로고    scopus 로고
    • Functions of pulmonary epithelial integrins: From development to disease
    • Sheppard D. Functions of pulmonary epithelial integrins: from development to disease. Physiol Rev 2003;83:673-686. (Pubitemid 36828923)
    • (2003) Physiological Reviews , vol.83 , Issue.3 , pp. 673-686
    • Sheppard, D.1
  • 29
    • 0043281578 scopus 로고    scopus 로고
    • The role of connexins in human disease
    • DOI 10.1097/01.AUD.0000079801.55588.13
    • Chang EH, Van Camp G, Smith RJ. The role of connexins in human disease. Ear Hear 2003;24:314-323. (Pubitemid 37022143)
    • (2003) Ear and Hearing , vol.24 , Issue.4 , pp. 314-323
    • Chang, E.H.1    Van Camp, G.2    Smith, R.J.H.3
  • 34
    • 0030589587 scopus 로고    scopus 로고
    • Targeted mutations in cell adhesion genes: What have we learned from them?
    • DOI 10.1006/dbio.1996.0314
    • Hynes RO. Targeted mutations in cell adhesion genes: what have we learned from them? Dev Biol 1996;180:402-412. (Pubitemid 27037349)
    • (1996) Developmental Biology , vol.180 , Issue.2 , pp. 402-412
    • Hynes, R.O.1
  • 35
    • 0032587606 scopus 로고    scopus 로고
    • Synergistic activities of alpha3 and alpha6 integrins are required during apical ectodermal ridge formation and organogenesis in the mouse
    • De Arcangelis A, Mark M, Kreidberg J, Sorokin L, Georges-Labouesse E. Synergistic activities of alpha3 and alpha6 integrins are required during apical ectodermal ridge formation and organogenesis in the mouse. Development 1999;126:3957-3968. (Pubitemid 29440492)
    • (1999) Development , vol.126 , Issue.17 , pp. 3957-3968
    • De Arcangelis, A.1    Mark, M.2    Kreidberg, J.3    Sorokin, L.4    Georges-Labouesse, E.5
  • 41
    • 78349238517 scopus 로고    scopus 로고
    • Beta6 integrin subunit deficiency alleviates lung injury in a mouse model of bronchopulmonary dysplasia
    • Hogmalm A, Sheppard D, Lappalainen U, Bry K. Beta6 integrin subunit deficiency alleviates lung injury in a mouse model of bronchopulmonary dysplasia. Am J Respir Cell Mol Biol 2010;43:88-98.
    • (2010) Am J Respir Cell Mol Biol , vol.43 , pp. 88-98
    • Hogmalm, A.1    Sheppard, D.2    Lappalainen, U.3    Bry, K.4
  • 43
    • 33644620397 scopus 로고    scopus 로고
    • Lung development in laminin gamma2 deficiency: Abnormal tracheal hemidesmosomes with normal branching morphogenesis and epithelial differentiation
    • Nguyen NM, Pulkkinen L, Schlueter JA, Meneguzzi G, Uitto J, Senior RM. Lung development in laminin gamma2 deficiency: abnormal tracheal hemidesmosomes with normal branching morphogenesis and epithelial differentiation. Respir Res 2006;7:28.
    • (2006) Respir Res , vol.7 , pp. 28
    • Nguyen, N.M.1    Pulkkinen, L.2    Schlueter, J.A.3    Meneguzzi, G.4    Uitto, J.5    Senior, R.M.6
  • 46
    • 0037128938 scopus 로고    scopus 로고
    • Claudin-based tight junctions are crucial for the mammalian epidermal barrier: A lesson from claudin-1-deficient mice
    • DOI 10.1083/jcb.200110122
    • Furuse M, Hata M, Furuse K, Yoshida Y, Haratake A, Sugitani Y, Noda T, Kubo A, Tsukita S. Claudin-based tight junctions are crucial for the mammalian epidermal barrier: a lesson from claudin-1-deficient mice. J Cell Biol 2002;156:1099-1111. (Pubitemid 34839858)
    • (2002) Journal of Cell Biology , vol.156 , Issue.6 , pp. 1099-1111
    • Furuse, M.1    Hata, M.2    Furuse, K.3    Yoshida, Y.4    Haratake, A.5    Sugitani, Y.6    Noda, T.7    Kubo, A.8    Tsukita, S.9
  • 53
    • 57349133000 scopus 로고    scopus 로고
    • Salt and acid-base metabolism in claudin-16 knockdown mice: Impact for the pathophysiology of FHHNC patients
    • Himmerkus N, Shan Q, Goerke B, Hou J, Goodenough DA, Bleich M. Salt and acid-base metabolism in claudin-16 knockdown mice: impact for the pathophysiology of FHHNC patients. Am J Physiol Renal Physiol 2008;295:F1641-F1647.
    • (2008) Am J Physiol Renal Physiol , vol.295
    • Himmerkus, N.1    Shan, Q.2    Goerke, B.3    Hou, J.4    Goodenough, D.A.5    Bleich, M.6
  • 57
    • 38949172779 scopus 로고    scopus 로고
    • Splice-site mutations in the tric gene underlie autosomal recessive nonsyndromic hearing impairment in Pakistani families
    • Chishti MS, Bhatti A, Tamim S, Lee K, McDonald ML, Leal SM, Ahmad W. Splice-site mutations in the tric gene underlie autosomal recessive nonsyndromic hearing impairment in Pakistani families. J Hum Genet 2008;53:101-105.
    • (2008) J Hum Genet , vol.53 , pp. 101-105
    • Chishti, M.S.1    Bhatti, A.2    Tamim, S.3    Lee, K.4    McDonald, M.L.5    Leal, S.M.6    Ahmad, W.7
  • 59
    • 40749084863 scopus 로고    scopus 로고
    • Early embryonic lethality of mice lacking ZO-2, but not ZO-3, reveals critical and nonredundant roles for individual zonula occludens proteins in mammalian development
    • Xu J, Kausalya PJ, Phua DC, Ali SM, Hossain Z, Hunziker W. Early embryonic lethality of mice lacking ZO-2, but not ZO-3, reveals critical and nonredundant roles for individual zonula occludens proteins in mammalian development. Mol Cell Biol 2008;28:1669-1678.
    • (2008) Mol Cell Biol , vol.28 , pp. 1669-1678
    • Xu, J.1    Kausalya, P.J.2    Phua, D.C.3    Ali, S.M.4    Hossain, Z.5    Hunziker, W.6
  • 62
    • 33645525311 scopus 로고    scopus 로고
    • Absence of the tight junctional protein AF-6 disrupts epithelial cell-cell junctions and cell polarity during mouse development
    • DOI 10.1016/S0960-9822(99)80392-3
    • Zhadanov AB, Provance DW, Speer CA, Coffin JD, Goss D, Blixt JA, Reichert CM, Mercer JA. Absence of the tight junctional protein AF-6 disrupts epithelial cell-cell junctions and cell polarity during mouse development. Curr Biol 1999;9:880-888. (Pubitemid 29456005)
    • (1999) Current Biology , vol.9 , Issue.16 , pp. 880-888
    • Zhadanov, A.B.1    Provance Jr., D.W.2    Speer, C.A.3    Coffin, J.D.4    Goss, D.5    Blixt, J.A.6    Reichert, C.M.7    Mercer, J.A.8
  • 63
    • 0034425423 scopus 로고    scopus 로고
    • Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpesvirus receptor, in cleft lip/palate-ectodermal dysplasia
    • DOI 10.1038/78119
    • Suzuki K, Hu D, Bustos T, Zlotogora J, Richieri-Costa A, Helms JA, Spritz RA. Mutations of PVRL1, encoding a cell-cell adhesion molecule/herpesvirus receptor, in cleft lip/palate-ectodermal dysplasia. Nat Genet 2000;25:427-430. (Pubitemid 32983436)
    • (2000) Nature Genetics , vol.25 , Issue.4 , pp. 427-430
    • Suzuki, K.1    Hu, D.2    Bustos, T.3    Zlotogora, J.4    Richieri-Costa, A.5    Helms, J.A.6    Spritz, R.A.7
  • 75
    • 32044453541 scopus 로고    scopus 로고
    • p120-catenin mediates inflammatory responses in the skin
    • DOI 10.1016/j.cell.2005.11.043, PII S0092867406000080
    • Perez-Moreno M, Davis MA, Wong E, Pasolli HA, Reynolds AB, Fuchs E. P120-catenin mediates inflammatory responses in the skin. Cell 2006;124:631-644. (Pubitemid 43199446)
    • (2006) Cell , vol.124 , Issue.3 , pp. 631-644
    • Perez-Moreno, M.1    Davis, M.A.2    Wong, E.3    Pasolli, H.A.4    Reynolds, A.B.5    Fuchs, E.6
  • 76
    • 0035936807 scopus 로고    scopus 로고
    • Hyperproliferation and defects in epithelial polarity upon conditional ablation of alpha-catenin in skin
    • DOI 10.1016/S0092-8674(01)00246-X
    • Vasioukhin V, Bauer C, Degenstein L, Wise B, Fuchs E. Hyperproliferation and defects in epithelial polarity upon conditional ablation of alpha-catenin in skin. Cell 2001;104:605-617. (Pubitemid 32201954)
    • (2001) Cell , vol.104 , Issue.4 , pp. 605-617
    • Vasioukhin, V.1    Bauer, C.2    Degenstein, L.3    Wise, B.4    Fuchs, E.5
  • 77
    • 0036108620 scopus 로고    scopus 로고
    • Cadherin and catenin alterations in human cancer
    • DOI 10.1002/gcc.10083
    • Hajra K, Fearon E. Cadherin and catenin alterations in human cancer. Genes Chromosomes Cancer 2002;34:255-268. (Pubitemid 34553304)
    • (2002) Genes Chromosomes and Cancer , vol.34 , Issue.3 , pp. 255-268
    • Hajra, K.M.1    Fearon, E.R.2
  • 82
    • 33644984369 scopus 로고    scopus 로고
    • Desmocollin 3 is required for pre-implantation development of the mouse embryo
    • Den Z, Cheng X, Merched-Sauvage M, Koch PJ. Desmocollin 3 is required for pre-implantation development of the mouse embryo. J Cell Sci 2006;119:482-489.
