Publication:
REGULATION OF THE EUKARYOTIC PROTEIN-SYNTHESIS BY PHOSPHORYLATION OF ELONGATION FACTOR-II

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dc.contributor.authorsERDOGDU, G; CIRAKOGLU, B; KAN, B
dc.date.accessioned2022-03-12T16:57:24Z
dc.date.accessioned2026-01-10T17:10:57Z
dc.date.available2022-03-12T16:57:24Z
dc.date.issued1993
dc.description.abstractThe phosphorylation of elongation factor 2 (EF-2) by Ca2+/calmodulin kinase III decreases its activity and results in inhibition of translation. The effects of different experimental conditions on the phosphorylation of EF-2 in rabbit reticulocyte have been investigated. The phosphorylation of EF-2 was enhanced in the presence of GDP and inhibited by cyclic-AMP and NEM whereas the ADP-ribosylation of EF-2 did not change the extent of its phosphorylation.
dc.identifier.doidoiWOS:A1993LB52800005
dc.identifier.issn0749-5331
dc.identifier.urihttps://hdl.handle.net/11424/226932
dc.identifier.wosWOS:A1993LB52800005
dc.language.isoeng
dc.publisherMBR PRESS INC
dc.relation.ispartofBIOCHEMICAL ARCHIVES
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectMR 100,000 SUBSTRATE
dc.subjectFACTOR-II
dc.subjectKINASE-III
dc.subjectINITIATION
dc.subjectIDENTIFICATION
dc.subjectACTIVATION
dc.subjectEF-2
dc.subjectHEME
dc.titleREGULATION OF THE EUKARYOTIC PROTEIN-SYNTHESIS BY PHOSPHORYLATION OF ELONGATION FACTOR-II
dc.typearticle
dspace.entity.typePublication
oaire.citation.endPage99
oaire.citation.issue2
oaire.citation.startPage91
oaire.citation.titleBIOCHEMICAL ARCHIVES
oaire.citation.volume9

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