About: Sculpting the proteome with small molecules

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Sculpting the proteome with small molecules
Creator	Finley, Daniel King, Randall
Source	Medline; PMC
abstract	The ubiquitin-proteasome system (UPS) pervades the biology of eukaryotes. Because it depends on the activity of hundreds of different enzymes and protein-protein interactions, the UPS provides many opportunities for selective modulation of the pathway with small molecules. Here we discuss the principles that underlie the development of effective inhibitors or activators of the pathway. We emphasize insights from structural analysis and describe strategies for evaluating the selectivity of compounds.
has issue date	2014-10-17(xsd:dateTime)
bibo:doi	10.1038/nchembio.1671
bibo:pmid	25325686
has license	green-oa
sha1sum (hex)	9a67a1447a5d8910a9d58b9ebc584812e20977a4
schema:url	https://doi.org/10.1038/nchembio.1671
resource representing a document's title	Sculpting the proteome with small molecules
has PubMed Central identifier	PMC4639395
has PubMed identifier	25325686
schema:publication	Nature Chemical Biology
resource representing a document's body	covid:9a67a1447a5d8910a9d58b9ebc584812e20977a4#body_text
is schema:about of	named entity 'SELECTIVE' named entity 'ACTIVITY' named entity 'PROVIDES' named entity 'SELECTIVITY' named entity 'DISCUSS' named entity 'Because' named entity 'PROTEIN-PROTEIN INTERACTIONS' named entity 'EFFECTIVE' named entity 'MODULATION' named entity 'DIFFERENT' named entity 'STRATEGIES' named entity 'INHIBITORS' named entity 'SMALL MOLECULES' named entity 'INSIGHTS' named entity 'EUKARYOTES' named entity 'STRUCTURAL ANALYSIS' named entity 'ENZYMES' named entity 'PROTEOME' named entity 'SMALL MOLECULES' named entity 'UBIQUITIN-PROTEASOME SYSTEM' named entity 'UPS' named entity 'DESCRIBE' named entity 'HERE' named entity 'EVALUATING' named entity 'BIOLOGY' named entity 'PATHWAY' named entity 'DEVELOPMENT' named entity 'depends' named entity 'biology' named entity 'structural analysis' named entity 'small molecules' named entity 'ubiquitin-proteasome' named entity 'eukaryotes' named entity 'UPS' named entity 'compounds' named entity 'substrate' named entity 'structural analysis' named entity 'physiological function' named entity 'chemical biology' named entity 'enzyme' named entity 'enzyme' named entity 'p53' named entity 'auxin' named entity 'Nedd8' named entity 'binding pocket' named entity 'ubiquitin' named entity 'protein stability' named entity 'ubiquitin' named entity 'biochemical' named entity 'mammals' named entity 'synergistically' named entity 'autoubiquitination' named entity '2a-c' named entity 'cysteine' named entity 'KEAP1' named entity 'small molecules' named entity 'substrate binding' named entity 'ubiquitin' named entity 'HECT' named entity 'ligase' named entity 'endogenous' named entity 'protein' named entity 'ubiquitin' named entity 'protein' named entity 'Usp1' named entity 'transcriptional repressors' named entity 'Usp7' named entity 'potency' named entity 'sequence motifs' named entity 'enzyme classes' named entity 'lenalidomide' named entity 'protein stability' named entity 'antioxidant' named entity 'enzyme' named entity 'deubiquitinating' named entity 'Usp14' named entity 'Nedd8' named entity 'general features' named entity 'Nrf2' named entity 'physiological'

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