Cargando…
Low Stability of Integrin-Binding Deficient Mutant of FGF1 Restricts Its Biological Activity
Fibroblast growth factor 1 (FGF1) has been shown to interact with integrin α(v)β(3) through a specific binding site, involving Arg35 residue. The FGF1 mutant (R35E) with impaired integrin binding was found to be defective in its proliferative response, although it was still able to interact with FGF...
Autores principales: | Szlachcic, Anna, Sochacka, Martyna, Czyrek, Aleksandra, Opalinski, Lukasz, Krowarsch, Daniel, Otlewski, Jacek, Zakrzewska, Malgorzata |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6721657/ https://www.ncbi.nlm.nih.gov/pubmed/31443196 http://dx.doi.org/10.3390/cells8080899 |
Ejemplares similares
-
FGF12 is a novel component of the nucleolar NOLC1/TCOF1 ribosome biogenesis complex
por: Sochacka, Martyna, et al.
Publicado: (2022) -
FHF1 is a bona fide fibroblast growth factor that activates cellular signaling in FGFR-dependent manner
por: Sochacka, Martyna, et al.
Publicado: (2020) -
Increased Protein Stability of FGF1 Can Compensate for Its Reduced Affinity for Heparin
por: Zakrzewska, Malgorzata, et al.
Publicado: (2009) -
FGF1 protects FGFR1-overexpressing cancer cells against drugs targeting tubulin polymerization by activating AKT via two independent mechanisms
por: Szymczyk, Jakub, et al.
Publicado: (2022) -
FGF2 Dual Warhead Conjugate with Monomethyl Auristatin E and α-Amanitin Displays a Cytotoxic Effect towards Cancer Cells Overproducing FGF Receptor 1
por: Świderska, Karolina Weronika, et al.
Publicado: (2018)