Cargando…
Interleukin-1 Stimulates ADAM17 through a Mechanism Independent of its Cytoplasmic Domain or Phosphorylation at Threonine 735
ADAM17 (a disintegrin and metalloproteinase) is a membrane-anchored metalloproteinase that regulates the release of EGFR-ligands, TNFα and other membrane proteins from cells. ADAM17 can be rapidly activated by a variety of signaling pathways, yet little is known about the underlying mechanism. Sever...
Autores principales: | Hall, Katherine C., Blobel, Carl P. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3288042/ https://www.ncbi.nlm.nih.gov/pubmed/22384041 http://dx.doi.org/10.1371/journal.pone.0031600 |
Ejemplares similares
-
New insights into the phosphorylation of the threonine motif of the β1 integrin cytoplasmic domain
por: Böttcher, Ralph T, et al.
Publicado: (2022) -
Targeted truncation of the ADAM17 cytoplasmic domain in mice results in protein destabilization and a hypomorphic phenotype
por: Lora, Jose, et al.
Publicado: (2021) -
ADAM17 cytoplasmic domain modulates Thioredoxin-1 conformation and activity
por: e Costa, Rute A.P., et al.
Publicado: (2020) -
Analysis of the Conditions That Affect the Selective Processing of Endogenous Notch1 by ADAM10 and ADAM17
por: Alabi, Rolake O., et al.
Publicado: (2021) -
Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
por: Sahin, Umut, et al.
Publicado: (2004)