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3.
Figure 4

Figure 4. Structures of spergualin and related polyamines. From: Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target.

Select structures from larger series are shown for clarity. See the text for references.

Christopher G. Evans, et al. J Med Chem. ;53(12):4585-4602.
4.
Figure 7

Figure 7. Chemical structures of Hsp70 inhibitors. From: Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target.

Select compounds from larger series are shown for clarity. See the text for references.

Christopher G. Evans, et al. J Med Chem. ;53(12):4585-4602.
5.
Figure 5

Figure 5. Structures of dihydropyrimidines with activity against Hsp70 family members. From: Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target.

Select compounds from larger series are shown for clarity. See the text for references.

Christopher G. Evans, et al. J Med Chem. ;53(12):4585-4602.
6.
Figure 2

Figure 2. Roles of Hsp70 in anti-apoptotic signaling. From: Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target.

Hsp70 is thought to promote survival and block apoptosis through interactions with multiple steps in the pathway. For some substrates, Hsp70’s role appears to be stabilization of the substrate, while it appears to mediate the degradation of other substrates. The regulatory mechanisms that govern these activities are not known. See the main text and Table 1 for references.

Christopher G. Evans, et al. J Med Chem. ;53(12):4585-4602.
7.
Figure 1

Figure 1. Structure and ATPase cycle of Hsp70. From: Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target.

(A) Heat shock protein 70 is composed of a 45 kDa nucleotide-binding domain (NBD), connected to a 30kDa substrate-binding domain (SBD) by a short, hydrophobic linker. The SBD contains a beta-sandwich and a helical lid domain. The representative structure shown is of prokaryotic DnaK in complex with ADP and a peptide substrate (PDB # 2KHO). (B) Schematic of ATP hydrolysis and the role of co-chaperones.

Christopher G. Evans, et al. J Med Chem. ;53(12):4585-4602.
8.
Figure 3

Figure 3. Potential roles for Hsp70 in protein misfolding and aggregation. From: Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target.

Hsp70 has been linked to multiple steps of the protein misfolding and aggregation pathway, including in preventing misfolding, blocking early stages of aggregation and in mediating the degradation of misfolded intermediates through coupling to the ubiquitin-proteasome system. The Hsp70 co-chaperones BAG2 and CHIP have both been linked to clearance of misfolded proteins. In some systems (including yeast prions), Hsp70 activity is required for fibril formation. For simplicity, this schematic encompasses broad aspects of the misfolding pathway of amyloid beta, polyglutamines and tau, although important differences likely exist. See the main text and Table 2 for references.

Christopher G. Evans, et al. J Med Chem. ;53(12):4585-4602.

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