    • (2006) J Cell Sci , vol.119 , pp. 482-489
    • Den, Z.1    Cheng, X.2    Merched-Sauvage, M.3    Koch, P.J.4
  • 85
    • 34249657898 scopus 로고    scopus 로고
    • Desmoglein-2 mutations in arrhythmogenic right ventricular cardiomyopathy: A genotype-phenotype characterization of familial disease
    • DOI 10.1093/eurheartj/ehl380
    • Syrris P, Ward D, Asimaki A, Evans A, Sen-Chowdhry S, Hughes SE, McKenna WJ. Desmoglein-2 mutations in arrhythmogenic right ventricular cardiomyopathy: a genotype-phenotype characterization of familial disease. Eur Heart J 2007;28:581-588. (Pubitemid 47355498)
    • (2007) European Heart Journal , vol.28 , Issue.5 , pp. 581-588
    • Syrris, P.1    Ward, D.2    Asimaki, A.3    Evans, A.4    Sen-Chowdhry, S.5    Hughes, S.E.6    McKenna, W.J.7
  • 86
    • 1842857530 scopus 로고    scopus 로고
    • Loss of desmoglein 2 suggests essential functions for early embryonic development and proliferation of embryonal stem cells
    • Eshkind L, Tian Q, Schmidt A, Franke WW, Windoffer R, Leube RE. Loss of desmoglein 2 suggests essential functions for early embryonic development and proliferation of embryonal stem cells. Eur J Cell Biol 2002;81:592-598. (Pubitemid 35446792)
    • (2002) European Journal of Cell Biology , vol.81 , Issue.11 , pp. 592-598
    • Eshkind, L.1    Tian, Q.2    Schmidt, A.3    Franke, W.W.4    Windoffer, R.5    Leube, R.E.6
  • 87
    • 0030902370 scopus 로고    scopus 로고
    • Targeted disruption of the pemphigus vulgaris antigen (desmoglein 3) gene in mice causes loss of keratinocyte cell adhesion with a phenotype similar to pemphigus vulgaris
    • DOI 10.1083/jcb.137.5.1091
    • Koch PJ, Mahoney MG, Ishikawa H, Pulkkinen L, Uitto J, Shultz L, Murphy GF, Whitaker-Menezes D, Stanley JR. Targeted disruption of the pemphigus vulgaris antigen (desmoglein 3) gene in mice causes loss of keratinocyte cell adhesion with a phenotype similar to pemphigus vulgaris. J Cell Biol 1997;137:1091-1102. (Pubitemid 27251044)
    • (1997) Journal of Cell Biology , vol.137 , Issue.5 , pp. 1091-1102
    • Koch, P.J.1    Mahoney, M.G.2    Ishikawa, H.3    Pulkkinen, L.4    Uitto, J.5    Shultz, L.6    Murphy, G.F.7    Whitaker-Menezes, D.8    Stanley, J.R.9
  • 96
    • 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 GI, 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 2001;128:929-941. (Pubitemid 32288203)
    • (2001) Development , vol.128 , Issue.6 , pp. 929-941
    • Gallicano, G.I.1    Bauer, C.2    Fuchs, E.3
  • 97
    • 20644437528 scopus 로고    scopus 로고
    • Desmoplakin is required early in development for assembly of desmosomes and cytoskeletal linkage
    • DOI 10.1083/jcb.143.7.2009
    • Gallicano GI, Kouklis P, Bauer C, Yin M, Vasioukhin V, Degenstein L, Fuchs E. Desmoplakin is required early in development for assembly of desmosomes and cytoskeletal linkage. J Cell Biol 1998;143:2009-2022. (Pubitemid 29022620)
    • (1998) Journal of Cell Biology , vol.143 , Issue.7 , pp. 2009-2022
    • Ian, G.G.1    Kouklis, P.2    Bauer, C.3    Yin, M.4    Vasioukhin, V.5    Degenstein, L.6    Fuchs, E.7
  • 98
    • 0033832770 scopus 로고    scopus 로고
    • Genomic amplification of the human plakophilin 1 gene and detection of a new mutation in ectodermal dysplasia/skin fragility syndrome
    • Whittock NV, Haftek M, Angoulvant N, Wolf F, Perrot H, Eady RA, McGrath JA. Genomic amplification of the human plakophilin 1 gene and detection of a new mutation in ectodermal dysplasia/skin fragility syndrome. J Invest Dermatol 2000;115:368-374.
    • (2000) J Invest Dermatol , vol.115 , pp. 368-374
    • Whittock, N.V.1    Haftek, M.2    Angoulvant, N.3    Wolf, F.4    Perrot, H.5    Eady, R.A.6    McGrath, J.A.7
  • 101
    • 0034679297 scopus 로고    scopus 로고
    • Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease)
    • McKoy G, Protonotarios N, Crosby A, Tsatsopoulou A, Anastasakis A, Coonar A, Norman M, Baboonian C, Jeffery S, McKenna WJ. Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (naxos disease). Lancet 2000;355:2119-2124. (Pubitemid 30364661)
    • (2000) Lancet , vol.355 , Issue.9221 , pp. 2119-2124
    • McKoy, G.1    Protonotarios, N.2    Crosby, A.3    Tsatsopoulou, A.4    Anastasakis, A.5    Coonar, A.6    Norman, M.7    Baboonian, C.8    Jeffery, S.9    McKenna, W.J.10
  • 103
    • 0029121987 scopus 로고
    • Mutations in the 180-KD bullous pemphigoid antigen (BPAG2), a hemidesmosomal transmembrane collagen (COL17A1), in generalized atrophic benign epidermolysis bullosa
    • McGrath JA, Gatalica B, Christiano AM, Li K, Owaribe K, McMillan JR, Eady RA, Uitto J. Mutations in the 180-KD bullous pemphigoid antigen (BPAG2), a hemidesmosomal transmembrane collagen (COL17A1), in generalized atrophic benign epidermolysis bullosa. Nat Genet 1995;11:83-86.
