Structural proteins of the dermal-epidermal junction targeted by autoantibodies in pemphigoid diseases.

Item

http://www.wikidata.org/entity/Q42514770

description

2017 nî lūn-bûn

@nan

2017年の論文

@ja

2017年学术文章

@wuu

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

@yue

2017年學術文章

@zh

2017年學術文章

@zh-hant

name

Structural proteins of the der ...... bodies in pemphigoid diseases.

@en

Structural proteins of the der ...... bodies in pemphigoid diseases.

@nl

type

Item

label

Structural proteins of the der ...... bodies in pemphigoid diseases.

@en

Structural proteins of the der ...... bodies in pemphigoid diseases.

@nl

prefLabel

Structural proteins of the der ...... bodies in pemphigoid diseases.

@en

Structural proteins of the der ...... bodies in pemphigoid diseases.

@nl

P1476

Structural proteins of the der ...... ibodies in pemphigoid diseases

@en

P2093

Detlef Zillikens

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

P2860

Form and function: the laminin family of heterotrimers

Crystal structure of the extracellular segment of integrin alpha Vbeta3

Analysis of the interactions between BP180, BP230, plectin and the integrin alpha6beta4 important for hemidesmosome assembly

The N terminus of the transmembrane protein BP180 interacts with the N-terminal domain of BP230, thereby mediating keratin cytoskeleton anchorage to the cell surface at the site of the hemidesmosome

Not just scaffolding: plectin regulates actin dynamics in cultured cells

Laminin isoforms containing the gamma3 chain are unable to bind to integrins due to the absence of the glutamic acid residue conserved in the C-terminal regions of the gamma1 and gamma2 chains

Binding of integrin alpha6beta4 to plectin prevents plectin association with F-actin but does not interfere with intermediate filament binding

Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin

Hemidesmosome formation is initiated by the beta4 integrin subunit, requires complex formation of beta4 and HD1/plectin, and involves a direct interaction between beta4 and the bullous pemphigoid antigen 180

The localization of bullous pemphigoid antigen 180 (BP180) in hemidesmosomes is mediated by its cytoplasmic domain and seems to be regulated by the beta4 integrin subunit

P304

1154-1162

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P31

scholarly article

P356

10.1111/EXD.13446

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

P433

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

P478

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

P50

Enno Schmidt

Stephanie Goletz

P577

2017-12-01T00:00:00Z

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

P698

28887824

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

P921

autoantibody