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malfunction
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reduced proteasomal activity contributes to the accumulation of carbonylated proteins in chronic experimental autoimmune encephalomyelitis. Chymotrysin-like and caspase-like activities of the 20S proteasome are impaired in chronic experimental autoimmune encephalomyelitis, while the amount of proteasome is unchanged, determination of proteasome failure by the build-up of ubiquitinated proteins, mostly within astrocytes, diminished activity of the 20S proteasome is a major contributor to the accumulation of carbonylated proteins in astrocytes of chronic experimental autoimmune encephalomyelitis mice
malfunction
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T-DNA insertion mutation in RPN1a results in increased trichome branches on main stem, and trichome number on rosette leaves and the main stem compared with the wild type plant
malfunction
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reduced proteasomal activity contributes to the accumulation of carbonylated proteins in chronic experimental autoimmune encephalomyelitis. Chymotrysin-like and caspase-like activities of the 20S proteasome are impaired in chronic experimental autoimmune encephalomyelitis, while the amount of proteasome is unchanged, determination of proteasome failure by the build-up of ubiquitinated proteins, mostly within astrocytes, diminished activity of the 20S proteasome is a major contributor to the accumulation of carbonylated proteins in astrocytes of chronic experimental autoimmune encephalomyelitis mice
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metabolism
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inhibition of the proteolytic activity of the proteasome induces apoptosis and suppresses essential functions of activated human CD4+ T cells, and proteasome inhibition activates the mitochondrial pathway of apoptosis in human CD4+ T cells, detailed mechanisms of apoptosis, overview
metabolism
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the expression of unstable proteins is regulated by transcriptional regulation and not by degradation of the unstable protein by the ubiquitin/proteasome system, overview
metabolism
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the expression of unstable proteins is regulated by transcriptional regulation and not by degradation of the unstable protein by the ubiquitin/proteasome system, overview
metabolism
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the expression of unstable proteins is regulated by transcriptional regulation and not by degradation of the unstable protein by the ubiquitin/proteasome system, overview
metabolism
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the ubiquitin-proteasome pathway plays an important role in a variety of cellular functions, primarily via its proteolytic activity, and is one of the vital pathways in the cell that becomes dysfunctional as a result of chronic ethanol consumption. The inhibition of proteasome activity in the nucleus is therefore etiologically involved in the accumulation of damaged proteins in the nucleus, and in the deregulation of transcription
physiological function
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it is possible to restore significant levels of enzyme activity to 17 of 18 disease causing missense mutations in human cystathionine beta-synthase expressed in Saccharomyces cerevisiae by exposure to ethanol, proteasome inhibitors, e.g. bortezomib or MG132, or deletion of the Hsp26 small heat shock protein. All three of these treatments induce Hsp70, which is necessary but not sufficient for rescue, overview. The treatment can also rescue disease-causing mutations in human p53 and the methylene tetrahydrofolate reductase gene
physiological function
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oxidative stress caused by tert-butyl hydroperoxide and proteasome inhibition by lactacystin induce apoptosis in neurons and astrocytes. Suppression of proteasome activity triggers the translocation of cathepsin D from lysosomes to cytosol, mechanism, overview
physiological function
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physiological effects of partial inhibition of proteolytic activities of the proteasome, overview
physiological function
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proteasome inhibition increases the sensitivity of tumor cells toward cytolytic T-cell attack by NOXA-mediated enhancement of mitochondrial second mitochondria-derived activator of caspase, SMAC, release, overview
physiological function
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the 20S proteasome is a multicatalytic protease playing a crucial role in cellular protein turnover in eukaryotes. It is involved in the maintenance of the biological homeostasis and degradation of key components of the cellmachinery. Critical cellular functions such as transcription, cell-cycle progression, cell differenciation, antigen processing, and tumor suppression rely on this molecular system
physiological function
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the proteasome, a multicatalytic protease, is responsible for the generation of most MHC class I ligands
physiological function
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the ubiquitin-proteasome pathway is essential for promoting the exchange of transcriptional factors on chromatin
physiological function
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the ubiquitin-proteasome system is involved in many cellular functions by mediating selective protein degradation. Protein substrates are first selected and marked by polyubiquitination, polyubiquitinated proteins are next recognized and degraded by the 26S proteasome, which consists of a 20S catalytic core particle and a 19S regulatory particle. Once polyubiquitin on a substrate protein is recruited to the 19S RP, the protein moiety is unfolded, translocated into the 20S CP, and finally degraded with release of polyubiquitin, which is processed into free ubiquitin and recycled
