About: Atomistic Autophagy: The Structures of Cellular Self-Digestion

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Atomistic Autophagy: The Structures of Cellular Self-Digestion
Creator	Hurley, James Schulman, Brenda
Source	Elsevier; Medline; PMC
abstract	Autophagy is directed by numerous distinct autophagy-related (Atg) proteins. These transmit starvation-induced signals to lipids and regulatory proteins and assemble a double-membrane autophagosome sequestering bulk cytoplasm and/or selected cargos destined for degradation upon autophagosome fusion with a vacuole or lysosome. This Review discusses the structural mechanisms by which Atg proteins sense membrane curvature, mediate a PI(3)P-signaling cascade, and utilize autophagy-specific ubiquitin-like protein cascades to tether proteins to autophagosomal membranes. Recent elucidation of molecular interactions enabling vesicle nucleation, elongation, and cargo recruitment provides insights into how dynamic protein-protein and protein-membrane interactions may dictate size, shape, and contents of autophagosomes.
has issue date	2014-04-10(xsd:dateTime)
bibo:doi	10.1016/j.cell.2014.01.070
bibo:pmid	24725401
has license	els-covid
sha1sum (hex)	6ef138c1a83b15f86805a688241e4d728c05d33a
schema:url	https://doi.org/10.1016/j.cell.2014.01.070
resource representing a document's title	Atomistic Autophagy: The Structures of Cellular Self-Digestion
has PubMed Central identifier	PMC4038036
has PubMed identifier	24725401
schema:publication	Cell
resource representing a document's body	covid:6ef138c1a83b15f86805a688241e4d728c05d33a#body_text
is schema:about of	named entity 'membranes' named entity 'assemble' named entity 'autophagosomes' named entity 'directed' named entity 'Recent' named entity 'signals' named entity 'lysosome' named entity 'mediate' named entity 'Autophagy' named entity 'numerous' named entity 'fusion' named entity 'dynamic' named entity 'autophagosome' named entity 'protein' named entity 'ubiquitin-like protein' named entity 'vacuole' named entity 'protein-protein' named entity 'Atg proteins' named entity 'autophagosome' named entity 'PI(3)P' named entity 'lipids' named entity 'nucleation' named entity 'cytoplasm' named entity 'cytoplasm' named entity 'protein' named entity 'Atg8' named entity 'Atg7' named entity 'autophagy' named entity 'Atg7' named entity 'Atg4' named entity 'Beclin 1' named entity 'PI(3)P' named entity 'active site' named entity 'WIPI' named entity 'ATP' named entity 'ubiquitinated' named entity 'Atg16' named entity 'autophagy' named entity 'lipidation' named entity 'sulfate ion' named entity 'Cys' named entity 'Suzuki' named entity 'Atg3' named entity 'PI(3)P' named entity 'Atg7' named entity 'vacuole' named entity 'autophagy' named entity 'closed conformation' named entity 'PI(3)P' named entity 'ATG4' named entity 'Atg8' named entity 'active sites' named entity 'lipid' named entity 'MgATP' named entity 'lipid' named entity 'spindle checkpoint' named entity 'Optineurin' named entity 'Vps34' named entity 'Atg14' named entity 'Atg8' named entity 'thioester' named entity 'helical' named entity 'ligation' named entity 'Atg3' named entity 'Atg4' named entity 'Atg13' named entity 'protein complexes' named entity 'Atg12' named entity 'Atg3' named entity 'protomers' named entity 'Atg1' named entity 'Atg8' named entity 'Atg7' named entity 'Atg18' named entity 'phosphopeptide' named entity 'autophagosome' named entity 'ATG12' named entity 'NDP52' named entity 'lipid vesicles' named entity 'phosphate'

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