Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function.

about

Validation of ADAM10 metalloprotease as a Bacillus thuringiensis Cry3Aa toxin functional receptor in Colorado potato beetle (Leptinotarsa decemlineata).Activation of cell-surface proteases promotes necroptosis, inflammation and cell migration.

P2860

Q39130777-0C8F9238-3979-4862-95BA-327C0A675AFF Q42032616-2F1A35BB-3657-47F5-9EAA-FB0BD509A4BB

P2860

Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function.

Item

http://www.wikidata.org/entity/Q38042836

description

article científic

@ca

article scientifique

@fr

articol științific

@ro

articolo scientifico

@it

artigo científico

@gl

artigo científico

@pt

artigo científico

@pt-br

artikel ilmiah

@id

artikull shkencor

@sq

artículo científico

@es

name

Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function.

@en

type

Item

label

Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function.

@en

prefLabel

Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function.

@en

P1476

Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function.

@en

P2093

Karina Reiss

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

Sucharit Bhakdi

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

P2860

The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion

The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts

Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding.

P2X(7) receptor and macrophage function

A common fold mediates vertebrate defense and bacterial attack

Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense

Extracellular adenosine 5'-triphosphate induces a loss of CD23 from human dendritic cells via activation of P2X7 receptors

The transmembrane CXC-chemokine ligand 16 is induced by IFN-gamma and TNF-alpha and shed by the activity of the disintegrin-like metalloproteinase ADAM10

The ADAM metalloproteinases

Coupling of two pools of P2X7 receptors to distinct intracellular signaling pathways in rat submandibular gland

P2888

s00430-012-0260-3

P304

419-426

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

P31

scholarly article

P356

10.1007/S00430-012-0260-3

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

P433

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

P478

201

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

P577

2012-09-13T00:00:00Z

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

P6179

1049649716

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

P698

22972233

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

Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function.

about

P2860

P2860

Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P6179

P698

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P6179

P698