physiological function
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proteasome-mediated proteolysis is important for synaptic plasticity, neuronal development, protein quality control, and many other processes in neurons. The standard 26S subunits and a set of 28 proteasome-interacting proteins that associate substoichiometrically and may serve as regulators or cofactors in the brain differing in composition from other tissues. The content of proteasomes and their set of associated proteins can be altered by neuronal activity, in a manner likely to influence synaptic plasticity and learning
physiological function
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the 20S proteasome, which is the major proteolytic enzyme of the cell, is responsible for the generation of antigenic peptides derived from endogenously expressed foreign or aberrant protein molecules. The proteasome-generated spliced peptides are presented by MHC class I molecules to the outside world so that they can be specifically recognised by cytotoxic T lymphocytes at the cell surface. Peptide splicing is an intrinsic additional catalytic property of the proteasome
physiological function
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the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
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the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
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the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
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the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
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the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable
physiological function
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the 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. The 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Unlike the entire 26S proteasome, the 20S CP performs a relative simple protease function and is biochemically very stable. Immunoproteasome is responsible for breaking down foreign proteins into short antigenic peptides, which are ligands of MHC class I molecules. ATPase induced gate opening in the 20S CP
physiological function
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the RPN1a subunit of the 26S proteasome is involved in trichome's branching in Arabidopsis thaliana through the giberellin and cytokinin signaling pathways
physiological function
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proteasomal substrates usually are tagged by a substrate-anchored polyubiquitin chain, while some proteins are degraded following monoubiquitination. For randomly sampled representative substrates, monoubiquitinated substrates are smaller than the polyubiquitinated ones, are enriched in specific pathways
physiological function
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proteasomal substrates usually are tagged by a substrate-anchored polyubiquitin chain, while some proteins are degraded following monoubiquitination. For randomly sampled representative substrates, monoubiquitinated substrates are smaller than the polyubiquitinated ones, are enriched in specific pathways, and, in humans, are structurally less disordered
physiological function
subunit PSMA8 is expressed in spermatocytes from the pachytene stage, and assembles a type of testis-specific core proteasome. Deletion of PSMA8 decreases the abundance of proteasome in testes. Meiotic proteins that are normally degraded at late prophase I, such as RAD51 and RPA1, remain stable in PSMA8-deleted spermatocytes. PSMA8-null spermatocytes exhibit delayed M-phase entry and are finally arrested at this stage, resulting in male infertility
physiological function
the 19S regulatory particle in 26S proteasomes performs stepwise substrate unfolding and opens the chamber gate in an ATP-dependent manner. Spontaneous dissociation of the regulatory particle in isolated 26S proteasomes leaves core particles with different gate sizes related presumably to different stages in the gate opening
physiological function
ubiquitin C-terminal hydrolase Ubp6 binds to the regulatory particle non-ATPase (Rpn) 1 via its N-terminal ubiquitin-like domain, whereas its catalytic ubiquitin-specific protease domain is positioned variably. Addition of ubiquitin aldehyde stabilizes the binding of the ubiquitin-specific protease domain in a position where it bridges the proteasome subunits Rpn1 and the regulatory particle triple-A ATPase (Rpt) 1. The ubiquitin-specific protease domain binds to Rpt1 in the immediate vicinity of the Ubp6 active site. The catalytic triad is positioned in proximity to the mouth of the ATPase module and to the deubiquitylating enzyme Rpn11. On the proteasome side, binding of Ubp6 favors conformational switching of the 26S proteasome into an intermediate-energy conformational state, in particular upon the addition of ubiquitin aldehyde
physiological function
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proteasome-mediated proteolysis is important for synaptic plasticity, neuronal development, protein quality control, and many other processes in neurons. The standard 26S subunits and a set of 28 proteasome-interacting proteins that associate substoichiometrically and may serve as regulators or cofactors in the brain differing in composition from other tissues. The content of proteasomes and their set of associated proteins can be altered by neuronal activity, in a manner likely to influence synaptic plasticity and learning
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additional information
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a decrease in proteasome activity induced by the injection of lactacystin in the corpus callosum in the remyelination process that normally occurs after cuprizone-induced demyelination markedly improves the remyelination process. It also attenuates the activation of NFkappaB and the recruitment of microglia and astrocytes, thus helping in the recovery of the mitochondrial respiratory chain activities that are affected by cuprizone treatment
