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Ting Xiao, Xiuci Liang, Hailan Liu, Feng Zhang, Wen Meng, and Fang Hu

( Haynes et al . 2007 , Broadley & Hartl 2008 , Haynes & Ron 2010 , Hu & Liu 2011 ). HSP60, an important mitochondrial stress protein, has been shown to play key roles in the protein synthesis, folding, and delivery of misfolded proteins to proteolytic

Open access

Hyon-Seung Yi, Joon Young Chang, and Minho Shong

( Aldridge et al . 2007 ). In this context, the mitochondrial chaperone systems are required for facilitating protein-folding within the mitochondria ( Fig. 3 ). While HSP60 plays a prominent role in the UPR mt response, other mitochondrial chaperones are

Free access

I Paron, C D’Ambrosio, A Scaloni, M T Berlingieri, P L Pallante, A Fusco, N Bivi, G Tell, and G Damante

chaperone or chaperone-like activities were found to be significantly altered. Particularly, two members of the heat-shock protein family, Hsp90-beta and Hsp60, were found to be significantly increased. Hsp90-beta upregulation is very important for p53

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Jin-Seung Choung, Young-Sun Lee, and Hee-Sook Jun

(ab 54481, Abcam), HSP60 (ab 46798, Abcam) or β-actin (sc-47778, Santa Cruz Biotechnology) antibody. Membranes were then incubated with horseradish peroxidase-conjugated goat anti-rabbit IgG (sc-2004, Santa Cruz Biotechnology) or goat anti-mouse IgG