Cargando…
Phosphoproteomic analysis reveals major default phosphorylation sites outside long intrinsically disordered regions of Arabidopsis plasma membrane proteins
BACKGROUND: Genome-wide statistics established that long intrinsically disordered regions (over 30 residues) are predicted in a large part of proteins in all eukaryotes, with a higher ratio in trans-membrane proteins. At functional level, such unstructured and flexible regions were suggested for yea...
Autores principales: | Nespoulous, Claude, Rofidal, Valérie, Sommerer, Nicolas, Hem, Sonia, Rossignol, Michel |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2012
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3537754/ https://www.ncbi.nlm.nih.gov/pubmed/23110452 http://dx.doi.org/10.1186/1477-5956-10-62 |
Ejemplares similares
-
Functional phosphoproteomic profiling of phosphorylation sites in membrane fractions of salt-stressed Arabidopsis thaliana
por: Hsu, Jue-Liang, et al.
Publicado: (2009) -
Integrating Phosphoproteomics and Bioinformatics to Study Brassinosteroid-Regulated Phosphorylation Dynamics in Arabidopsis
por: Lin, Li-Ling, et al.
Publicado: (2015) -
Excreted/Secreted Proteins from Trypanosome Procyclic Strains
por: Atyame Nten, Celestine Michelle, et al.
Publicado: (2010) -
Phosphoproteomics reveals extensive in vivo phosphorylation of Arabidopsis proteins involved in RNA metabolism
por: la Fuente van Bentem, Sergio de, et al.
Publicado: (2006) -
Conservation of kinase-phosphorylation site pairings: Evidence for an evolutionarily dynamic phosphoproteome
por: McDonald, Megan, et al.
Publicado: (2018)