Cargando…
The dynamic interactome of human Aha1 upon Y223 phosphorylation
Heat Shock Protein 90 (Hsp90) is an essential chaperone that supports the function of a wide range of signaling molecules. Hsp90 binds to a suite of co-chaperone proteins that regulate Hsp90 function through alteration of intrinsic ATPase activity. Several studies have determined Aha1 to be an impor...
Autores principales: | Wolfgeher, Donald, Dunn, Diana M., Woodford, Mark R., Bourboulia, Dimitra, Bratslavsky, Gennady, Mollapour, Mehdi, Kron, Stephen J., Truman, Andrew W. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4659802/ https://www.ncbi.nlm.nih.gov/pubmed/26693507 http://dx.doi.org/10.1016/j.dib.2015.10.028 |
Ejemplares similares
-
c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells
por: Dunn, Diana M., et al.
Publicado: (2015) -
The quantitative changes in the yeast Hsp70 and Hsp90 interactomes upon DNA damage
por: Truman, Andrew W., et al.
Publicado: (2014) -
Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors
por: Woodford, Mark R., et al.
Publicado: (2016) -
Extracellular Phosphorylation of TIMP-2 by Secreted c-Src Tyrosine Kinase Controls MMP-2 Activity
por: Sánchez-Pozo, Javier, et al.
Publicado: (2018) -
Epichaperomics reveals dysfunctional chaperone protein networks
por: Woodford, Mark R., et al.
Publicado: (2023)