Vis enkel innførsel

dc.contributor.authorVarland, Sylvia
dc.contributor.authorOsberg, Camilla
dc.contributor.authorArnesen, Thomas
dc.PublishedProteomics 2015eng
dc.description.abstractThe vast majority of eukaryotic proteins are N-terminally modified by one or more processing enzymes. Enzymes acting on the very first amino acid of a polypeptide include different peptidases, transferases, and ligases. Methionine aminopeptidases excise the initiator methionine leaving the nascent polypeptide with a newly exposed amino acid that may be further modified. N-terminal acetyl-, methyl-, myristoyl-, and palmitoyltransferases may attach an acetyl, methyl, myristoyl, or palmitoyl group, respectively, to the α-amino group of the target protein N-terminus. With the action of ubiquitin ligases, one or several ubiquitin molecules are transferred, and hence, constitute the N-terminal modification. Modifications at protein N-termini represent an important contribution to proteomic diversity and complexity, and are essential for protein regulation and cellular signaling. Consequently, dysregulation of the N-terminal modifying enzymes is implicated in human diseases. We here review the different protein N-terminal modifications occurring co- or post-translationally with emphasis on the responsible enzymes and their substrate specificities.en_US
dc.publisherWiley-VCH Verlag GmbH & Co. KGaA, Weinheimen_US
dc.rightsAttribution CC BYeng
dc.subjectα-amino groupeng
dc.subjectCell biologyeng
dc.titleN-terminal modifications of cellular proteins: the enzymes involved, their substrate specificities and biological effectsen_US
dc.typePeer reviewed
dc.typeJournal article
dc.rights.holderCopyright 2015 The Authorsen_US
dc.subject.nsiVDP::Medisinske Fag: 700en_US

Tilhørende fil(er)


Denne innførselen finnes i følgende samling(er)

Vis enkel innførsel

Attribution CC BY
Med mindre annet er angitt, så er denne innførselen lisensiert som Attribution CC BY