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1 mbrane zone antigens directly interfere with hemidesmosomal adhesion, activating complement and Fc re
5 diseases in which autoantibodies target the hemidesmosomal antigen BP180 and desmosomal antigens Dsg
12 py using mAbs specific for this integrin and hemidesmosomal components and its loss from a cytokerati
13 ocalize with hemidesmosome proteins, whereas hemidesmosomal components in cells expressing GFP-beta4K
14 ed no major abnormalities in localization of hemidesmosomal components, but desmosomal components org
15 asal cell carcinomas in their loss of normal hemidesmosomal components, presence of p53 mutations, fr
16 rescued the alterations in the deposition of hemidesmosomal components, such as plectin, collagen typ
18 4 subunit mediates both association with the hemidesmosomal cytoskeleton and recruitment of the signa
20 s, is known to be caused by mutations in the hemidesmosomal genes ITGA6 and ITGB4, which encode the a
21 l electrophoresis, co-migrated with BP180, a hemidesmosomal glycoprotein associated with two other au
22 n occurs intracellularly at the level of the hemidesmosomal inner plaque, which contains plectin, a h
23 e mutation, p.Gln1124X, leads to the loss of hemidesmosomal inner plaques and a complete absence of s
24 isoform that led to ultrastructural loss of hemidesmosomal inner plaques and clinical features of tr
25 Here, we show that keratinocytes lacking hemidesmosomal integrin alpha6beta4 exhibit increased fo
26 on of EGF receptor (EGF-R) combines with the hemidesmosomal integrin alpha6beta4 in both normal and n
28 either the beta 4 integrin subunit or HD1, a hemidesmosomal plaque component, showed that in control
29 s in the ITGA6 and ITGB4 genes, encoding the hemidesmosomal protein alpha6beta4-integrin, have been i
30 BP180 (also termed type XVII collagen) is a hemidesmosomal protein and plays a critical role in cell
31 characterized by autoantibodies against the hemidesmosomal protein BP180 (BPAg2, type XVII collagen)
32 mediated by antibodies directed against the hemidesmosomal protein BP180 (collagen XVII, BPAG2), and
33 al separation triggered by antibodies to the hemidesmosomal protein BP180 (collagen XVII, BPAG2).
34 ntibodies that recognize epitopes within the hemidesmosomal protein BP180, including its NC16A domain
40 The quest for the function of BPAG1, a major hemidesmosomal protein of skin keratinocytes, has led to
41 n the plectin gene (PLEC1), encoding another hemidesmosomal protein previously linked to EB with musc
43 a4 integrin (ITGB4), and in the gene for the hemidesmosomal protein type XVII collagen (COL17A1/BPAG2
45 ted with autoantibodies directed against the hemidesmosomal proteins BP180 and BP230 and inflammation
46 disease arises from autoantibodies targeting hemidesmosomal proteins BP180 and BP230, which are cruci
49 e does not affect expression levels of other hemidesmosomal proteins, nor the amount of beta4 integri
51 ntified in the BPAG2/COL17A1 gene encoding a hemidesmosomal transmembrane protein, the 180 kDa bullou
52 h late-onset muscular dystrophy (EB-MD) is a hemidesmosomal variant of EB due to mutations in the ple