Cargando…
Mutational analysis of the membrane-proximal cleavage site of L- selectin: relaxed sequence specificity surrounding the cleavage site
L-selectin expression is regulated in part by membrane-proximal cleavage from the cell surface of leukocytes and L-selectin-transfected cells. The downregulation of L-selectin from the surface of neutrophils is speculated to be a process involved in the adhesion cascade leading to neutrophil recruit...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1995
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192138/ https://www.ncbi.nlm.nih.gov/pubmed/7543142 |
Ejemplares similares
-
Membrane proximal cleavage of L-selectin: identification of the cleavage site and a 6-kD transmembrane peptide fragment of L-selectin
Publicado: (1994) -
Active Site Mutations Change the Cleavage Specificity of Neprilysin
por: Sexton, Travis, et al.
Publicado: (2012) -
The relaxed requirements of the integron cleavage site allow predictable changes in integron target specificity
por: Frumerie, Clara, et al.
Publicado: (2010) -
Role of sequence and position of the cleavage sites in prothrombin activation
por: Stojanovski, Bosko M., et al.
Publicado: (2021) -
Analysing Point Mutations in Protein Cleavage Sites by Using Enzyme Specificity Matrices
por: Triebel, Jakob, et al.
Publicado: (2019)