Immunohistochemical and mutation analyses demonstrate that procollagen VII is processed to collagen VII through removal of the NC-2 domain. - sprookjes - yvandenbroek - TriplyDB

Immunohistochemical and mutation analyses demonstrate that procollagen VII is processed to collagen VII through removal of the NC-2 domain.

Immunohistochemical and mutation analyses demonstrate that procollagen VII is processed to collagen VII through removal of the NC-2 domain.

http://www.wikidata.org/entity/Q36382726

about

Digenic junctional epidermolysis bullosa: mutations in COL17A1 and LAMB3 genes.Three novel homozygous point mutations and a new polymorphism in the COL17A1 gene: relation to biological and clinical phenotypes of junctional epidermolysis bullosa Dystrophic epidermolysis bullosa: a review Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen Interactions of the amino-terminal noncollagenous (NC1) domain of type VII collagen with extracellular matrix components. A potential role in epidermal-dermal adherence in human skin High frequency of the 425A-->G splice-site mutation and novel mutations of the COL7A1 gene in central Europe: significance for future mutation detection strategies in dystrophic epidermolysis bullosa Two forms of collagen XVII in keratinocytes. A full-length transmembrane protein and a soluble ectodomain Mutation analysis and characterization of COL7A1 mutations in dystrophic epidermolysis bullosa Collagen XVII is destabilized by a glycine substitution mutation in the cell adhesion domain Col15 Collagen XXVIII, a novel von Willebrand factor A domain-containing protein with many imperfections in the collagenous domain Generalized dystrophic epidermolysis bullosa: identification of a novel, homozygous glycine substitution, G2031S, in exon 73 of COL7A1 in monozygous triplets.Some, but not all, glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils, and skin blistering.Mechanisms of fibroblast cell therapy for dystrophic epidermolysis bullosa: high stability of collagen VII favors long-term skin integrity Basement membrane zone type XV collagen is a disulfide-bonded chondroitin sulfate proteoglycan in human tissues and cultured cells.Prevalence of collagen VII-specific autoantibodies in patients with autoimmune and inflammatory diseases Blister-inducing antibodies target multiple epitopes on collagen VII in mice.Keratinocytes from patients lacking collagen XVII display a migratory phenotype Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechanisms underlying defective anchoring fibril formation.Metalloproteinases in Drosophila to humans that are central players in developmental processes.The shed ectodomain of collagen XVII/BP180 is targeted by autoantibodies in different blistering skin diseases.Compound heterozygosity for missense (L156P) and nonsense (R554X) mutations in the beta4 integrin gene (ITGB4) underlies mild, nonlethal phenotype of epidermolysis bullosa with pyloric atresia.A hypomorphic mouse model of dystrophic epidermolysis bullosa reveals mechanisms of disease and response to fibroblast therapy.Experimental models of epidermolysis bullosa acquisita.The bone morphogenetic protein 1/Tolloid-like metalloproteinases Global remodelling of cellular microenvironment due to loss of collagen VII.Cross-linking of the dermo-epidermal junction of skin regenerating from keratinocyte autografts. Anchoring fibrils are a target for tissue transglutaminase.Gene therapy: pursuing restoration of dermal adhesion in recessive dystrophic epidermolysis bullosa.The recombinant expression of full-length type VII collagen and characterization of molecular mechanisms underlying dystrophic epidermolysis bullosa.Analysis of the functional consequences of targeted exon deletion in COL7A1 reveals prospects for dystrophic epidermolysis bullosa therapy.Characterization of molecular mechanisms underlying mutations in dystrophic epidermolysis bullosa using site-directed mutagenesis.High Local Concentrations of Intradermal MSCs Restore Skin Integrity and Facilitate Wound Healing in Dystrophic Epidermolysis Bullosa.Dominant-negative effects of COL7A1 mutations can be rescued by controlled overexpression of normal collagen VII.Supramolecular interactions in the dermo-epidermal junction zone: anchoring fibril-collagen VII tightly binds to banded collagen fibrils Autoantibodies to type VII collagen mediate Fcgamma-dependent neutrophil activation and induce dermal-epidermal separation in cryosections of human skin.Tissue-specific expression and long-term deposition of human collagen VII in the skin of transgenic mice: implications for gene therapy.The carboxyl terminus of type VII collagen mediates antiparallel dimer formation and constitutes a new antigenic epitope for epidermolysis Bullosa acquisita autoantibodies.Stable integration of large (>100 kb) PAC constructs in HaCaT keratinocytes using an integrin-targeting peptide delivery system.Dohi memorial lecture. Clinical implications of basic research on heritable skin diseases.Development and characterization of a recombinant truncated type VII collagen "minigene". Implication for gene therapy of dystrophic epidermolysis bullosa.Blistering skin diseases: models for studies on epidermal-dermal adhesion.

