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  • ubiquitin-proteas
  • Degradation of cAMP-responsive element-binding protein by the ubiquitin-proteasome pathway contributes to glucotoxicity in beta-cells and human pancreatic islets. (biomedsearch.com)
  • CONCLUSIONS: These studies demonstrate that the CREB degradation by the ubiquitin-proteasome pathway contributes to beta-cell dysfunction and death upon glucotoxicity and provide new insight into the cellular mechanisms of glucotoxicity. (biomedsearch.com)
  • Increased expression of the ubiquitin-proteasome pathway in murine myotubes by proteolysis-inducing factor (PIF) is associated with activation of the transcription factor NF-kappaB. (nih.gov)
  • Many studies have identified the ubiquitin proteasome pathway (UPP) to be important for successful DENV production, but how the UPP contributes to DENV life cycle as host factors remains ill defined. (nih.gov)
  • cytosolic
  • This results in the release of CAR from the cytosolic complex, followed by translocation into the nucleus. (nih.gov)
  • With increased CCRP expression and in concert with HSP70, a heteromeric protein complex that includes CAR, CCRP, and HSP70 is favored resulting in cytosolic stabilization of CAR. (nih.gov)
  • cathepsins
  • Based on our results, the susceptibility of Env-A244 to cathepsins and not to proteasomes suggests a possible mechanism for the generation of Env-specific CD4(+)T cell and antibody responses in the RV144 vaccinees. (nih.gov)
  • inactivation
  • In the early and mid 1970s two thiol-activated endopeptidases, responsible for more than 90% of bradykinin inactivation, were isolated from cytosol of rabbit brain, and characterized. (wikipedia.org)
  • cells
  • Molecular and imaging analyses in β-lactone treated THP-1 cells suggest that proteasome function does not prevent virus assembly but rather DENV egress. (nih.gov)
  • CLDN1 is a major component in forming tight junction complexes between cells, which foster cell-cell adhesion of cell membranes. (wikipedia.org)
  • cytoplasm
  • Currently, it is known that in its inactive state, CAR is retained in the cytoplasm in a protein complex with HSP90 and the tetratricopeptide repeat protein cytosoplasmic CAR retention protein (CCRP). (nih.gov)
  • pathway
  • Env-A244 was resistant to proteasomes, thus diminishing the possibility of the generation of class I epitopes by the classical MHC class I pathway. (nih.gov)
  • cell
  • An essential function of the modified proteasome complex, the immunoproteasome, is the processing of numerous MHC class-I restricted T cell epitopes. (wikipedia.org)
  • Type 2 RIPs consist of an A chain that is functionally equivalent to a type 1 RIP, covalently connected by a single disulfide bond to a B chain that is catalytically inactive, but serves to mediate transport of the A-B protein complex from the cell surface, via vesicle carriers, to the lumen of the endoplasmic reticulum (ER). (wikipedia.org)
  • Chains
  • Whereas type 1 RIPs are composed of a single protein chain that possesses catalytic activity, type 2 RIPs, also known as holotoxins, are composed of two different protein chains that form a heterodimeric complex. (wikipedia.org)
  • early
  • Much of the early work leading up to the discovery of the ubiquitin proteasome system occurred in the late 1970s and early 1980s at the Technion in the laboratory of Avram Hershko, where Aaron Ciechanover worked as a graduate student. (wikipedia.org)
  • cytosolic
  • This results in the release of CAR from the cytosolic complex, followed by translocation into the nucleus. (nih.gov)
  • With increased CCRP expression and in concert with HSP70, a heteromeric protein complex that includes CAR, CCRP, and HSP70 is favored resulting in cytosolic stabilization of CAR. (nih.gov)
  • The proteasome subcomponents are often referred to by their Svedberg sedimentation coefficient (denoted S). The proteasome most exclusively used in mammals is the cytosolic 26S proteasome, which is about 2000 kilodaltons (kDa) in molecular mass containing one 20S protein subunit and two 19S regulatory cap subunits. (wikipedia.org)
  • cytoplasm
  • Currently, it is known that in its inactive state, CAR is retained in the cytoplasm in a protein complex with HSP90 and the tetratricopeptide repeat protein cytosoplasmic CAR retention protein (CCRP). (nih.gov)
  • Treatment with the proteasome inhibitor MG132 (5 µM) causes CAR to accumulate in the cytoplasm of transfected HepG2 cells. (nih.gov)
  • human
  • Each conjugate sample (~110 nM) was incubated with 4 nM of human proteasome in the presence or absence of USP14 (80 nM). (nih.gov)
  • Conjugates (~110 nM) were incubated with human proteasome (4 nM) in the presence or absence of USP14 (80 nM). (nih.gov)
  • d, Ub n -Sic1 PY (~200 nM) was incubated with human proteasome (5 nM) in the presence or absence of USP14 (100 nM). (nih.gov)
  • Human proteasome (4 nM) was incubated with Ub n -securin (~100 nM) generated by UbcH10 and APC/C. Where indicated, USP14 (80 nM) was added. (nih.gov)
  • a, For ATP-depletion, purified human proteasomes were treated with hexokinase or mock-treated with vehicle for hexokinase (i.e. water). (nih.gov)
  • activity
  • Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome. (uniprot.org)
  • Structural basis for the different stability and activity between the Cdk5 (show CDK5 ELISA Kits ) complexes with p35 (show ANXA1 ELISA Kits ) and p39 (show JUN ELISA Kits ) activators. (antibodies-online.com)
  • Proteasome activity is expressed as arbitrary fluorescence units. (statsignaling.com)
  • Whereas type 1 RIPs are composed of a single protein chain that possesses catalytic activity, type 2 RIPs, also known as holotoxins, are composed of two different protein chains that form a heterodimeric complex. (wikipedia.org)
  • protein complex
  • Cohesion between sister chromatids is established during DNA replication and depends on a protein complex called cohesin. (ox.ac.uk)
  • Type 2 RIPs consist of an A chain that is functionally equivalent to a type 1 RIP, covalently connected by a single disulfide bond to a B chain that is catalytically inactive, but serves to mediate transport of the A-B protein complex from the cell surface, via vesicle carriers, to the lumen of the endoplasmic reticulum (ER). (wikipedia.org)
  • Cells
  • CLDN1 is a major component in forming tight junction complexes between cells, which foster cell-cell adhesion of cell membranes. (wikipedia.org)
  • Structure
  • In structure, the proteasome is a cylindrical complex containing a "core" of four stacked rings forming a central pore. (wikipedia.org)
  • Although electron microscopy data revealing the stacked-ring structure of the proteasome became available in the mid-1980s, the first structure of the proteasome core particle was not solved by X-ray crystallography until 1994. (wikipedia.org)
  • chain
  • The propolypeptide is cleaved within protein bodies by an endopeptidase to produce the mature ricin protein that is composed of a 267 residue A chain and a 262 residue B chain that are covalently linked by a single disulfide bond. (wikipedia.org)
  • responsible
  • In the early and mid 1970s two thiol-activated endopeptidases, responsible for more than 90% of bradykinin inactivation, were isolated from cytosol of rabbit brain, and characterized. (wikipedia.org)