    • (1995) Nat Genet , vol.11 , pp. 83-86
    • McGrath, J.A.1    Gatalica, B.2    Christiano, A.M.3    Li, K.4    Owaribe, K.5    McMillan, J.R.6    Eady, R.A.7    Uitto, J.8
  • 104
    • 0031019014 scopus 로고    scopus 로고
    • Cloning of the human type XVII collagen gene (COL17A1), and detection of novel mutations in generalized atrophic benign epidermolysis bullosa
    • Gatalica B, Pulkkinen L, Li K, Kuokkanen K, Ryynänen M, McGrath JA, Uitto J. Cloning of the human type XVII collagen gene (COL17A1), and detection of novel mutations in generalized atrophic benign epidermolysis bullosa. Am J Hum Genet 1997;60:352-365. (Pubitemid 27058406)
    • (1997) American Journal of Human Genetics , vol.60 , Issue.2 , pp. 352-365
    • Gatalica, B.1    Pulkkinen, L.2    Li, K.3    Kuokkanen, K.4    Ryynanen, M.5    McGrath, J.A.6    Uitto, J.7
  • 107
    • 0030793302 scopus 로고    scopus 로고
    • A homozygous in-frame deletion in the collagenous domain of bullous pemphigoid antigen BP180 (type XVII collagen) causes generalized atrophic benign epidermolysis bullosa
    • Chavanas S, Gache Y, Tadini G, Pulkkinen L, Uitto J, Ortonne JP, Meneguzzi G. A homozygous in-frame deletion in the collagenous domain of bullous pemphigoid antigen BP180 (type XVII collagen) causes generalized atrophic benign epidermolysis bullosa. J Invest Dermatol 1997;109:74-78. (Pubitemid 27305652)
    • (1997) Journal of Investigative Dermatology , vol.109 , Issue.1 , pp. 74-78
    • Chavanas, S.1    Gache, Y.2    Tadini, G.3    Pulkkinen, L.4    Uitto, J.5    Ortonne, J.P.6    Meneguzzi, G.7
  • 108
    • 0031930104 scopus 로고    scopus 로고
    • A deletion mutation in COL17A1 in five Austrian families with generalized atrophic benign epidermolysis bullosa represents propagation of an ancestral allele
    • DOI 10.1046/j.1523-1747.1998.00101.x
    • Darling TN, Koh BB, Bale SJ, Compton JG, Bauer JW, Hintner H, Yancey KB. A deletion mutation in COL17A1 in five Austrian families with generalized atrophic benign epidermolysis bullosa represents propagation of an ancestral allele. J Invest Dermatol 1998;110:170-173. (Pubitemid 28105853)
    • (1998) Journal of Investigative Dermatology , vol.110 , Issue.2 , pp. 170-173
    • Darling, T.N.1    Koh, B.B.2    Bale, S.J.3    Compton, J.G.4    Bauer, J.W.5    Hintner, H.6    Yancey, K.B.7
  • 110
    • 0033889376 scopus 로고    scopus 로고
    • Hemizygosity for a glycine substitution in collagen XVII: Unfolding and degradation of the ectodomain
    • DOI 10.1046/j.1523-1747.2000.00049.x
    • Tasanen K, Floeth M, Schumann H, Bruckner-Tuderman L. Hemizygosity for a glycine substitution in collagen XVII: unfolding and degradation of the ectodomain. J Invest Dermatol 2000;115:207-212. (Pubitemid 30637189)
    • (2000) Journal of Investigative Dermatology , vol.115 , Issue.2 , pp. 207-212
    • Tasanen, K.1    Floeth, M.2    Schumann, H.3    Bruckner-Tuderman, L.4
  • 112
    • 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 FJ, Shimizu H, Murata S, Yaoita H, Hachisuka H, Nishikawa T, McLean WH, Uitto J. Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy. Hum Mol Genet 1996;5:1539-1546. (Pubitemid 26328869)
    • (1996) Human Molecular Genetics , vol.5 , Issue.10 , 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
  • 117
    • 11944249876 scopus 로고    scopus 로고
    • Plectin gene mutations can cause epidermolysis bullosa with pyloric atresia
    • DOI 10.1111/j.0022-202X.2004.23564.x
    • Pfendner E, Uitto J. Plectin gene mutations can cause epidermolysis bullosa with pyloric atresia. J Invest Dermatol 2005;124:111-115. (Pubitemid 40100957)
    • (2005) Journal of Investigative Dermatology , vol.124 , Issue.1 , pp. 111-115
    • Pfendner, E.1    Uitto, J.2
  • 118
    • 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 1997;11:3143-3156. (Pubitemid 27528055)
    • (1997) Genes and Development , vol.11 , Issue.23 , pp. 3143-3156
    • Andra, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fassler, R.5    Propst, F.6    Wiche, G.7
  • 119
    • 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
    • DOI 10.1182/blood-2004-04-1512
    • Karamatic Crew V, Burton N, Kagan A, Green CA, Levene C, Flinter F, Brady RL, Daniels G, Anstee DJ. 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 2004;104:2217-2223. (Pubitemid 39331816)
    • (2004) Blood , vol.104 , Issue.8 , pp. 2217-2223
    • Crew, V.K.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
  • 121
    • 0028895182 scopus 로고
    • Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with herlitz junctional epidermolysis bullosa
    • Vidal F, Baudoin C, Miquel C, Galliano MF, Christiano AM, Uitto J, Ortonne JP, Meneguzzi G. Cloning of the laminin alpha 3 chain gene (LAMA3) and identification of a homozygous deletion in a patient with herlitz junctional epidermolysis bullosa. Genomics 1995;30:273-280.
    • (1995) Genomics , vol.30 , pp. 273-280
    • Vidal, F.1    Baudoin, C.2    Miquel, C.3    Galliano, M.F.4    Christiano, A.M.5    Uitto, J.6    Ortonne, J.P.7    Meneguzzi, G.8
  • 122
    • 0030029420 scopus 로고    scopus 로고
    • Mutational hotspots in the LAMB3 gene in the lethal (Herlitz) type of junctional epidermolysis bullosa
    • DOI 10.1093/hmg/5.2.231
    • Kivirikko S, McGrath JA, Pulkkinen L, Uitto J, Christiano AM. Mutational hotspots in the LAMB3 gene in the lethal (Herlitz) type of junctional epidermolysis bullosa. Hum Mol Genet 1996;5:231-237. (Pubitemid 26036919)
    • (1996) Human Molecular Genetics , vol.5 , Issue.2 , pp. 231-237
    • Kivirikko, S.1    McGrath, J.A.2    Pulkkinen, L.3    Uitto, J.4    Christiano, A.M.5
  • 124
    • 0033553883 scopus 로고    scopus 로고
    • Targeted disruption of the LAMA3 gene in mice reveals abnormalities in survival and late stage differentiation of epithelial cells
    • DOI 10.1083/jcb.145.6.1309
    • Ryan MC, Lee K, Miyashita Y, Carter WG. Targeted disruption of the LAMA3 gene in mice reveals abnormalities in survival and late stage differentiation of epithelial cells. J Cell Biol 1999;145:1309-1323. (Pubitemid 29293640)
    • (1999) Journal of Cell Biology , vol.145 , Issue.6 , pp. 1309-1323
    • Ryan, M.C.1    Lee, K.2    Miyashita, Y.3    Carter, W.G.4
  • 126
    • 0028568985 scopus 로고
    • A homozygous nonsense mutation in the beta 3 chain gene of laminin 5 (LAMB3) in herlitz junctional epidermolysis bullosa
    • Pulkkinen L, Christiano AM, Gerecke D, Wagman DW, Burgeson RE, Pittelkow MR, Uitto J. A homozygous nonsense mutation in the beta 3 chain gene of laminin 5 (LAMB3) in herlitz junctional epidermolysis bullosa. Genomics 1994;24:357-360.
    • (1994) Genomics , vol.24 , pp. 357-360
    • Pulkkinen, L.1    Christiano, A.M.2    Gerecke, D.3    Wagman, D.W.4    Burgeson, R.E.5    Pittelkow, M.R.6    Uitto, J.7
  • 127
    • 0028919592 scopus 로고
    • Altered laminin 5 expression due to mutations in the gene encoding the beta 3 chain (LAMB3) in generalized atrophic benign epidermolysis bullosa
    • McGrath JA, Pulkkinen L, Christiano AM, Leigh IM, Eady RA, Uitto J. Altered laminin 5 expression due to mutations in the gene encoding the beta 3 chain (LAMB3) in generalized atrophic benign epidermolysis bullosa. J Invest Dermatol 1995;104:467-474.
