Cargando…
Identification of in vivo HSP90-interacting proteins reveals modularity of HSP90 complexes is dependent on the environment in psychrophilic bacteria
Heat shock protein 90 (HSP90) is a conserved molecular chaperone that functions as part of complexes in which different client proteins target it to diverse sets of substrates. In this paper, HSP90 complexes were investigated in γ-proteobacteria from mild (Shewanella oneidensis) and cold environment...
Autores principales: | García-Descalzo, Laura, Alcazar, Alberto, Baquero, Fernando, Cid, Cristina |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3059794/ https://www.ncbi.nlm.nih.gov/pubmed/20890740 http://dx.doi.org/10.1007/s12192-010-0233-7 |
Ejemplares similares
-
Modularity and Intrinsic Evolvability of Hsp90-Buffered Change
por: Carey, Charles C., et al.
Publicado: (2006) -
Y‐632 inhibits heat shock protein 90 (Hsp90) function by disrupting the interaction between Hsp90 and Hsp70/Hsp90 organizing protein, and exerts antitumor activity in vitro and in vivo
por: Wang, Wenqian, et al.
Publicado: (2016) -
The ‘active life’ of Hsp90 complexes()
por: Prodromou, Chrisostomos
Publicado: (2012) -
Circulating heat shock protein 90 (Hsp90) and autoantibodies to Hsp90 are increased in patients with atopic dermatitis
por: Sitko, Krzysztof, et al.
Publicado: (2021) -
Hsp90 Inhibitors Prevent HSV-1 Replication by Directly Targeting UL42-Hsp90 Complex
por: Qin, Shurong, et al.
Publicado: (2022)