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N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and lon...

N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and lon...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2709202327

N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity

About this item

Full title

N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

Journal title

bioRxiv, 2022-09

Language

English

Formats

Publication information

Publisher

Cold Spring Harbor: Cold Spring Harbor Laboratory Press

More information

Scope and Contents

Contents

Most eukaryotic proteins are N-terminally acetylated, but the functional impact on a global scale has remained obscure. Using genome-wide CRISPR knockout screens in human cells, we reveal a strong genetic dependency between a major N-terminal acetyltransferase and specific ubiquitin ligases. Biochemical analyses uncover that both the ubiquitin liga...

Alternative Titles

Full title

N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_2709202327

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2709202327

Other Identifiers

E-ISSN

2692-8205

DOI

10.1101/2022.09.01.505523