    • (1995) J Invest Dermatol , vol.104 , pp. 467-474
    • McGrath, J.A.1    Pulkkinen, L.2    Christiano, A.M.3    Leigh, I.M.4    Eady, R.A.5    Uitto, J.6
  • 129
    • 0031930182 scopus 로고    scopus 로고
    • Novel mutations in the LAMB3 gene shared by two Japanese unrelated families with Herlitz junctional epidermolysis bullosa, and their application for prenatal testing
    • DOI 10.1046/j.1523-1747.1998.00105.x
    • Takizawa Y, Shimizu H, Pulkkinen L, Hiraoka Y, McGrath JA, Suzumori K, Aiso S, Uitto J, Nishikawa T. Novel mutations in the LAMB3 gene shared by two japanese unrelated families with herlitz junctional epidermolysis bullosa, and their application for prenatal testing. J Invest Dermatol 1998;110:174-178. (Pubitemid 28105854)
    • (1998) Journal of Investigative Dermatology , vol.110 , Issue.2 , pp. 174-178
    • Takizawa, Y.1    Shimizu, H.2    Pulkkinen, L.3    Hiraoka, Y.4    McGrath, J.A.5    Suzumori, K.6    Aiso, S.7    Uitto, J.8    Nishikawa, T.9
  • 131
    • 34248169121 scopus 로고    scopus 로고
    • Revertant mosaicism in junctional epidermolysis bullosa due to multiple correcting second-site mutations in LAMB3
    • DOI 10.1172/JCI30465
    • Pasmooij AM, Pas HH, Bolling MC, Jonkman MF. Revertant mosaicism in junctional epidermolysis bullosa due to multiple correcting second-site mutations in LAMB3. J Clin Invest 2007;117:1240-1248. (Pubitemid 46718412)
    • (2007) Journal of Clinical Investigation , vol.117 , Issue.5 , pp. 1240-1248
    • Pasmooij, A.M.G.1    Pas, H.H.2    Bolling, M.C.3    Jonkman, M.F.4
  • 132
    • 0028180092 scopus 로고
    • Mutations in the gamma 2 chain gene (LAMC2) of kalinin/laminin 5 in the junctional forms of epidermolysis bullosa
    • Pulkkinen L, Christiano AM, Airenne T, Haakana H, Tryggvason K, Uitto J. Mutations in the gamma 2 chain gene (LAMC2) of kalinin/laminin 5 in the junctional forms of epidermolysis bullosa. Nat Genet 1994;6:293-297.
    • (1994) Nat Genet , vol.6 , pp. 293-297
    • Pulkkinen, L.1    Christiano, A.M.2    Airenne, T.3    Haakana, H.4    Tryggvason, K.5    Uitto, J.6
  • 135
    • 0034244572 scopus 로고    scopus 로고
    • Complete paternal uniparental isodisomy of chromosome 1: A novel mechanism for Herlitz junctional epidermolysis bullosa
    • DOI 10.1046/j.1523-1747.2000.00052.x
    • Takizawa Y, Pulkkinen L, Chao SC, Nakajima H, Nakano Y, Shimizu H, Uitto J. Mutation report: complete paternal uniparental isodisomy of chromosome 1: a novel mechanism for Herlitz junctional epidermolysis bullosa. J Invest Dermatol 2000;115:307-311. (Pubitemid 30637203)
    • (2000) Journal of Investigative Dermatology , vol.115 , Issue.2 , pp. 307-311
    • Takizawa, Y.1    Pulkkinen, L.2    Chao, S.-C.3    Nakajima, H.4    Nakano, Y.5    Shimizu, H.6    Uitto, J.7
  • 136
    • 0034792542 scopus 로고    scopus 로고
    • Novel mutations in the LAMC2 gene in non-Herlitz junctional epidermolysis bullosa: Effects on laminin-5 assembly, secretion, and deposition
    • DOI 10.1046/j.0022-202x.2001.01453.x
    • Castiglia D, Posteraro P, Spirito F, Pinola M, Angelo C, Puddu P, Meneguzzi G, Zambruno G. Novel mutations in the LAMC2 gene in non-herlitz junctional epidermolysis bullosa: Effects on laminin-5 assembly, secretion, and deposition. J Invest Dermatol 2001;117:731-739. (Pubitemid 32955605)
    • (2001) Journal of Investigative Dermatology , vol.117 , Issue.3 , pp. 731-739
    • Castiglia, D.1    Posteraro, P.2    Spirito, F.3    Pinola, M.4    Angelo, C.5    Puddu, P.6    Meneguzzi, G.7    Zambruno, G.8
  • 139
    • 0033035808 scopus 로고    scopus 로고
    • Absence of integrin alpha1beta1 in the mouse causes loss of feedback regulation of collagen synthesis in normal and wounded dermis
    • Gardner H, Broberg A, Pozzi A, Laato M, Heino J. Absence of integrin alpha1beta1 in the mouse causes loss of feedback regulation of collagen synthesis in normal and wounded dermis. J Cell Sci 1999;112:263-272. (Pubitemid 29080649)
    • (1999) Journal of Cell Science , vol.112 , Issue.3 , pp. 263-272
    • Gardner, H.1    Broberg, A.2    Pozzi, A.3    Laato, M.4    Heino, J.5
  • 140
    • 0036314793 scopus 로고    scopus 로고
    • 2 integrin subunit-deficient mouse: A multifaceted phenotype including defects of branching morphogenesis and hemostasis
    • Chen J, Diacovo TG, Grenache DG, Santoro SA, Zutter MM. The alpha(2) integrin subunit-deficient mouse: a multifaceted phenotype including defects of branching morphogenesis and hemostasis. Am J Pathol 2002;161:337-344. (Pubitemid 34760799)
    • (2002) American Journal of Pathology , vol.161 , Issue.1 , pp. 337-344
    • Chen, J.1    Diacovo, T.G.2    Grenache, D.G.3    Santoro, S.A.4    Zutter, M.M.5
  • 142
    • 0026035227 scopus 로고
    • A deletion in the gene for glycoprotein IIb associated with Glanzmann's thrombasthenia
    • Burk CD, Newman PJ, Lyman S, Gill J, Coller BS, Poncz M. A deletion in the gene for glycoprotein IIb associated with Glanzmann's thrombasthenia. J Clin Invest 1991;87:270-276.
    • (1991) J Clin Invest , vol.87 , pp. 270-276
    • Burk, C.D.1    Newman, P.J.2    Lyman, S.3    Gill, J.4    Coller, B.S.5    Poncz, M.6
  • 143
    • 0026711020 scopus 로고
    • Molecular basis for Glanzmann's thrombasthenia (GT) in a compound heterozygote with glycoprotein IIb gene: A proposal for the classification of GT based on the biosynthetic pathway of glycoprotein IIb-IIIa complex
    • Kato A, Yamamoto K, Miyazaki S, Jung SM, Moroi M, Aoki N. Molecular basis for Glanzmann's thrombasthenia (GT) in a compound heterozygote with glycoprotein IIb gene: A proposal for the classification of GT based on the biosynthetic pathway of glycoprotein IIb-IIIa complex. Blood 1992;79:3212-3218.
    • (1992) Blood , vol.79 , pp. 3212-3218
    • Kato, A.1    Yamamoto, K.2    Miyazaki, S.3    Jung, S.M.4    Moroi, M.5    Aoki, N.6
  • 144
    • 0023664558 scopus 로고
    • Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors
    • Poncz M, Eisman R, Heidenreich R, Silver SM, Vilaire G, Surrey S, Schwartz E, Bennett JS. Structure of the platelet membrane glycoprotein IIb. Homology to the alpha subunits of the vitronectin and fibronectin membrane receptors. J Biol Chem 1987;262:8476-8482.
    • (1987) J Biol Chem , vol.262 , pp. 8476-8482
    • Poncz, M.1    Eisman, R.2    Heidenreich, R.3    Silver, S.M.4    Vilaire, G.5    Surrey, S.6    Schwartz, E.7    Bennett, J.S.8
  • 145
    • 0029154482 scopus 로고
    • The molecular genetic basis of Glanzmann's thrombasthenia in a gypsy population in France: Identification of a new mutation on the alpha IIb gene
    • Schlegel N, Gayet O, Morel-Kopp MC, Wyler B, Hurtaud-Roux MF, Kaplan C, Mc Gregor J. The molecular genetic basis of Glanzmann's thrombasthenia in a gypsy population in France: identification of a new mutation on the alpha IIb gene. Blood 1995;86:977-982.
    • (1995) Blood , vol.86 , pp. 977-982
    • Schlegel, N.1    Gayet, O.2    Morel-Kopp, M.C.3    Wyler, B.4    Hurtaud-Roux, M.F.5    Kaplan, C.6    Mc Gregor, J.7
  • 146
    • 0028951764 scopus 로고
    • Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association
    • Wilcox DA, Paddock CM, Lyman S, Gill JC, Newman PJ. Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association. J Clin Invest 1995;95:1553-1560.
