Cargando…
Cell Entry of Arginine-rich Peptides Is Independent of Endocytosis
Arginine-rich peptides are a subclass of cell-penetrating peptides that are taken up by living cells and can be detected freely diffusing inside the cytoplasm and nucleoplasm. This phenomenon has been attributed to either an endocytic mode of uptake and a subsequent release from vesicles or to direc...
Autores principales: | Ter-Avetisyan, Gohar, Tünnemann, Gisela, Nowak, Danny, Nitschke, Matthias, Herrmann, Andreas, Drab, Marek, Cardoso, M. Cristina |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2009
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2635027/ https://www.ncbi.nlm.nih.gov/pubmed/19047062 http://dx.doi.org/10.1074/jbc.M805550200 |
Ejemplares similares
-
Subunit Organization in the TatA Complex of the Twin Arginine Protein Translocase: A SITE-DIRECTED EPR SPIN LABELING STUDY
por: White, Gaye F., et al.
Publicado: (2010) -
Steroidogenic Activity of StAR Requires Contact with Mitochondrial VDAC1 and Phosphate Carrier Protein
por: Bose, Mahuya, et al.
Publicado: (2008) -
Identification of Pore Residues Engaged in Determining Divalent Cationic
Permeation in Transient Receptor Potential Melastatin Subtype Channel
2
por: Xia, Rong, et al.
Publicado: (2008) -
Time-resolved Mechanism of Extracellular Gate Opening and Substrate
Binding in a Glutamate
Transporter
por: Shrivastava, Indira H., et al.
Publicado: (2008) -
The Reticulon and Dp1/Yop1p Proteins Form Immobile Oligomers in the Tubular Endoplasmic Reticulum
por: Shibata, Yoko, et al.
Publicado: (2008)