The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins.

By C. Dickey, A. Kamal, K. Lundgren, Natalia Klosak, Rachel M. Bailey, Judy H. Dunmore, Peter E. A. Ash, Sareh Shoraka, Jelena Zlatković, C. Eckman and 6 more. Journal of Clinical Investigation, 2007

645 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/1b0f960a0400491b8dc3b1d870644a2800b413dc

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. Susmita Kaushik
2. Esther Wong
3. A. Cuervo
4. E. Mandelkow
5. L. Mucke
6. N. Mizushima

In Molecular Biology

1. E. Masliah
2. A. Cuervo
3. E. Huang
4. William W. Seeley
5. E. Mandelkow
6. L. Mucke

Citations in the corpus

• Biochemistry and cell biology of tau protein in neurofibrillary degeneration. (2012, neutral): “involved Dickey et al. (2007); Tortosa”
• Acetylation of tau inhibits its degradation and contributes to tauopathy. (2010, positive): “These results suggest that deacetylation preferentially enhances degradation of p-tau, consistent with the observation that p-tau species are selectively degraded via the UPS pathway (Dickey et al., 2007; Dickey et al., 2006).”
• The Many Faces of Tau (2011, background): “The peptide NAP stabilizes microtubules (Divinski et al., 2006) and reduces tau hyperphosphorylation (Vulih-Shultzman et al., 2007), suggesting that microtubule-stabilizing compounds can have more than one mechanism of action.”
• Therapeutics of Alzheimer's disease: Past, present and future. (2014, background): “Heat shock protein 90 (Hsp 90), a chaperone involved in folding the denatured proteins, seems to play a role in preventing tau degradation (Dickey et al., 2007).”
• Post-translational modifications of tau protein: implications for Alzheimer's disease. (2011, positive): “Tau phosphorylation at S262, S293, S324 and S356, respectively found in KXGS of R1, R2, R3 and R4 domains, have been shown to decrease tau binding to microtubules (Dickey et al., 2007; Drewes et al., 1995).”
• Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing. (2009, background): “Since recent reports demonstrated that Tau phosphorylated at the KXGS motifs of the repeat domain is less susceptible to proteasomal degradation mediated by Hsp90 (20,46), we suspected that this kind of phosphorylated Tau may be preferentially degraded via the lysosome.”