a(CHEBI:ATP)
The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566
The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566
The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566
ATP is reduced in the proaggregant transgenic slices, matching the lower mitochondrial density, compared with littermate controls or antiaggregant Tau transgenic slices (Fig. 3H) PubMed:27671637
ATP is reduced in the proaggregant transgenic slices, matching the lower mitochondrial density, compared with littermate controls or antiaggregant Tau transgenic slices (Fig. 3H) PubMed:27671637
This suggests that the energy status of the neurons is compromised by proaggregant but not by antiaggregant Tau PubMed:27671637
In human astrocytes, ATP released from damaged or dying cells after traumatic brain injury activates the NLRP2 inflammasome, leading to the maturation of both IL-1β and IL-18 (Minkiewicz et al., 2013) PubMed:24561250
Spinal cord injury elevates extracellular ATP levels during neuroinflammation, which may act on purinergic receptors to trigger the activation of inflammasome (de Rivero Vaccari et al., 2012; Minkiewicz et al., 2013) PubMed:24561250
In another study, neurons from Tg mAPP/ABAD mice were shown to exhibit decreased activity of cyclooxygenase (COX) enzyme, spontaneous release of ROS, loss of mitochondrial membrane potential, a decrease in ATP production and release of cytochrome c from mitochondria with subsequent induction of caspase-3-like activity followed by apoptotic cell death. PubMed:30444369
Dysfunctional mitochondria are critically harmful to cells, as this leads to decreased synthesis of cellular ATP and accumulation of ROS, which further overburden and damage other functional mitochondria. PubMed:29758300
Accordingly, heme exposures of more than 10 μM caused the significant and progressive depletion of cellular ATP, which was measured after an 8-h exposure period. PubMed:26794659
This ATP depletion was prevented by the addition of the heme scavenger, hemopexin (Figure 5b). PubMed:26794659
The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566
The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566
The ATP-dependent chaperones are comprised of the 5 HSP90s, 17 HSP70s, 14 HSP60s, 6 ER-specific, and 8 MITO-specific Hsp100/AAA+ ATPases, respectively. PubMed:25437566
Another key early finding was that the cleavage of the ubiquitin chain from the substrate was ATP-dependent and was coupled to the translocation of the protein substrate into the 20S core PubMed:24457024
Another key early finding was that the cleavage of the ubiquitin chain from the substrate was ATP-dependent and was coupled to the translocation of the protein substrate into the 20S core PubMed:24457024
ATP is reduced in the proaggregant transgenic slices, matching the lower mitochondrial density, compared with littermate controls or antiaggregant Tau transgenic slices (Fig. 3H) PubMed:27671637
Activators include bacteria, virus, fungus, protoza, microbial proteins, crystalline urea, RNA, Alum, ATP, potassium efflux, fatty acids, Aβ, and most recently, degraded mitochondrial DNA (Liu et al., 2013a; Mathew et al., 2012; Schmidt and Lenz, 2012) PubMed:24561250
Spinal cord injury elevates extracellular ATP levels during neuroinflammation, which may act on purinergic receptors to trigger the activation of inflammasome (de Rivero Vaccari et al., 2012; Minkiewicz et al., 2013) PubMed:24561250
ATP, a danger-associated molecular pattern that is released from damaged cells after brain injury, activates the NLRP2 inflammasome, which consists of the NLRP2 receptor, ASC and caspase-1, in human astrocytes (Minkiewicz et al., 2013) PubMed:24561250
The ATP-induced activation of the NLRP2 inflammasome interacts with the ATP-release pannexin 1 channel and ATP-gated P2X7 receptor leading to the maturation of IL-1β (Minkiewicz et al., 2013) PubMed:24561250
In human astrocytes, ATP released from damaged or dying cells after traumatic brain injury activates the NLRP2 inflammasome, leading to the maturation of both IL-1β and IL-18 (Minkiewicz et al., 2013) PubMed:24561250
In addition, Brilliant Blue G (BBG), a P2X7 receptor antagonist, inhibits ATP-induced activation of the NLRP2 inflammasome in human astrocytes (Minkiewicz et al., 2013) PubMed:24561250
Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257
Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257
Chaperones that function broadly in de novo folding and refolding (i.e., the chaperonins, Hsp70s, and Hsp90s) are ATP regulated and recognize segments of exposed hydropho- bic amino acid residues, which are later buried in the interior of the natively folded protein. PubMed:23746257
ATP-independent chaperones, such as the small Hsps, may function as additional holdases that buffer aggregation. PubMed:23746257
GroEL and GroES undergo a complex binding-and-release cycle that is allosterically regulated by ATP binding and hydrolysis in the GroEL subunits (Figure 6b) (4, 77, 100, 136). PubMed:23746257
This ATP depletion was prevented by the addition of the heme scavenger, hemopexin (Figure 5b). PubMed:26794659
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.