bp(GO:"protein catabolic process")
For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719
For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719
For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719
For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719
It was initially believed that the presence of DUBs at the proteasome (such as Uch37/UchL5 and Usp14) would promote the degradation of proteins through facilitating substrate processing (see also the next section) PubMed:24457024
It was initially believed that the presence of DUBs at the proteasome (such as Uch37/UchL5 and Usp14) would promote the degradation of proteins through facilitating substrate processing (see also the next section) PubMed:24457024
However, recent studies have shown that, by contrast, upon chemical inhibition of the proteasome-bound DUB Usp14, the degradation of aggregation-prone substrates in mammalian tissue culture cells significantly increased [65] PubMed:24457024
Alternatively, either Hsp70 or Hsp90 can recruit the ubiquitin E3 ligase, C-terminal Hsp70 interacting protein (CHIP), to degrade the bound substrate [104] PubMed:21882945
Although both Hsp70 and Hsp90 can promote degradation of client proteins, it has recently been shown that, functionally, the Hsp70 complex often dominates triage decisions [85,107,109] PubMed:21882945
Although both Hsp70 and Hsp90 can promote degradation of client proteins, it has recently been shown that, functionally, the Hsp70 complex often dominates triage decisions [85,107,109] PubMed:21882945
The PN branch of degradation includes the ubiquitin- proteasome system (UPS) and machinery of autophagy (23, 196–200). PubMed:23746257
Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257
The PN branch of degradation includes the ubiquitin- proteasome system (UPS) and machinery of autophagy (23, 196–200). PubMed:23746257
Once formed, new autophagosomes move through a stepwise maturation process that culminates with fusion to a lysosome permitting degradation of the lumenal contents. PubMed:18930136
For example, upregulation of the pathway is observed during massive degradation of skeletal muscle proteins that occurs under normal fasting but also under pathological conditions such as cancer-induced cachexia, severe sepsis, metabolic acidosis, or following denervation PubMed:14556719
Hsp70 chaperones are a ubiquitous class of proteins. They are involved in a wide range of protein quality control functions, including de novo protein folding, refolding of stress- denatured proteins, protein transport, mem- brane translocation, and protein degradation. PubMed:23746257
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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.