Cargando…
The Human PDZome 2.0: Characterization of a New Resource to Test for PDZ Interactions by Yeast Two-Hybrid
PSD95-disc large-zonula occludens (PDZ) domains are globular modules of 80–90 amino acids that co-evolved with multicellularity. They commonly bind to carboxy-terminal sequences of a plethora of membrane-associated proteins and influence their trafficking and signaling. We previously built a PDZ res...
Autores principales: | Castro-Cruz, Monica, Lembo, Frédérique, Borg, Jean-Paul, Travé, Gilles, Vincentelli, Renaud, Zimmermann, Pascale |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10456741/ https://www.ncbi.nlm.nih.gov/pubmed/37623798 http://dx.doi.org/10.3390/membranes13080737 |
Ejemplares similares
-
The Human PDZome: A Gateway to PSD95-Disc Large-Zonula Occludens (PDZ)-mediated Functions
por: Belotti, Edwige, et al.
Publicado: (2013) -
Interactomic affinity profiling by holdup assay: Acetylation and distal residues impact the PDZome-binding specificity of PTEN phosphatase
por: Jané, Pau, et al.
Publicado: (2020) -
Prevalence, Specificity and Determinants of Lipid-Interacting PDZ Domains from an In-Cell Screen and In Vitro Binding Experiments
por: Ivarsson, Ylva, et al.
Publicado: (2013) -
Proteomic peptide phage display uncovers novel interactions of the PDZ1‐2 supramodule of syntenin
por: Garrido‐Urbani, Sarah, et al.
Publicado: (2016) -
An RNA Aptamer Targets the PDZ-Binding Motif of the HPV16 E6 Oncoprotein
por: Belyaeva, Tamara A., et al.
Publicado: (2014)