FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W146580823> ?p ?o ?g. }

• W146580823 endingPage "400" @default.
• W146580823 startingPage "398" @default.
• W146580823 abstract "To the Editor: Dystrophic epidermolysis bullosa (DEB) is a group of inherited skin diseases characterized by blistering and scarring induced by mild trauma. Both the dominant and the recessive forms show tissue separation below the basement membrane at the level of the anchoring fibrils, as determined by transmission electron microscopy and/or immunoepitope mapping. In different DEB variants anchoring fibrils have been shown to be morphologically altered, reduced in number, or entirely absent. In connection with the fact that the fibrils consist predominantly of type VII collagen (Burgeson, 1993Burgeson R.E. Type VII collagen, anchoring fibrils, and epidermolysis bullosa.J Invest Dermatol. 1993; 101: 252-255Abstract Full Text PDF PubMed Google Scholar), mutations in the corresponding gene, COL7A1, have been shown to underlie DEB (Christiano et al., 1994Christiano A.M. Ryynänen M. Uitto J. Dominant dystrophic epidermolysis bullosa: Identification of a Gly→Ser substitution in the triple helical domain of type VII collagen.Proc Natl Acad Sci USA. 1994; 91: 3549-3553Crossref PubMed Scopus (119) Google Scholar;Järvikallio et al., 1997Järvikallio A. Pulkkinen L. Uitto J. Molecular basis of dystrophic epidermolysis bullosa: Mutations in the type VII collagen gene (COL7A1).Hum Mutat. 1997; 10: 338-347Crossref PubMed Scopus (92) Google Scholar). So far, more than 100 COL7A1 mutations have been reported worldwide (Christiano et al., 1994Christiano A.M. Ryynänen M. Uitto J. Dominant dystrophic epidermolysis bullosa: Identification of a Gly→Ser substitution in the triple helical domain of type VII collagen.Proc Natl Acad Sci USA. 1994; 91: 3549-3553Crossref PubMed Scopus (119) Google Scholar, Christiano et al., 1995Christiano A.M. Morricone A. Paradisi M. Angelo C. Mazzanti C. Cavalieri R. Uitto J. A glycine-to-arginine substitution in the triple helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa.J Invest Dermatol. 1995; 104: 438-440Abstract Full Text PDF PubMed Scopus (51) Google ScholarChristiano et al., 1996aChristiano A.M. McGrath J.A. Uitto J. Influence of the second COL7A1 mutation in determining the phenotypic severity of recessive dystrophic epidermolysis bullosa.J Invest Dermatol. 1996; 106: 766-770Crossref PubMed Scopus (44) Google Scholar, Christiano et al., 1996bChristiano A.M. Bart B.J. Epstein E.H. Uitto J. Genetic basis of Bart’s syndrome: a glycine substitution mutation in the type VII collagen gene.J Invest Dermatol. 1996; 106: 1340-1342Crossref PubMed Scopus (27) Google Scholar;Hovnanian et al., 1997Hovnanian A. Rochat A. Bodemer C. et al.Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechansim underlying defective anchoring fibril formation.Am J Hum Genet. 1997; 61: 599-610Abstract Full Text PDF PubMed Scopus (139) Google Scholar;Järvikallio et al., 1997Järvikallio A. Pulkkinen L. Uitto J. Molecular basis of dystrophic epidermolysis bullosa: Mutations in the type VII collagen gene (COL7A1).Hum Mutat. 1997; 10: 338-347Crossref PubMed Scopus (92) Google Scholar). Most are family specific and the correlations between the clinical phenotype, the inheritance, and the mutation still remain in part elusive. Several missense mutations have been identified in the region of the amino acid residues 1994–2060 in the pro-α1(VII) chain that are encoded by exon 73 of COL7A1 (Christiano et al., 1995Christiano A.M. Morricone A. Paradisi M. Angelo C. Mazzanti C. Cavalieri R. Uitto J. A glycine-to-arginine substitution in the triple helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa.J Invest Dermatol. 1995; 104: 438-440Abstract Full Text PDF PubMed Scopus (51) Google Scholar, Christiano et al., 1996aChristiano A.M. McGrath J.A. Uitto J. Influence of the second COL7A1 mutation in determining the phenotypic severity of recessive dystrophic epidermolysis bullosa.J Invest Dermatol. 