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4 diseases in which autoantibodies target the hemidesmosomal antigen BP180 and desmosomal antigens Dsg
11 py using mAbs specific for this integrin and hemidesmosomal components and its loss from a cytokerati
12 ocalize with hemidesmosome proteins, whereas hemidesmosomal components in cells expressing GFP-beta4K
13 ed no major abnormalities in localization of hemidesmosomal components, but desmosomal components org
14 asal cell carcinomas in their loss of normal hemidesmosomal components, presence of p53 mutations, fr
15 rescued the alterations in the deposition of hemidesmosomal components, such as plectin, collagen typ
17 4 subunit mediates both association with the hemidesmosomal cytoskeleton and recruitment of the signa
19 s, is known to be caused by mutations in the hemidesmosomal genes ITGA6 and ITGB4, which encode the a
20 l electrophoresis, co-migrated with BP180, a hemidesmosomal glycoprotein associated with two other au
21 n occurs intracellularly at the level of the hemidesmosomal inner plaque, which contains plectin, a h
22 e mutation, p.Gln1124X, leads to the loss of hemidesmosomal inner plaques and a complete absence of s
23 isoform that led to ultrastructural loss of hemidesmosomal inner plaques and clinical features of tr
24 on of EGF receptor (EGF-R) combines with the hemidesmosomal integrin alpha6beta4 in both normal and n
26 either the beta 4 integrin subunit or HD1, a hemidesmosomal plaque component, showed that in control
27 s in the ITGA6 and ITGB4 genes, encoding the hemidesmosomal protein alpha6beta4-integrin, have been i
28 characterized by autoantibodies against the hemidesmosomal protein BP180 (BPAg2, type XVII collagen)
29 mediated by antibodies directed against the hemidesmosomal protein BP180 (collagen XVII, BPAG2), and
30 al separation triggered by antibodies to the hemidesmosomal protein BP180 (collagen XVII, BPAG2).
36 The quest for the function of BPAG1, a major hemidesmosomal protein of skin keratinocytes, has led to
37 n the plectin gene (PLEC1), encoding another hemidesmosomal protein previously linked to EB with musc
39 a4 integrin (ITGB4), and in the gene for the hemidesmosomal protein type XVII collagen (COL17A1/BPAG2
41 ted with autoantibodies directed against the hemidesmosomal proteins BP180 and BP230 and inflammation
44 e does not affect expression levels of other hemidesmosomal proteins, nor the amount of beta4 integri
45 ntified in the BPAG2/COL17A1 gene encoding a hemidesmosomal transmembrane protein, the 180 kDa bullou
46 h late-onset muscular dystrophy (EB-MD) is a hemidesmosomal variant of EB due to mutations in the ple
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