    • (1995) J Clin Invest , vol.95 , pp. 1553-1560
    • Wilcox, D.A.1    Paddock, C.M.2    Lyman, S.3    Gill, J.C.4    Newman, P.J.5
  • 147
    • 0029947855 scopus 로고    scopus 로고
    • 3
    • Basani RB, Vilaire G, Shattil SJ, Kolodziej MA, Bennett JS, Poncz M. Glanzmann thrombasthenia due to a two amino acid deletion in the fourth calcium-binding domain of alpha IIb: Demonstration of the importance of calcium-binding domains in the conformation of alpha IIb beta 3. Blood 1996;88:167-173. (Pubitemid 26230684)
    • (1996) Blood , vol.88 , Issue.1 , pp. 167-173
    • Basani, R.B.1    Vilaire, G.2    Shattil, S.J.3    Kolodziej, M.A.4    Bennett, J.S.5    Poncz, M.6
  • 149
    • 0032032356 scopus 로고    scopus 로고
    • Glycoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/IIIa
    • Grimaldi CM, Chen F, Wu C, Weiss HJ, Coller BS, French DL. Glycoprotein IIb Leu214Pro mutation produces Glanzmann thrombasthenia with both quantitative and qualitative abnormalities in GPIIb/IIIa. Blood 1998;91:1562-1571. (Pubitemid 28110320)
    • (1998) Blood , vol.91 , Issue.5 , pp. 1562-1571
    • Grimaldi, C.M.1    Chen, F.2    Wu, C.3    Weiss, H.J.4    Coller, B.S.5    French, D.L.6
  • 150
    • 0034663430 scopus 로고    scopus 로고
    • Thrombasthenic mice generated by replacement of the integrin alpha(IIb) gene: Demonstration that transcriptional activation of this megakaryocytic locus precedes lineage commitment
    • Tronik-Le Roux D, Roullot V, Poujol C, Kortulewski T, Nurden P, Marguerie G. Thrombasthenic mice generated by replacement of the integrin alpha(IIb) gene: demonstration that transcriptional activation of this megakaryocytic locus precedes lineage commitment. Blood 2000;96:1399-1408. (Pubitemid 30658470)
    • (2000) Blood , vol.96 , Issue.4 , pp. 1399-1408
    • Tronik-Le, R.D.1    Roullot, V.2    Poujol, C.3    Kortulewski, T.4    Nurden, P.5    Marguerie, G.6
  • 151
    • 0030604540 scopus 로고    scopus 로고
    • Differential requirements for alpha4 integrins during fetal and adult hematopoiesis
    • DOI 10.1016/S0092-8674(00)81301-X
    • Arroyo AG, Yang JT, Rayburn H, Hynes RO. Differential requirements for alpha4 integrins during fetal and adult hematopoiesis. Cell 1996;85:997-1008. (Pubitemid 26231167)
    • (1996) Cell , vol.85 , Issue.7 , pp. 997-1008
    • Arroyo, A.G.1    Yang, J.T.2    Rayburn, H.3    Hynes, R.O.4
  • 152
    • 0027371908 scopus 로고
    • 5 integrin-deficient mice
    • Yang JT, Rayburn H, Hynes RO. Embryonic mesodermal defects in alpha 5 integrin-deficient mice. Development 1993;119:1093-1105. (Pubitemid 23358579)
    • (1993) Development , vol.119 , Issue.4 , pp. 1093-1105
    • Yang, J.T.1    Rayburn, H.2    Hynes, R.O.3
  • 154
    • 0029908558 scopus 로고    scopus 로고
    • Absence of integrin alpha6 leads to epidermolysis bullosa and neonatal death in mice
    • DOI 10.1038/ng0796-370
    • Georges-Labouesse E, Messaddeq N, Yehia G, Cadalbert L, Dierich A, Le Meur M. Absence of integrin alpha 6 leads to epidermolysis bullosa and neonatal death in mice. Nat Genet 1996;13:370-373. (Pubitemid 26230508)
    • (1996) Nature Genetics , vol.13 , Issue.3 , pp. 370-373
    • Georges-Labouesse, E.1    Messaddeq, N.2    Yehia, G.3    Cadalbert, L.4    Dierich, A.5    Le, M.M.6
  • 156
    • 0030614865 scopus 로고    scopus 로고
    • Integrin alpha8beta1 is critically important for epithelial-mesenchymal interactions during kidney morphogenesis
    • DOI 10.1016/S0092-8674(00)81903-0
    • Müller U, Wang D, Denda S, Meneses JJ, Pedersen RA, Reichardt LF. Integrin alpha8beta1 is critically important for epithelial-mesenchymal interactions during kidney morphogenesis. Cell 1997;88:603-613. (Pubitemid 27152403)
    • (1997) Cell , vol.88 , Issue.5 , pp. 603-613
    • Muller, U.1    Wang, D.2    Denda, S.3    Meneses, J.J.4    Pedersen, R.A.5    Reichardt, L.F.6
  • 161
    • 0032514841 scopus 로고    scopus 로고
    • Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all alphav integrins
    • Bader BL, Rayburn H, Crowley D, Hynes RO. Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all alpha V integrins. Cell 1998;95:507-519. (Pubitemid 28533307)
    • (1998) Cell , vol.95 , Issue.4 , pp. 507-519
    • Bader, B.L.1    Rayburn, H.2    Crowley, D.3    Hynes, R.O.4
  • 163
    • 0026504546 scopus 로고
    • An initiation codon mutation in CD18 in association with the moderate phenotype of leukocyte adhesion deficiency
    • Sligh JE Jr, Hurwitz MY, Zhu CM, Anderson DC, Beaudet AL. An initiation codon mutation in CD18 in association with the moderate phenotype of leukocyte adhesion deficiency. J Biol Chem 1992;267:714-718.
    • (1992) J Biol Chem , vol.267 , pp. 714-718
    • Sligh Jr., J.E.1    Hurwitz, M.Y.2    Zhu, C.M.3    Anderson, D.C.4    Beaudet, A.L.5
  • 165
    • 0026761286 scopus 로고
    • A spontaneous mutation of integrin alpha IIb beta 3 (platelet glycoprotein IIb-IIIa) helps define a ligand binding site
    • Bajt ML, Ginsberg MH, Frelinger AL, Berndt MC, Loftus JC. A spontaneous mutation of integrin alpha IIb beta 3 (platelet glycoprotein IIb-IIIa) helps define a ligand binding site. J Biol Chem 1992;267:3789-3794.
    • (1992) J Biol Chem , vol.267 , pp. 3789-3794
    • Bajt, M.L.1    Ginsberg, M.H.2    Frelinger, A.L.3    Berndt, M.C.4    Loftus, J.C.5
  • 166
    • 0025062149 scopus 로고
    • A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation
    • Loftus JC, O'Toole TE, Plow EF, Glass A, Frelinger AL III, Ginsberg MH. A beta 3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation. Science 1990;249:915-918.
    • (1990) Science , vol.249 , pp. 915-918
    • Loftus, J.C.1    O'Toole, T.E.2    Plow, E.F.3    Glass, A.4    Frelinger III, A.L.5    Ginsberg, M.H.6
  • 167
    • 0026720994 scopus 로고
    • A new variant of Glanzmann's thrombasthenia (Strasbourg I). Platelets with functionally defective glycoprotein IIb-IIIa complexes and a glycoprotein IIIa 214arg-214trp mutation
    • Lanza F, Stierlé A, Fournier D, Morales M, André G, Nurden AT, Cazenave JP. A new variant of Glanzmann's thrombasthenia (Strasbourg I). Platelets with functionally defective glycoprotein IIb-IIIa complexes and a glycoprotein IIIa 214arg-214trp mutation. J Clin Invest 1992;89:1995-2004.
