About: Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases
Creator	Uversky, Vladimir Giri, Rajanish Kumar, Prateek Gadhave, Kundlik Kapuganti, Shivani
Source	Medline; PMC
abstract	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.
has issue date	2020-05-21(xsd:dateTime)
bibo:doi	10.3390/biom10050796
bibo:pmid	32455657
has license	cc-by
sha1sum (hex)	ecfe74334da1f6ef429584be4c0b2f98f117f2c5
schema:url	https://doi.org/10.3390/biom10050796
resource representing a document's title	Unstructured Biology of Proteins from Ubiquitin-Proteasome System: Roles in Cancer and Neurodegenerative Diseases
has PubMed Central identifier	PMC7278180
has PubMed identifier	32455657
schema:publication	Biomolecules
resource representing a document's body	covid:ecfe74334da1f6ef429584be4c0b2f98f117f2c5#body_text
is schema:about of	named entity 'ENZYME' named entity 'FUNCTION' named entity 'BASED' named entity 'RELATIONSHIPS' named entity 'LARGE' named entity 'cancer targets' named entity 'ubiquitin' named entity 'neurodegenerative' named entity 'PSMD4' named entity 'UBQLN1' named entity 'deubiquitinating' named entity 'protein degradation' named entity 'UPS' named entity 'enzyme' named entity 'proteasomal' named entity 'immunological' named entity 'protein' named entity 'UBQLN2' named entity 'Ubiquitin' named entity 'zinc' named entity 'disordered proteins' named entity 'kDa' named entity 'quality control' named entity 'interleukin-1β' named entity 'proteasome' named entity 'gene mutations' named entity 'spleen' named entity 'proteome' named entity 'PTM' named entity 'N-terminus' named entity 'phosphorylation sites' named entity 'PDB' named entity 'autophagy' named entity 'adenylation' named entity 'binding domains' named entity 'UPS' named entity 'polyubiquitinated' named entity 'intrinsic disorder' named entity 'toroid' named entity 'cysteine' named entity 'serous tubal intraepithelial carcinoma' named entity 'deubiquitinating enzyme' named entity 'receptor' named entity 'PSMD4' named entity 'protein' named entity 'Avram Hershko' named entity 'USP7' named entity 'PTM' named entity 'Arginine' named entity 'UCHL1' named entity 'mice' named entity 'C-terminal' named entity 'leucine-rich repeat' named entity 'USP7' named entity 'USP14' named entity 'ubiquitylation' named entity 'UBQLN2' named entity 'PSMD2' named entity 'protein degradation' named entity 'cardiovascular disease' named entity 'UBQLN1' named entity 'ATPases' named entity 'eukaryotic cells' named entity 'ubiquitin-like' named entity 'interact' named entity 'UPS' named entity 'polyglutamine' named entity 'amino acid residues' named entity 'protein' named entity 'proteasome' named entity 'nitrosylation' named entity 'cell proliferation' named entity 'salmon pink' named entity 'Enzyme' named entity 'UniProt' named entity 'UBQLN2' named entity 'ATPases'

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