1996; 106: 766-770Crossref PubMed Scopus (44) Google Scholar;Hovnanian et al., 1997Hovnanian A. Rochat A. Bodemer C. et al.Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechansim underlying defective anchoring fibril formation.Am J Hum Genet. 1997; 61: 599-610Abstract Full Text PDF PubMed Scopus (139) Google Scholar;Järvikallio et al., 1997Järvikallio A. Pulkkinen L. Uitto J. Molecular basis of dystrophic epidermolysis bullosa: Mutations in the type VII collagen gene (COL7A1).Hum Mutat. 1997; 10: 338-347Crossref PubMed Scopus (92) Google Scholar;Winberg et al., 1997Winberg J.O. Hammami-Hauasli N. Nilssen O. et al.Modulation of disease severity of dystrophic epidermolysis bullosa by a splice site mutation in combination with a missense mutation in the COL7A1 gene.Hum Mol Genet. 1997; 6: 1125-1135Crossref PubMed Scopus (37) Google Scholar;Hammami-Hauasli et al., 1998Hammami-Hauasli N. Schumann H. Raghunath M. Kilgus O. Lüthi U. Luger T. Bruckner-Tuderman L. Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering.J Biol Chem. 1998; 272: 19228-19234Crossref Scopus (65) Google Scholar;Kon et al., 1998Kon A. Pulkkinen L. Ishida-Yamamoto A. Hashimoto I. Uitto J. Novel COL7A1 mutations in dystrophic forms of epidermolysis bullosa.J Invest Dermatol. 1998; 111: 534-537Abstract Full Text Full Text PDF PubMed Scopus (44) Google Scholar). 1Rouan F, Pulkkinen L, Jonkman MF, Uitto J: Novel and recurrent glycine substitution mutations in COL7A1 in dystrophic epidermolysis bullosa: genotype/phenotype correlations. J Invest Dermatol 110:508, 1998 (abstr.)1Rouan F, Pulkkinen L, Jonkman MF, Uitto J: Novel and recurrent glycine substitution mutations in COL7A1 in dystrophic epidermolysis bullosa: genotype/phenotype correlations. J Invest Dermatol 110:508, 1998 (abstr.) To determine whether exon 73 represents a gene region of mutational clustering or of putative hotspots, we examined 53 DEB families of mostly European origin for mutations in this exon. All patients fulfilled the clinical criteria of DEB (Fine et al., 1991Fine J.D. Bauer E.A. Briggaman R.A. et al.Revised clinical and laboratory criteria for subtypes of inherited epidermolysis bullosa: consensus report by the subcommittee on diagnosis and classification of the National Epidermolysis Bullosa Registry.J Am Acad Dermatol. 1991; 24: 119-135Abstract Full Text PDF PubMed Scopus (466) Google Scholar). The genomic DNA obtained from probands and immediate family members was screened according toChristiano et al., 1997Christiano A.M. Hoffman G.G. Zhang X. Xu Y. Tamai Y. Greenspan D.S. Uitto J. Strategy for identification of sequence variations in COL7A1, and a novel 2-bp deletion mutation in recessive dystrophic epidermolysis bullosa.Hum Mutat. 1997; 10: 408-414Crossref PubMed Scopus (102) Google Scholar utilizing heteroduplex analysis with conformation sensitive gel electrophoresis. The heteroduplex forming polymerase chain reaction products were examined by direct automated sequence analysis and verified by restriction enzyme digestion. In 15 of 53 DEB families (28%) a missense mutation was disclosed. We identified the novel transversion 6127G→T, designated G2043W, which occurred de novo in a dominant manner (Figure 1). The sequence variation did not represent a neutral polymorphism because it was not found in 150 normal chromosomes by SmaI digestion. In addition, we disclosed eight different recurrent point mutations, including five dominantly inherited amino acid substitutions, designated G2006D, G2015E, G2034W, G2034R, and G2043R, and two recessively inherited substitutions, designated R2008C and R2008G Table 1The inheritance of the point mutation G2009R remained unknown, because no parental DNA was available.Table 1Mutations in exon 73 of COL7A1 in 15 unrelated DEB families of this studyFamilyAgeDEB-subtypeInheritanceMutationSequencingVerificationHaplotypeReferenceEB-Thö5 ygeneralisataADG2006D6017G→AsequencingheterozygousHammami-Hauasli et al. 1998EB-Ram3 ylocalisataARR2008C6072C→TBsiE1homozygousKon et al., 1998Kon A. Pulkkinen L. Ishida-Yamamoto A. Hashimoto I. Uitto J. Novel COL7A1 mutations in dystrophic forms of epidermolysis bullosa.J Invest Dermatol. 