GPI-anchored diphtheria toxin receptor allows membrane translocation of the toxin without detectable ion channel activity.

about

Viruses activate a genetically conserved cell death pathway in a unicellular organism Oligomerization of membrane-bound diphtheria toxin (CRM197) facilitates a transition to the open form and deep insertion Bacteria in cancer therapy: a novel experimental strategy.

P2860

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P2860

GPI-anchored diphtheria toxin receptor allows membrane translocation of the toxin without detectable ion channel activity.

Item

http://www.wikidata.org/entity/Q38361609

description

1996 nî lūn-bûn

@nan

1996年の論文

@ja

1996年学术文章

@wuu

1996年学术文章

@zh-cn

1996年学术文章

@zh-hans

1996年学术文章

@zh-my

1996年学术文章

@zh-sg

1996年學術文章

@yue

1996年學術文章

@zh

1996年學術文章

@zh-hant

name

GPI-anchored diphtheria toxin ...... tectable ion channel activity.

@en

type

Item

label

GPI-anchored diphtheria toxin ...... tectable ion channel activity.

@en

prefLabel

GPI-anchored diphtheria toxin ...... tectable ion channel activity.

@en

P1476

GPI-anchored diphtheria toxin ...... tectable ion channel activity.

@en

P2093

Lanzrein M

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

Sand O

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

P2860

Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches

A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF

The crystal structure of diphtheria toxin

Diphtheria toxin

Heparin-binding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity

Diphtheria toxin: mode of action and structure

Hypersensitivity to diphtheria toxin by mouse cells expressing both diphtheria toxin receptor and CD9 antigen

Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoluril

Expression of functional diphtheria toxin receptors on highly toxin-sensitive mouse cells that specifically bind radioiodinated toxin

Human immunodeficiency virus infection is efficiently mediated by a glycolipid-anchored form of CD4.

P304

725-734

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P31

scholarly article

P407

English

P433

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

P478

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

P50

Sjur Olsnes

P577

1996-02-01T00:00:00Z

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

P698

8631294

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P932

450271

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

GPI-anchored diphtheria toxin receptor allows membrane translocation of the toxin without detectable ion channel activity.

about

P2860

P2860

GPI-anchored diphtheria toxin receptor allows membrane translocation of the toxin without detectable ion channel activity.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P407

P433

P478

P50

P577

P698

P932

P1433

P1476

P2093

P2860

P304

P31

P407

P433

P478

P50

P577

P698

P932