    • (1992) J Clin Invest , vol.89 , pp. 1995-2004
    • Lanza, F.1    Stierlé, A.2    Fournier, D.3    Morales, M.4    André, G.5    Nurden, A.T.6    Cazenave, J.P.7
  • 168
    • 0026614923 scopus 로고
    • Ser-752→pro mutation in the cytoplasmic domain of integrin beta 3 subunit and defective activation of platelet integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia
    • Chen YP, Djaffar I, Pidard D, Steiner B, Cieutat AM, Caen JP, Rosa JP. Ser-752→pro mutation in the cytoplasmic domain of integrin beta 3 subunit and defective activation of platelet integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) in a variant of Glanzmann thrombasthenia. Proc Natl Acad Sci USA 1992;89:10169-10173.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10169-10173
    • Chen, Y.P.1    Djaffar, I.2    Pidard, D.3    Steiner, B.4    Cieutat, A.M.5    Caen, J.P.6    Rosa, J.P.7
  • 169
    • 0027499394 scopus 로고
    • Glanzmann's thrombasthenia caused by homozygosity for a splice defect that leads to deletion of the first coding exon of the glycoprotein IIIa mRNA
    • Simsek S, Heyboer H, de Bruijne-Admiraal LG, Goldschmeding R, Cuijpers HT, von dem Borne AE. Glanzmann's thrombasthenia caused by homozygosity for a splice defect that leads to deletion of the first coding exon of the glycoprotein IIIa mRNA. Blood 1993;81:2044-2049. (Pubitemid 23106718)
    • (1993) Blood , vol.81 , Issue.8 , pp. 2044-2049
    • Simsek, S.1    Heyboer, H.2    De Bruijne-Admiraal, L.G.3    Goldschmeding, R.4    Cuijpers, H.T.M.5    Von Dem, B.A.E.G.K.6
  • 170
    • 0030915793 scopus 로고    scopus 로고
    • Glanzmann thrombasthenia caused by an 11.2-kb deletion in the glycoprotein IIIa (beta;3) is a second mutation in Iraqi Jews that stemmed from a distinct founder
    • Rosenberg N, Yatuv R, Orion Y, Zivelin A, Dardik R, Peretz H, Seligsohn U. Glanzmann thrombasthenia caused by an 11.2-kb deletion in the glycoprotein IIIa (beta3) is a second mutation in Iraqi jews that stemmed from a distinct founder. Blood 1997;89:3654-3662. (Pubitemid 27227088)
    • (1997) Blood , vol.89 , Issue.10 , pp. 3654-3662
    • Rosenberg, N.1    Yatuv, R.2    Orion, Y.3    Zivelin, A.4    Dardik, R.5    Peretz, H.6    Seligsohn, U.7
  • 171
    • 0030664425 scopus 로고    scopus 로고
    • 3 complex
    • Wang R, Shattil SJ, Ambruso DR, Newman PJ. Truncation of the cytoplasmic domain of beta3 in a variant form of Glanzmann thrombasthenia abrogates signaling through the integrin alpha(IIb)-beta3 complex. J Clin Invest 1997;100:2393-2403. (Pubitemid 27500165)
    • (1997) Journal of Clinical Investigation , vol.100 , Issue.9 , pp. 2393-2403
    • Wang, R.1    Shattil, S.J.2    Ambruso, D.R.3    Newman, P.J.4
  • 172
    • 0032534999 scopus 로고    scopus 로고
    • Truncation of glycoprotein (GP) IIIa (616-762) prevents complex formation with GPIIB: Novel mutation in exon 11 of GPIIIa associated with thrombasthenia
    • Ferrer M, Tao J, Iruín G, Sánchez-Ayuso M, González-Rodríguez J, Parrilla R, González-Manchón C. Truncation of glycoprotein (GP) IIIa (616-762) prevents complex formation with GPIIb: Novel mutation in exon 11 of GPIIIa associated with thrombasthenia. Blood 1998;92:4712-4720. (Pubitemid 29005873)
    • (1998) Blood , vol.92 , Issue.12 , pp. 4712-4720
    • Ferrer, M.1    Tao, J.2    Iruin, G.3    Sanchez-Ayuso, M.4    Gonzajez-Rodriguez, J.5    Parrilla, R.6    Gonzalez-Manchon, C.7
  • 173
    • 33645786359 scopus 로고    scopus 로고
    • Molecular diversity of Glanzmann thrombasthenia in southern India: New insights into mRNA splicing and structure-function correlations of alphaIIb-beta3 integrin (ITGA2B, ITGB3)
    • Peretz H, Rosenberg N, Landau M, Usher S, Nelson EJ, Mor-Cohen R, French DL, Mitchell BW, Nair SC, Chandy M, et al. Molecular diversity of Glanzmann thrombasthenia in southern India: new insights into mRNA splicing and structure-function correlations of alphaIIb-beta3 integrin (ITGA2B, ITGB3). Hum Mutat 2006;27:359-369.
    • (2006) Hum Mutat , vol.27 , pp. 359-369
    • Peretz, H.1    Rosenberg, N.2    Landau, M.3    Usher, S.4    Nelson, E.J.5    Mor-Cohen, R.6    French, D.L.7    Mitchell, B.W.8    Nair, S.C.9    Chandy, M.10
  • 178
    • 0032875192 scopus 로고    scopus 로고
    • Splicing modulation of integrin beta4 pre-mRNA carrying a branch point mutation underlies epidermolysis bullosa with pyloric atresia undergoing spontaneous amelioration with ageing
    • DOI 10.1093/hmg/8.11.2097
    • Chavanas S, Gache Y, Vailly J, Kanitakis J, Pulkkinen L, Uitto J, Ortonne J, Meneguzzi G. Splicing modulation of integrin beta4 pre-mRNA carrying a branch point mutation underlies epidermolysis bullosa with pyloric atresia undergoing spontaneous amelioration with ageing. Hum Mol Genet 1999;8:2097-2105. (Pubitemid 29458738)
    • (1999) Human Molecular Genetics , vol.8 , Issue.11 , pp. 2097-2105
    • Chavanas, S.1    Gache, Y.2    Vailly, J.3    Kanitakis, J.4    Pulkkinen, L.5    Uitto, J.6    Ortonne, J.-P.7    Meneguzzi, G.8
  • 179
    • 0034068641 scopus 로고    scopus 로고
    • A homozygous missense mutation in the cytoplasmic tail of beta4 integrin, G931D, that disrupts hemidesmosome assembly and underlies non-Herlitz junctional epidermolysis bullosa without pyloric atresia? [3]
    • DOI 10.1046/j.1523-1747.2000.00960-3.x
    • Inoue M, Tamai K, Shimizu H, Owaribe K, Nakama T, Hashimoto T, McGrath JA. A homozygous missense mutation in the cytoplasmic tail of beta4 integrin, G931d, that disrupts hemidesmosome assembly and underlies non-Herlitz junctional epidermolysis bullosa without pyloric atresia? J Invest Dermatol 2000;114:1061-1064. (Pubitemid 30252734)
    • (2000) Journal of Investigative Dermatology , vol.114 , Issue.5 , pp. 1061-1064
    • Inoue, M.1    Tamai, K.2    Shimizu, H.3    Owaribe, K.4    Nakama, T.5    Hashimoto, T.6    McGrath, J.A.7
  • 182
    • 42949147509 scopus 로고    scopus 로고
    • Deletion of the first pair of fibronectin type III repeats of the integrin beta-4 gene is associated with epidermolysis bullosa, pyloric atresia and aplasia cutis congenita in the original carmi syndrome patients
    • Birnbaum RY, Landau D, Elbedour K, Ofir R, Birk OS, Carmi R. Deletion of the first pair of fibronectin type III repeats of the integrin beta-4 gene is associated with epidermolysis bullosa, pyloric atresia and aplasia cutis congenita in the original carmi syndrome patients. Am J Med Genet A 2008;146A:1063-1066.
