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10.3390/biom10050796 http://scihub22266oqcxt.onion/10.3390/biom10050796 32455657!7278180!32455657     free     free     free Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 251.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biomolecules 2020 ; 10 (5): ä Nephropedia Template TP {{tp|p=32455657|t=2020. Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases |pdf=|usr=}}{{32455657}} gab.com Text Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases JO: Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=32455657 #FOAvip The 26S proteasome is a large (~2.5 MDa) protein complex consisting of at least 33 different subunits and many other components, which form the ubiquitin proteasomal system (UPS), an ATP-dependent protein degradation system in the cell. UPS serves as an essential component of the cellular protein surveillance machinery, and its dysfunction leads to cancer, neurodegenerative and immunological disorders. Importantly, the functions and regulations of proteins are governed by the combination of ordered regions, intrinsically disordered protein regions (IDPRs) and molecular recognition features (MoRFs). The structure-function relationships of UPS components have not been identified completely; therefore, in this study, we have carried out the functional intrinsic disorder and MoRF analysis for potential neurodegenerative disease and anti-cancer targets of this pathway. Our report represents the presence of significant intrinsic disorder and disorder-based binding regions in several UPS proteins, such as extraproteasomal polyubiquitin receptors (UBQLN1 and UBQLN2), proteasome-associated polyubiquitin receptors (ADRM1 and PSMD4), deubiquitinating enzymes (DUBs) (ATXN3 and USP14), and ubiquitinating enzymes (E2 (UBE2R2) and E3 (STUB1) enzyme). We believe this study will have implications for the conformation-specific roles of different regions of these proteins. This will lead to a better understanding of the molecular basis of UPS-associated diseases. Twit Text FOAVip Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases ????Biomolecules http://www.kidney.de/pget.php?&tw=1&pmid=32455657 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32455657 #FOAvip English Wikipedia <ref>{{Cite pmid|32455657}}</ref> Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases #MMPMID32455657 Gadhave K; Kumar P; Kapuganti SK; Uversky VN; Giri R Biomolecules 2020[May]; 10 (5): ä PMID32455657show ga The 26S proteasome is a large (~2.5 MDa) protein complex consisting of at least 33 different subunits and many other components, which form the ubiquitin proteasomal system (UPS), an ATP-dependent protein degradation system in the cell. UPS serves as an essential component of the cellular protein surveillance machinery, and its dysfunction leads to cancer, neurodegenerative and immunological disorders. Importantly, the functions and regulations of proteins are governed by the combination of ordered regions, intrinsically disordered protein regions (IDPRs) and molecular recognition features (MoRFs). The structure-function relationships of UPS components have not been identified completely; therefore, in this study, we have carried out the functional intrinsic disorder and MoRF analysis for potential neurodegenerative disease and anti-cancer targets of this pathway. Our report represents the presence of significant intrinsic disorder and disorder-based binding regions in several UPS proteins, such as extraproteasomal polyubiquitin receptors (UBQLN1 and UBQLN2), proteasome-associated polyubiquitin receptors (ADRM1 and PSMD4), deubiquitinating enzymes (DUBs) (ATXN3 and USP14), and ubiquitinating enzymes (E2 (UBE2R2) and E3 (STUB1) enzyme). We believe this study will have implications for the conformation-specific roles of different regions of these proteins. This will lead to a better understanding of the molecular basis of UPS-associated diseases. |*Ubiquitination[MESH] |Adaptor Proteins, Signal Transducing/chemistry/metabolism[MESH] |Ataxin-3/chemistry/metabolism[MESH] |Autophagy-Related Proteins/chemistry/metabolism[MESH] |Humans[MESH] |Intracellular Signaling Peptides and Proteins/chemistry/metabolism[MESH] |Intrinsically Disordered Proteins/*chemistry/metabolism[MESH] |Neoplasms/*metabolism[MESH] |Neurodegenerative Diseases/*metabolism[MESH] |Proteasome Endopeptidase Complex/*chemistry/metabolism[MESH] |Protein Binding[MESH] |Protein Folding[MESH] |Protein Interaction Maps[MESH] |RNA-Binding Proteins/chemistry/metabolism[MESH] |Repressor Proteins/chemistry/metabolism[MESH] |Ubiquitin Thiolesterase/chemistry/metabolism[MESH] |Ubiquitin-Activating Enzymes/chemistry/metabolism[MESH]Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Rol(epmc).pdf DeepDyve Pubget Overpricing