Nanopublications

Matches in Nanopublications for { ?s ?p ?o <http://www.tkuhn.ch/bel2nanopub/RAMtiiDoZuOKLH3w_v-7MuHc1lHdIWT-vdPLY9QXRdZ3E#provenance>. }

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_5 label "Selventa" provenance.
large_corpus.bel title "BEL Framework Large Corpus Document" provenance.
large_corpus.bel description "Approximately 61,000 statements." provenance.
large_corpus.bel version "1.4" provenance.
large_corpus.bel authoredBy _5 provenance.
assertion wasDerivedFrom large_corpus.bel provenance.
assertion wasDerivedFrom _4 provenance.
assertion hadPrimarySource 17170114 provenance.
_4 wasQuotedFrom 17170114 provenance.
_4 value "{From full text} For example, phosphorylation of eIF2{alpha} by GCN2 (EIF2AK4) is enhanced by amino acid limitation, UV irradiation, and proteasome inhibition (13?16). Phosphorylation of eIF2{alpha} inhibits general protein synthesis by reducing the levels of eIF2-GTP that are required for binding of initiator tRNA to the translation apparatus. Concomitant with lowered protein synthesis, eIF2{alpha} phosphorylation leads to preferential translation of ATF4, a basic zipper (bZIP) transcription activator important for directing transcription of stress-related genes (17?20). Reduced protein synthesis conserves energy and provides the cell time for ATF4 and other stress-responsive transcription factors to reconfigure gene expression slated to alleviate damage elicited by the underlying stress. Other members of the eIF2 kinase family include PEK/Perk (EIF2AK3), whose activity is enhanced by endoplasmic reticulum (ER) stress (21, 22); HRI (EIF2AK1), which is regulated by heme deficiency and oxidative stress (23); and PKR (EIF2AK2), which functions in an antiviral pathway (24).{P@S52 is the common phosphorylation site between all 4 kinases and confirmed in Uniprot}" provenance.