P2860

Q24534377-8F565068-D88A-41F1-9313-084F40A278A2 Q24676917-2D739F9F-3497-45BD-9AFC-F78AA2801D2F Q28084871-5A734FE7-4DD7-466A-A78C-28300ADC51ED Q28216359-D6C24619-0DEA-446D-B312-2FBFC8C729F3 Q28239509-D95833F2-4937-407C-90CB-9B86673CEDA5 Q28250077-60EDEF64-10D1-47C3-955D-3E0987B1B759 Q28283395-FAB93C43-E934-4E5B-B105-70CA53270C80 Q28284115-C69C841B-00BF-4B38-A54A-81B326970B8B Q28369420-0226D09E-0C3B-437F-8174-446D95E61010 Q28510535-BBCC3932-56DE-4B72-B72D-C5A99B2494DA Q31892676-93F5DDEE-567B-4552-A292-6C783D7CCBBF Q32052839-4A57B036-C648-4A4A-8CB6-BAC8BD0A9A94 Q33713926-2BF7CE89-2DC6-4E2E-9EAA-6E2A1FE8A5D9 Q33900267-03AE1A34-D058-4E11-A89B-003D1801B31C Q34218525-E8CA3E65-E193-49A9-A0E3-0C796B4AE2EB Q34336809-3CE4FA72-D6A7-4855-AAC1-6FA23305B1A8 Q35098451-0CC09273-B43E-42D9-84FA-969FDCECC1A6 Q35249597-413C00D6-C537-413A-816F-FA06A885CBDF Q35604976-FCF665E7-2551-481C-B125-EFADF97E2B23 Q35745439-50D9CC1E-9E28-4B53-8E94-8D46FC24C31C Q35764527-4042D185-5DE7-4C2C-B3D9-DE82ADC1600E Q36512219-29B4F93E-9BFC-49DB-84D2-272EA224BFBE Q36828943-E3A73DDB-1647-485F-A248-890975FB4E5D Q36846125-C5241F14-F8E2-4033-8446-041513C629AD Q36856682-DA18CA77-2145-4613-B08C-216F9D1280D8 Q37359299-F90798E1-F102-4745-B843-ED56C7B9EAEA Q38150897-D7839A69-9F4F-4EFE-92F7-73E2475AFB82 Q38294958-8AD20FD1-4F95-43DF-A151-68B8F03E1869 Q38772377-4D16FFA0-255A-44A8-B2D0-96E58C4C1EE5 Q39599980-1D774CA9-41AF-4D82-BEDF-79D27A2FFA55 Q39789694-13EA2019-C991-484D-AB1D-457E23EDF81C Q39804335-67422262-65E1-4E20-92D3-EBA1DD828C17 Q40454600-48888B81-DBDC-4403-8727-E793CAE9AB30 Q40719797-22BD3692-89BE-4AEF-8FCE-8BAB0FA311ED Q40738230-B4627364-722A-4040-8D9A-4156BFA8BCF6 Q40817995-1A1E747F-9E99-484D-AECF-452656C6B357 Q40850934-A077BE85-F370-476D-85D6-CCB1AF618609 Q40872692-80F12704-C078-42EC-A667-BC29A8713806 Q40878358-956491F9-F649-43BD-9DD1-2110428E8B13 Q41481751-942302B7-B178-497E-B2C0-1823EEBBB57D

P2860

Immunohistochemical and mutation analyses demonstrate that procollagen VII is processed to collagen VII through removal of the NC-2 domain.

http://www.wikidata.org/entity/Q36382726

description

1995 nî lūn-bûn

@nan

1995年の論文

@ja

1995年学术文章

@wuu

1995年学术文章

@zh-cn

1995年学术文章

@zh-hans

1995年学术文章

@zh-my

1995年学术文章

@zh-sg

1995年學術文章

@yue

1995年學術文章

@zh

1995年學術文章

@zh-hant

name

Immunohistochemical and mutati ...... gh removal of the NC-2 domain.

@ast

Immunohistochemical and mutati ...... gh removal of the NC-2 domain.

@en

type

label

Immunohistochemical and mutati ...... gh removal of the NC-2 domain.

@ast

Immunohistochemical and mutati ...... gh removal of the NC-2 domain.

@en

prefLabel

Immunohistochemical and mutati ...... gh removal of the NC-2 domain.

@ast

Immunohistochemical and mutati ...... gh removal of the NC-2 domain.