additional information
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inhibition of the proteasomes by gold complexes results in accumulation of ubiquitinated proteins and proteasome target proteins, and induction of cell death, but at significantly different levels
additional information
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inhibition of this enzymatic activity with beta-subunit-specific proteasome inhibitors may provide an anti-tumoral effect by inhibiting cell proliferation and angiogenesis, and by selectively inducing apoptosis of tumor cells
additional information
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primary Waldenstroem macroglobulinemia cells express higher level of immunoproteasome 20S compared with constitutive proteasome 20S. Selective inhibition of the chymotrypsin-like activity of constitutive proteasome 20S and immunoproteasome 20S represents a sufficient and successful strategy to induce antineoplastic effect in hematologic tumors
additional information
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proteasome inhibitors, but not a Nedd8 pathway inhibitor, upregulate RNA levels of PSM genes in cancer cells
additional information
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the 26S proteasome consists of a 20S multicatalytic core capped on either end with 19S regulatory subunits. The 20S proteasome is a chambered, barrel-like structure containing two heptameric rings made from alpha subunits and two heptameric rings made from beta subunits. The alpha rings perform capping and gating functions, whereas three of the beta subunits, beta1, beta2, and beta5, contain the NH2-terminal threonines responsible for the different proteasome proteolytic activities. The beta1, beta2, and beta5 subunits are referred to as caspase-like, trypsin-like, and chymotrypsin-like, respectively
additional information
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the 26S proteasome consists of a 20S multicatalytic core capped on either end with 19S regulatory subunits. The 20S proteasome is a chambered, barrel-like structure containing two heptameric rings made from alpha subunits and two heptameric rings made from beta subunits. The alpha rings perform capping and gating functions, whereas three of the beta subunits, beta1, beta2, and beta5, contain the NH2-terminal threonines responsible for the different proteasome proteolytic activities. The beta1, beta2, and beta5 subunits are referred to as caspase-like, trypsin-like, and chymotrypsin-like, respectively
additional information
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the barrel-shaped proteolytic 20S proteasome core particle which consists of four seven-subunit rings, is capped at one or both ends by 19S regulatory particles and is the central part of the large, 2.4 MDa, multi-subunit protease complexes performing ATP-dependent degradation of poly-ubiquitinated proteins, and being responsible for the majority of the non-lysosomal proteolysis which occurs in eukaryotic cells
additional information
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the proteasomal chymotrypsin-like activity inhibition is associated with accumulated levels of ubiquitinated proteins
additional information
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activity and subunit composition of the 26 S proteasomes in plants, detailed overview. The 26 S proteasome is composed of two subparticles, the 20 S core protease that compartmentalizes the protease active sites and the 19 S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. A diverse and highly dynamic population of proteasomes is assembled in plants, which may expand the target specificity and functions of intracellular proteolysis, overview
additional information
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development of an integrated proteomic approach, QTAX, for quantitative analysis of tandem affinity purified in vivo cross-linked protein complexes to capture protein interactions of all natures in a single analysis, overview. Investigation of cell cycle specific proteasome interaction networks
additional information
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development of SpliceMet: a method that combines combinatorial computations with mass spectrometric analyses of proteasome-generated spliced peptides, for analysis of peptides, presented by MHC class I molecules on the cell surface, in a manner independent of cytotoxic T lymphocytes, kinetics, detailed overview
additional information
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structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
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structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
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structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
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structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
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structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
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structures of the 26S proteasome, e.g. the 19S subunits of 26S proteasome, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain, or the molecular structures of the barrel-shaped 20S protease core particle, 20S CP, detailed overview
additional information
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activity and subunit composition of the 26 S proteasomes in plants, detailed overview. The 26 S proteasome is composed of two subparticles, the 20 S core protease that compartmentalizes the protease active sites and the 19 S regulatory particle that recognizes and translocates appropriate substrates into the core protease lumen for breakdown. A diverse and highly dynamic population of proteasomes is assembled in plants, which may expand the target specificity and functions of intracellular proteolysis, overview
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