    • (2008) Am J Med Genet A , vol.146 A , pp. 1063-1066
    • Birnbaum, R.Y.1    Landau, D.2    Elbedour, K.3    Ofir, R.4    Birk, O.S.5    Carmi, R.6
  • 183
  • 184
    • 0033982574 scopus 로고    scopus 로고
    • Normal development, wound healing, and adenovirus susceptibility in beta5- deficient mice
    • DOI 10.1128/MCB.20.3.755-759.2000
    • Huang X, Griffiths M, Wu J, Farese RV, Sheppard D. Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice. Mol Cell Biol 2000;20:755-759. (Pubitemid 30044211)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.3 , pp. 755-759
    • Huang, X.1    Griffiths, M.2    Wu, J.3    Farese Jr., R.V.4    Sheppard, D.5
  • 185
    • 0035984003 scopus 로고    scopus 로고
    • Beta8 Integrins are required for vascular morphogenesis in mouse embryos
    • Zhu J, Motejlek K, Wang D, Zang K, Schmidt A, Reichardt LF. Beta8 integrins are required for vascular morphogenesis in mouse embryos. Development 2002;129:2891-2903. (Pubitemid 34874268)
    • (2002) Development , vol.129 , Issue.12 , pp. 2891-2903
    • Zhu, J.1    Motejlek, K.2    Wang, D.3    Zang, K.4    Schmidt, A.5    Reichardt, L.F.6
  • 187
    • 0030696315 scopus 로고    scopus 로고
    • Two different connexin 26 mutations in an inbred kindred segregating non-syndromic recessive deafness: Implications for genetic studies in isolated populations
    • DOI 10.1093/hmg/6.12.2163
    • Carrasquillo MM, Zlotogora J, Barges S, Chakravarti A. Two different connexin 26 mutations in an inbred kindred segregating non-syndromic recessive deafness: implications for genetic studies in isolated populations. Hum Mol Genet 1997;6:2163-2172. (Pubitemid 27477960)
    • (1997) Human Molecular Genetics , vol.6 , Issue.12 , pp. 2163-2172
    • Carrasquillo, M.M.1    Zlotogora, J.2    Barges, S.3    Chakravarti, A.4
  • 189
    • 0032546033 scopus 로고    scopus 로고
    • Connexin 26 R143W mutation associated with recessive nonsyndromic sensorineural deafness in Africa [4]
    • DOI 10.1056/NEJM199802193380812
    • Brobby GW, Muller-Myhsok B, Horstmann RD. Connexin 26 r143w mutation associated with recessive nonsyndromic sensorineural deafness in Africa. N Engl J Med 1998;338:548-550. (Pubitemid 28103143)
    • (1998) New England Journal of Medicine , vol.338 , Issue.8 , pp. 548-550
    • Brobby, G.W.1    Muller-Myhsok, B.2    Horstmann, R.D.3
  • 192
    • 6344225698 scopus 로고    scopus 로고
    • Expanding the phenotypic spectrum of Cx26 disorders: Bart-Pumphrey syndrome is caused by a novel missense mutation in GJB2
    • DOI 10.1111/j.0022-202X.2004.23470.x
    • Richard G, Brown N, Ishida-Yamamoto A, Krol A. Expanding the phenotypic spectrum of CX26 disorders: Bart-pumphrey syndrome is caused by a novel missense mutation in GJB2. J Invest Dermatol 2004;123:856-863. (Pubitemid 39391929)
    • (2004) Journal of Investigative Dermatology , vol.123 , Issue.5 , pp. 856-863
    • Richard, G.1    Brown, N.2    Ishida-Yamamoto, A.3    Krol, A.4
  • 194
    • 0035500580 scopus 로고    scopus 로고
    • Connexin 26 gene (GJB2) mutation modulates the severity of hearing loss associated with the 1555A→G mitochondrial mutation
    • DOI 10.1002/1096-8628(20011101)103:4<334::AID-AJMG1574>3.0.CO;2-F
    • Abe S, Kelley PM, Kimberling WJ, Usami SI. Connexin 26 gene (GJB2) mutation modulates the severity of hearing loss associated with the 1555A→G mitochondrial mutation. Am J Med Genet 2001;103:334-338. (Pubitemid 32988601)
    • (2001) American Journal of Medical Genetics , vol.103 , Issue.4 , pp. 334-338
    • Abe, S.1    Kelley, P.M.2    Kimberling, W.J.3    Usami, S.-I.4
  • 195
    • 0034099846 scopus 로고    scopus 로고
    • A connexin 26 mutation causes a syndrome of sensorineural hearing loss and palmoplantar hyperkeratosis (MIM 148350)
    • Heathcote K, Syrris P, Carter ND, Patton MA. A connexin 26 mutation causes a syndrome of sensorineural hearing loss and palmoplantar hyperkeratosis (MIM 148350). J Med Genet 2000;37:50-51. (Pubitemid 30245875)
    • (2000) Journal of Medical Genetics , vol.37 , Issue.1 , pp. 50-51
    • Heathcote, K.1    Syrris, P.2    Carter, N.D.3    Patton, M.A.4
  • 198
    • 0035047780 scopus 로고    scopus 로고
    • W44C mutation in the connexin 26 gene associated with dominant non-syndromic deafness
    • DOI 10.1034/j.1399-0004.2001.590409.x
    • Tekin M, Arnos KS, Xia XJ, Oelrich MK, Liu XZ, Nance WE, Pandya A. W44c mutation in the connexin 26 gene associated with dominant non-syndromic deafness. Clin Genet 2001;59:269-273. (Pubitemid 32318394)
    • (2001) Clinical Genetics , vol.59 , Issue.4 , pp. 269-273
    • Tekin, M.1    Arnos, K.S.2    Xia, X.J.3    Oelrich, M.K.4    Liu, X.Z.5    Nance, W.E.6    Pandya, A.7
  • 199
    • 12244265494 scopus 로고    scopus 로고
    • Homozygosity for the V37I Connexin 26 mutation in three unrelated children with sensorineural hearing loss
    • DOI 10.1034/j.1399-0004.2002.610611.x
    • Bason L, Dudley T, Lewis K, Shah U, Potsic W, Ferraris A, Fortina P, Rappaport E, Krantz ID. Homozygosity for the V37I connexin 26 mutation in three unrelated children with sensorineural hearing loss. Clin Genet 2002;61:459-464. (Pubitemid 36372685)
    • (2002) Clinical Genetics , vol.61 , Issue.6 , pp. 459-464
    • Bason, L.1    Dudley, T.2    Lewis, K.3    Shah, U.4    Potsic, W.5    Ferraris, A.6    Fortina, P.7    Rappaport, E.8    Krantz, I.D.9
  • 201
    • 0242684552 scopus 로고    scopus 로고
    • Mutations in the gene for connexin 26 (GJB2) that cause hearing loss have a dominant negative effect on connexin 30
    • DOI 10.1093/hmg/ddg076
    • Marziano NK, Casalotti SO, Portelli AE, Becker DL, Forge A. Mutations in the gene for connexin 26 (GJB2) that cause hearing loss have a dominant negative effect on connexin 30. Hum Mol Genet 2003;12:805-812. (Pubitemid 36504023)
    • (2003) Human Molecular Genetics , vol.12 , Issue.8 , pp. 805-812
    • Marziano, N.K.1    Casalotti, S.O.2    Portelli, A.E.3    Becker, D.L.4    Forge, A.5
  • 204
    • 4344627625 scopus 로고    scopus 로고
    • Spectrum and frequencies of mutations in the GJB2 (Cx26) gene among 156 Czech patients with pre-lingual deafness
    • DOI 10.1111/j.1399-0004.2004.00283.x
    • Seeman P, Malíková M, Rasková D, Bendová O, Groh D, KubálkováM, Sakmaryová I, Seemanová E, Kabelka Z. Spectrum and frequencies of mutations in the GJB2 (CX26) gene among 156 Czech patients with pre-lingual deafness. Clin Genet 2004;66:152-157. (Pubitemid 39117523)
    • (2004) Clinical Genetics , vol.66 , Issue.2 , pp. 152-157
    • Seeman, P.1    Malikova, M.2    Raskova, D.3    Bendova, O.4    Groh, D.5    Kubalkova, M.6    Sakmaryova, I.7    Seemanova, E.8    Kabelka, Z.9
  • 206
  • 217
  • 229
    • 0032866609 scopus 로고    scopus 로고
    • Demyelinating X-linked Charcot-Marie-Tooth disease: Unusual electrophysiological findings
    • DOI 10.1002/(SICI)1097-4598(199910)22:10<1442::AID-MUS16>3.0.CO;2-6
    • Tabaraud F, Lagrange E, Sindou P, Vandenberghe A, Levy N, Vallat JM. Demyelinating X-linked Charcot-Marie-Tooth disease: unusual electrophysiological findings. Muscle Nerve 1999;22:1442-1447. (Pubitemid 29468431)
    • (1999) Muscle and Nerve , vol.22 , Issue.10 , pp. 1442-1447
    • Tabaraud, F.1    Lagrange, E.2    Sindou, P.3    Vandenberghe, A.4    Levy, N.5    Vallat, J.M.6
  • 231
    • 0029788204 scopus 로고    scopus 로고
    • Mutations of the noncoding region of the connexin32 gene in X-linked dominant Charcot-Marie-Tooth neuropathy
    • Ionasescu VV, Searby C, Ionasescu R, Neuhaus IM, Werner R. Mutations of the noncoding region of the connexin32 gene in X-linked dominant Charcot-Marie-Tooth neuropathy. Neurology 1996;47:541-544. (Pubitemid 26324057)
    • (1996) Neurology , vol.47 , Issue.2 , pp. 541-544
    • Ionasescu, V.V.1    Searby, C..2    Ionasescu, R.3    Neuhaus, I.M.4    Werner, R.5
  • 232
    • 0035960628 scopus 로고    scopus 로고
    • Episodes of generalized weakness in two sibs with the C164T mutation of the connexin 32 gene
    • Panas M, Kalfakis N, Karadimas C, Vassilopoulos D. Episodes of generalized weakness in two sibs with the C164T mutation of the connexin 32 gene. Neurology 2001;57:1906-1908. (Pubitemid 33096707)
    • (2001) Neurology , vol.57 , Issue.10 , pp. 1906-1908
    • Panas, M.1    Kalfakis, N.2    Karadimas, C.3    Vassilopoulos, D.4
  • 233
    • 0037167535 scopus 로고    scopus 로고
    • Novel mutation in X-linked Charcot-Marie-Tooth disease associated with CNS impairment
    • Kawakami H, Inoue K, Sakakihara I, Nakamura S. Novel mutation in X-linked Charcot-Marie-Tooth disease associated with CNS impairment. Neurology 2002;59:923-926.