@en

P1433

Q36382726-B447BA2C-354F-44E1-A739-33217D7466EC

P1476

Q36382726-62FDDC58-3261-4CD0-ADF3-BB7A2AE4B102

P2093

Q36382726-03B46ECC-6A2C-4ADA-A667-C486F8DDCF25

Q36382726-094313A2-7C65-42F7-882E-4F0D46644193

Q36382726-1F4187D9-DFA8-4136-8753-95CE626CABBC

Q36382726-518F8B4C-9C03-4E4F-91E2-A60B6A761C89

Q36382726-846F085D-126B-41D5-87BF-95BA081017AF

Q36382726-8D3FE808-DC4D-4E9A-B9C1-995F373E3245

Q36382726-D0DD7687-C591-48E7-84CA-584E36ED9988

P2860

Q36382726-184BB0D0-DB26-4E97-B417-DB4D38AC31CB

Q36382726-1E3B3659-C7A5-413F-8ED0-8A85582898F3

Q36382726-32007039-4247-47F2-84C1-0B5C0E7D5291

Q36382726-39F53082-CE01-414F-BD82-25CDF4DE1CB4

Q36382726-424F5D1D-7C84-4C12-8CBA-B269152AEF17

Q36382726-4D1666DD-85C2-45F0-B3B5-E611DA1DB7C1

Q36382726-533964E9-564B-4926-A3E0-236C16505B7F

Q36382726-657B887C-3E0B-4D97-8B65-F9191A90C3FF

Q36382726-6983C4F8-9AE2-4F86-913F-CA1926FC1040

Q36382726-8F8BE1C2-8A17-4179-A35D-F38BDA844FAE

P304

Q36382726-0397BD4C-EFBA-4EF5-830E-79DBB228D710

P31

Q36382726-CDB2F3FA-EDC8-467D-A669-2C249371F518

P356

Q36382726-384BB6E5-9A65-4C8A-9C77-D9CB06F414AE

P407

Q36382726-DD6037DD-2E4A-4262-9375-27F0FDF2EB85

P433

Q36382726-B82CE8B9-68EA-43CB-A693-468BB9CEFF58

P478

Q36382726-056B187D-6A11-4E96-92DB-F58714AC0CF5

P577

Q36382726-F3C3AEB6-5608-4165-A2C4-7152DE7C26E2

P698

Q36382726-B918325E-6A8F-4DB8-A637-F89E444FD4C4

P921

Q36382726-F91506C4-1AF5-487B-A156-93B2EA0F42B6

P932

Q36382726-FE19DE95-A070-479B-9949-6999A1360C0F

P356

P1433

Journal of Cell Biology

P1476

Immunohistochemical and mutati ...... gh removal of the NC-2 domain.

@en

P2093

Bruckner-Tuderman L

http://www.w3.org/2001/XMLSchema#string

Dours-Zimmermann MT

http://www.w3.org/2001/XMLSchema#string

Gedde-Dahl T Jr

http://www.w3.org/2001/XMLSchema#string

Kalinke DU

http://www.w3.org/2001/XMLSchema#string

Nilssen O

http://www.w3.org/2001/XMLSchema#string

Winberg JO

http://www.w3.org/2001/XMLSchema#string

Zimmermann DR

http://www.w3.org/2001/XMLSchema#string

P2860

Molecular characterization of a karyophilic, histone-binding protein: cDNA cloning, amino acid sequence and expression of nuclear protein N1/N2 of Xenopus laevis.

Epithelial origin of cutaneous anchoring fibrils

Cloning of human type VII collagen. Complete primary sequence of the alpha 1(VII) chain and identification of intragenic polymorphisms

Structural organization of the human type VII collagen gene (COL7A1), composed of more exons than any previously characterized gene

The carboxyl-terminal half of type VII collagen, including the non-collagenous NC-2 domain and intron/exon organization of the corresponding region of the COL7A1 gene

A missense mutation in type VII collagen in two affected siblings with recessive dystrophic epidermolysis bullosa

Type I procollagen carboxyl-terminal proteinase from chick embryo tendons. Purification and characterization

Type VII collagen, anchoring fibrils, and epidermolysis bullosa.

Type I procollagen C-proteinase from mouse fibroblasts. Purification and demonstration of a 55-kDa enhancer glycoprotein.

Transforming growth factor-beta stimulates collagen VII expression by cutaneous cells in vitro

P304

551-559

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1083/JCB.131.2.551

http://www.w3.org/2001/XMLSchema#string

P407

P433

2

http://www.w3.org/2001/XMLSchema#string

P478

131

http://www.w3.org/2001/XMLSchema#string

P577

1995-10-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

7593178

http://www.w3.org/2001/XMLSchema#string

P921

immunohistochemistry

P932

2199977

http://www.w3.org/2001/XMLSchema#string