1998; 111: 534-537Abstract Full Text Full Text PDF PubMed Scopus (44) Google ScholarEB-Al-K6 m?ARR2008C6072C→TBsiE1homozygousKon et al., 1998Kon A. Pulkkinen L. Ishida-Yamamoto A. Hashimoto I. Uitto J. Novel COL7A1 mutations in dystrophic forms of epidermolysis bullosa.J Invest Dermatol. 1998; 111: 534-537Abstract Full Text Full Text PDF PubMed Scopus (44) Google ScholarEB-79–125 ymutilans?R2008C6072C→TBsiE1heterozygousKon et al., 1998Kon A. Pulkkinen L. Ishida-Yamamoto A. Hashimoto I. Uitto J. Novel COL7A1 mutations in dystrophic forms of epidermolysis bullosa.J Invest Dermatol. 1998; 111: 534-537Abstract Full Text Full Text PDF PubMed Scopus (44) Google ScholarEB-Ser15 yinversaARR2008G6072C→GBsiE1homozygousHovnanian et al., 1997Hovnanian A. Rochat A. Bodemer C. et al.Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechansim underlying defective anchoring fibril formation.Am J Hum Genet. 1997; 61: 599-610Abstract Full Text PDF PubMed Scopus (139) Google ScholarEB-Kel14 ylocalisata?G2009R6073G→ADsaIheterozygousWinberg et al., 1997Winberg J.O. Hammami-Hauasli N. Nilssen O. et al.Modulation of disease severity of dystrophic epidermolysis bullosa by a splice site mutation in combination with a missense mutation in the COL7A1 gene.Hum Mol Genet. 1997; 6: 1125-1135Crossref PubMed Scopus (37) Google ScholarEB-Kuh7 ylocalisataADG2015E6044G→AsequencingheterozygousHammami-Hauasli et al. 1998EB-HapBe31 ylocalisataADG2034W6100G→TBstN1heterozygousFootnote 1EB-HapBj17 ylocalisataADG2034W6100G→TBstN1heterozygousFootnote 1EB-Cal64 ygeneralisataADG2034R6100G→AsequencingheterozygousHammami-Hauasli et al. 1998EB-Öst1 y??G2034R6100G→ABstN1heterozygousHammami-Hauasli et al. 1998EB-Fri29 ylocalisataAD, de novoG2043W6127G→TSmaIheterozygousThis studyEB-Sah32 ylocalisataADG2043R6127G→ASmaIheterozygousChristiano et al., 1995Christiano A.M. Morricone A. Paradisi M. Angelo C. Mazzanti C. Cavalieri R. Uitto J. A glycine-to-arginine substitution in the triple helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa.J Invest Dermatol. 1995; 104: 438-440Abstract Full Text PDF PubMed Scopus (51) Google ScholarEB-10–9825 ylocalisataADG2043R6127G→ASmaIheterozygousWinberg et al., 1997Winberg J.O. Hammami-Hauasli N. Nilssen O. et al.Modulation of disease severity of dystrophic epidermolysis bullosa by a splice site mutation in combination with a missense mutation in the COL7A1 gene.Hum Mol Genet. 1997; 6: 1125-1135Crossref PubMed Scopus (37) Google ScholarEB-Fec6 ylocalisata?G2043R6127G→ABsiE1heterozygousChristiano et al., 1995Christiano A.M. Morricone A. Paradisi M. Angelo C. Mazzanti C. Cavalieri R. Uitto J. A glycine-to-arginine substitution in the triple helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa.J Invest Dermatol. 1995; 104: 438-440Abstract Full Text PDF PubMed Scopus (51) Google Scholar Open table in a new tab Interestingly, the point mutations R2008C and G2043R were found in three different families each, and the point mutation G2034W in two families (Figure 2In concert with this, substitutions of the amino acid residues R2008, G2034, and G2043 have been repeatedly described in DEB patients of different ethnic backgrounds (Christiano et al., 1995Christiano A.M. Morricone A. Paradisi M. Angelo C. Mazzanti C. Cavalieri R. Uitto J. A glycine-to-arginine substitution in the triple helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa.J Invest Dermatol. 1995; 104: 438-440Abstract Full Text PDF PubMed Scopus (51) Google Scholar;Cserhalmi-Friedman et al., 1997Cserhalmi-Friedman P.B. Karpati S. Horvath A. Christiano A.M. Identification of the glycine to arginine substitution G2043R in the type VII collagen in a family with dominant dystrophic epidermolysis bullosa from Hungary.Exp Dermatol. 1997; 6: 303-307Crossref PubMed Scopus (15) Google Scholar;Hovnanian et al., 1997Hovnanian A. Rochat A. Bodemer C. et al.Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechansim underlying defective anchoring fibril formation.Am J Hum Genet. 1997; 61: 599-610Abstract Full Text PDF PubMed Scopus (139) Google Scholar;Winberg et al., 1997Winberg J.O. Hammami-Hauasli N. Nilssen O. et al.Modulation of disease severity of dystrophic epidermolysis bullosa by a splice site mutation in combination with a missense mutation in the COL7A1 gene.Hum Mol Genet. 1997; 6: 1125-1135Crossref PubMed Scopus (37) Google Scholar;Kon et al., 1998Kon A. Pulkkinen L. Ishida-Yamamoto A. Hashimoto I. Uitto J. Novel COL7A1 mutations in dystrophic forms of epidermolysis bullosa.J Invest Dermatol. 1998; 111: 534-537Abstract Full Text Full Text PDF PubMed Scopus (44) Google Scholar). 1Rouan F, Pulkkinen L, Jonkman MF, Uitto J: Novel and recurrent glycine substitution mutations in COL7A1 in dystrophic epidermolysis bullosa: genotype/phenotype correlations. J Invest Dermatol 110:508, 1998 (abstr.), 2Jonkman MF, Moreno G, Oranje AP, Pulkkinen L, Uitto J: Unusual dominant dystrophic epidermolysis bullosa phenotype caused by a novel glycine substitution mutation in the type VII collagen gene (COL7A1). J Invest Dermatol 110:511, 1998 (abstr.)2Jonkman MF, Moreno G, Oranje AP, Pulkkinen L, Uitto J: Unusual dominant dystrophic epidermolysis bullosa phenotype caused by a novel glycine substitution mutation in the type VII collagen gene (COL7A1). J Invest Dermatol 110:511, 1998 (abstr.) Consequently, the corresponding nucleotide positions 6072, 6100, 6127 of COL7A1 are likely to represent preferred locations for base-pair exchanges rather than mutations derived from common ancestors. The 53 DEB families were also tested for the presence of previously known common COL7A1 mutations in the exons 13, 70, 81, 104, and 116 by restriction enzyme digestion. These mutations were frequently found in either the Japanese (5818delC, 6573 + 1G→C, E2843X) 3Tamai K, Shikama I, Murai T et al. Japanese common mutations of the type VII collagen gene (COL7A1) in patients with recessive dystrophic epidermolysis bullosa (RDEB). J Invest Dermatol 108:648, 1997 (abstr.)3Tamai K, Shikama I, Murai T et al. Japanese common mutations of the type VII collagen gene (COL7A1) in patients with recessive dystrophic epidermolysis bullosa (RDEB). J Invest Dermatol 108:648, 1997 (abstr.) or the British population (R578X, 7786delG;Mellerio et al., 1997Mellerio J.E. Dunhill M.G.S. Allison W. et al.Recurrent mutations in the type VII collagen gene (COL7A1) in patients with recessive dystrophic epidermolysis bullosa.J Invest Dermatol. 1997; 109: 246-249Abstract Full Text PDF PubMed Scopus (49) Google Scholar). Only one DEB inversa patient in our collective was a heterozygous carrier of the substitution R578X in exon 13, indicating that these mutations are not common in a Central-European population. In summary, in this study we identified a missense mutation in exon 73 of COL7A1 in 28% of 53 unrelated DEB families. Addition of these gene defects to the previously published mutations yields a sum of 16 different gene defects in this exon of 201 bp. This large number of mutations, especially at some preferred nucleotide positions, suggests a gene region with high mutational frequency. Thus, it appears that exon 73 should be analyzed with priority by mutation screening of DEB patients. This knowledge is useful for accelerated mutation analysis of the COL7A1 gene, as well as for genetic counselling of DEB families with risk of recurrence. The authors thank Margit Schubert and Michaela Floeth for expert assistance and Dr. Alain Hovnanian and Dr. Anavaj Sakuntabhai for help with the Southern blot analysis. The authors’ work was supported by grants Br 1475/1–2 and 2–3 from the Deutsche Forschungsgemeinschaft, by the EU contract Nr. BMH-4–97–2559 and by DEBRA U.K." @default.
• W146580823 created "2016-06-24" @default.
• W146580823 creator A5021473670 @default.
• W146580823 creator A5031299889 @default.
• W146580823 creator A5037712860 @default.
• W146580823 creator A5043072143 @default.