    • (2002) Neurology , vol.59 , pp. 923-926
    • Kawakami, H.1    Inoue, K.2    Sakakihara, I.3    Nakamura, S.4
  • 234
    • 0344608882 scopus 로고    scopus 로고
    • Transient, recurrent, white matter lesions in X-linked Charcot-Marie-Tooth disease with novel connexin 32 mutation
    • DOI 10.1001/archneur.60.4.605
    • Hanemann CO, Bergmann C, Senderek J, Zerres K, Sperfeld AD. Transient, recurrent, white matter lesions in X-linked Charcot-Marie-Tooth disease with novel connexin 32 mutation. Arch Neurol 2003;60:605-609. (Pubitemid 36427976)
    • (2003) Archives of Neurology , vol.60 , Issue.4 , pp. 605-609
    • Hanemann, C.O.1    Bergmann, C.2    Senderek, J.3    Zerres, K.4    Sperfeld, A.-D.5
  • 238
    • 0032605229 scopus 로고    scopus 로고
    • Biological functions of connexin genes revealed by human genetic defects, dominant negative approaches and targeted deletions in the mouse
    • discussion 88-96
    • Willecke K, Kirchhoff S, Plum A, Temme A, Thonnissen E, Ott T. Biological functions of connexin genes revealed by human genetic defects, dominant negative approaches and targeted deletions in the mouse. Novartis Found Symp 1999;219:76-88, discussion 88-96.
    • (1999) Novartis Found Symp , vol.219 , pp. 76-88
    • Willecke, K.1    Kirchhoff, S.2    Plum, A.3    Temme, A.4    Thonnissen, E.5    Ott, T.6
  • 239
    • 0035899305 scopus 로고    scopus 로고
    • Synchronous activity of inhibitory networks in neocortex requires electrical synapses containing connexin36
    • DOI 10.1016/S0896-6273(01)00373-7
    • Deans MR, Gibson JR, Sellitto C, Connors BW, Paul DL. Synchronous activity of inhibitory networks in neocortex requires electrical synapses containing connexin36. Neuron 2001;31:477-485. (Pubitemid 32778565)
    • (2001) Neuron , vol.31 , Issue.3 , pp. 477-485
    • Deans, M.R.1    Gibson, J.R.2    Sellitto, C.3    Connors, B.W.4    Paul, D.L.5
  • 242
    • 0043026950 scopus 로고    scopus 로고
    • High incidence of cardiac malformations in Connexin40-deficient mice
    • DOI 10.1161/01.RES.0000084852.65396.70
    • Gu H, Smith FC, Taffet SM, Delmar M. High incidence of cardiac malformations in connexin40-deficient mice. Circ Res 2003;93:201-206. (Pubitemid 36993230)
    • (2003) Circulation Research , vol.93 , Issue.3 , pp. 201-206
    • Gu, H.1    Smith, F.C.2    Taffet, S.M.3    Delmar, M.4
  • 243
    • 0032567887 scopus 로고    scopus 로고
    • Mice lacking connexin40 have cardiac conduction abnormalities characteristic of atrioventricular block and bundle branch block
    • Simon AM, Goodenough DA, Paul DL. Mice lacking connexin40 have cardiac conduction abnormalities characteristic of atrioventricular block and bundle branch block. Curr Biol 1998;8:295-298. (Pubitemid 28111462)
    • (1998) Current Biology , vol.8 , Issue.5 , pp. 295-298
    • Simon, A.M.1    Goodenough, D.A.2    Paul, D.L.3
  • 250
    • 33746810189 scopus 로고    scopus 로고
    • A nonsense mutation in the first transmembrane domain of connexin 43 underlies autosomal recessive oculodentodigital syndrome
    • Richardson RJ, Joss S, Tomkin S, Ahmed M, Sheridan E, Dixon MJ. A nonsense mutation in the first transmembrane domain of connexin 43 underlies autosomal recessive oculodentodigital syndrome. J Med Genet 2006;43:e37.
    • (2006) J Med Genet , vol.43
    • Richardson, R.J.1    Joss, S.2    Tomkin, S.3    Ahmed, M.4    Sheridan, E.5    Dixon, M.J.6
  • 253
    • 0034019915 scopus 로고    scopus 로고
    • 3)
    • DOI 10.1007/s004390051029
    • Rees MI, Watts P, Fenton I, Clarke A, Snell RG, Owen MJ, Gray J. Further evidence of autosomal dominant congenital zonular pulverulent cataracts linked to 13q11 (CZP3) and a novel mutation in connexin 46 (GJA3). Hum Genet 2000;106:206-209. (Pubitemid 30156425)
    • (2000) Human Genetics , vol.106 , Issue.2 , pp. 206-209
    • Rees, M.I.1    Watts, P.2    Fenton, I.3    Clarke, A.4    Snell, R.G.5    Owen, M.J.6    Gray, J.7
  • 255
    • 0031283282 scopus 로고    scopus 로고
    • 3 connexin gene leads to proteolysis and cataractogenesis in mice
    • DOI 10.1016/S0092-8674(00)80471-7
    • Gong X, Li E, Klier G, Huang Q, Wu Y, Lei H, Kumar NM, Horwitz J, Gilula NB. Disruption of alpha3 connexin gene leads to proteolysis and cataractogenesis in mice. Cell 1997;91:833-843. (Pubitemid 28007739)
    • (1997) Cell , vol.91 , Issue.6 , pp. 833-843
    • Gong, X.1    Li, E.2    Klier, G.3    Huang, Q.4    Wu, Y.5    Lei, H.6    Kumar, N.M.7    Horwitz, J.8    Gilula, N.B.9
  • 259
    • 0038456539 scopus 로고    scopus 로고
    • Connexin 47 (Cx47)-deficient mice with enhanced green fluorescent protein reporter gene reveal predominant oligodendrocytic expression of Cx47 and display vacuolized myelin in the CNS
    • Odermatt B, Wellershaus K, Wallraff A, Seifert G, Degen J, Euwens C, Fuss B, Büssow H, Schilling K, Steinhäuser C, et al. Connexin 47 (CX47)-deficient mice with enhanced green fluorescent protein reporter gene reveal predominant oligodendrocytic expression of CX47 and display vacuolized myelin in the CNS. J Neurosci 2003;23:4549-4559. (Pubitemid 36706185)
    • (2003) Journal of Neuroscience , vol.23 , Issue.11 , pp. 4549-4559
    • Odermatt, B.1    Wellershaus, K.2    Wallraff, A.3    Seifert, G.4    Degen, J.5    Euwens, C.6    Fuss, B.7    Bussow, H.8    Schilling, K.9    Steinhauser, C.10    Willecke, K.11
  • 260
    • 0031959735 scopus 로고    scopus 로고
    • A missense mutation in the human connexin50 gene (GJA8) underlies autosomal dominant 'zonular pulverulent' cataract, on chromosome 1q
    • DOI 10.1086/301762
    • Shiels A, Mackay D, Ionides A, Berry V, Moore A, Bhattacharya S. A missense mutation in the human connexin50 gene (GJA8) underlies autosomal dominant "zonular pulverulent" cataract, on chromosome 1q. Am J Hum Genet 1998;62:526-532. (Pubitemid 28164609)
    • (1998) American Journal of Human Genetics , vol.62 , Issue.3 , pp. 526-532
    • Shiels, A.1    Mackay, D.2    Ionides, A.3    Berry, V.4    Moore, A.5    Bhattacharya, S.6
  • 262
    • 0035697326 scopus 로고    scopus 로고
    • Mutation in the connexin 50 gene (GJA8) in a Russian family with zonular pulverulent cataract
    • Polyakov AV, Shagina IA, Khlebnikova OV, Evgrafov OV. Mutation in the connexin 50 gene (GJA8) in a Russian family with zonular pulverulent cataract. Clin Genet 2001;60:476-478.
    • (2001) Clin Genet , vol.60 , pp. 476-478
    • Polyakov, A.V.1    Shagina, I.A.2    Khlebnikova, O.V.3    Evgrafov, O.V.4
  • 264
    • 33645115350 scopus 로고    scopus 로고
    • Novel mutations in GJA8 associated with autosomal dominant congenital cataract and microcornea
    • Devi RR, Vijayalakshmi P. Novel mutations in GJA8 associated with autosomal dominant congenital cataract and microcornea. Mol Vis 2006;12:190-195.
    • (2006) Mol Vis , vol.12 , pp. 190-195
    • Devi, R.R.1    Vijayalakshmi, P.2
  • 266
    • 0032476578 scopus 로고    scopus 로고
    • Targeted ablation of connexin50 in mice results in microphthalmia and zonular pulverulent cataracts
    • DOI 10.1083/jcb.143.3.815
    • White TW, Goodenough DA, Paul DL. Targeted ablation of connexin50 in mice results in microphthalmia and zonular pulverulent cataracts. J Cell Biol 1998;143:815-825. (Pubitemid 28512573)
    • (1998) Journal of Cell Biology , vol.143 , Issue.3 , pp. 815-825
    • White, T.W.1    Goodenough, D.A.2    Paul, D.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.