• W146580823 creator A5051433279 @default.
• W146580823 creator A5062211678 @default.
• W146580823 creator A5083220847 @default.
• W146580823 date "1999-03-01" @default.
• W146580823 modified "2023-10-02" @default.
• W146580823 title "Clustering of COL7A1 Mutations in Exon 73: Implications for Mutation Analysis in Dystrophic Epidermolysis Bullosa" @default.
• W146580823 cites W1552753876 @default.
• W146580823 cites W1965256975 @default.
• W146580823 cites W1973769892 @default.
• W146580823 cites W2015665533 @default.
• W146580823 cites W2020248762 @default.
• W146580823 cites W2021859278 @default.
• W146580823 cites W2034272829 @default.
• W146580823 cites W2065050072 @default.
• W146580823 cites W2067756121 @default.
• W146580823 cites W2082879855 @default.
• W146580823 cites W2100524190 @default.
• W146580823 cites W2114077263 @default.
• W146580823 cites W2115774235 @default.
• W146580823 cites W2766519045 @default.
• W146580823 doi "https://doi.org/10.1046/j.1523-1747.1999.00518.x" @default.
• W146580823 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10084325" @default.
• W146580823 hasPublicationYear "1999" @default.
• W146580823 type Work @default.
• W146580823 sameAs 146580823 @default.
• W146580823 citedByCount "34" @default.
• W146580823 countsByYear W1465808232012 @default.
• W146580823 countsByYear W1465808232013 @default.
• W146580823 countsByYear W1465808232014 @default.
• W146580823 countsByYear W1465808232015 @default.
• W146580823 countsByYear W1465808232016 @default.
• W146580823 countsByYear W1465808232020 @default.
• W146580823 countsByYear W1465808232021 @default.
• W146580823 countsByYear W1465808232023 @default.
• W146580823 crossrefType "journal-article" @default.
• W146580823 hasAuthorship W146580823A5021473670 @default.
• W146580823 hasAuthorship W146580823A5031299889 @default.
• W146580823 hasAuthorship W146580823A5037712860 @default.
• W146580823 hasAuthorship W146580823A5043072143 @default.
• W146580823 hasAuthorship W146580823A5051433279 @default.
• W146580823 hasAuthorship W146580823A5062211678 @default.
• W146580823 hasAuthorship W146580823A5083220847 @default.
• W146580823 hasBestOaLocation W1465808231 @default.
• W146580823 hasConcept C104317684 @default.
• W146580823 hasConcept C16005928 @default.
• W146580823 hasConcept C2776559720 @default.
• W146580823 hasConcept C2781207856 @default.
• W146580823 hasConcept C36823959 @default.
• W146580823 hasConcept C501734568 @default.
• W146580823 hasConcept C54355233 @default.
• W146580823 hasConcept C71924100 @default.
• W146580823 hasConcept C86803240 @default.
• W146580823 hasConceptScore W146580823C104317684 @default.
• W146580823 hasConceptScore W146580823C16005928 @default.
• W146580823 hasConceptScore W146580823C2776559720 @default.
• W146580823 hasConceptScore W146580823C2781207856 @default.
• W146580823 hasConceptScore W146580823C36823959 @default.
• W146580823 hasConceptScore W146580823C501734568 @default.
• W146580823 hasConceptScore W146580823C54355233 @default.
• W146580823 hasConceptScore W146580823C71924100 @default.
• W146580823 hasConceptScore W146580823C86803240 @default.
• W146580823 hasIssue "3" @default.
• W146580823 hasLocation W1465808231 @default.
• W146580823 hasLocation W1465808232 @default.
• W146580823 hasOpenAccess W146580823 @default.
• W146580823 hasPrimaryLocation W1465808231 @default.
• W146580823 hasRelatedWork W1970350365 @default.
• W146580823 hasRelatedWork W1978980070 @default.
• W146580823 hasRelatedWork W2039900325 @default.
• W146580823 hasRelatedWork W2047503396 @default.
• W146580823 hasRelatedWork W2096004943 @default.
• W146580823 hasRelatedWork W2403763997 @default.
• W146580823 hasRelatedWork W2405375092 @default.
• W146580823 hasRelatedWork W2413806815 @default.
• W146580823 hasRelatedWork W3032620360 @default.
• W146580823 hasRelatedWork W3203316275 @default.
• W146580823 hasVolume "112" @default.
• W146580823 isParatext "false" @default.
• W146580823 isRetracted "false" @default.
• W146580823 magId "146580823" @default.
• W146580823 workType "article" @default.