Control of protein degradation by N-terminal acetylation and the N-end rule pathway
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2092-6413
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Control of protein degradation by N-terminal acetylation and the N-end rule pathway ; volume:50 ; number:7 ; day:27 ; month:7 ; year:2018 ; pages:1-8 ; date:7.2018
Experimental & molecular medicine ; 50, Heft 7 (27.7.2018), 1-8, 7.2018
- Creator
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Nguyen, Kha The
- Contributor
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Mun, Sang-Hyeon
Lee, Chang-Seok
Hwang, Cheol-Sang
SpringerLink (Online service)
- DOI
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10.1038/s12276-018-0097-y
- URN
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urn:nbn:de:101:1-2018100420511473592462
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:22 AM CEST
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Nguyen, Kha The
- Mun, Sang-Hyeon
- Lee, Chang-Seok
- Hwang, Cheol-Sang
- SpringerLink (Online service)
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Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
Efficient N-Terminal Glycoconjugation of Proteins by the N-End Rule
Spotlight on protein N-terminal acetylation
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity
N-terminal acetylation can stabilize proteins independent of their ubiquitination
N-terminal cysteine acetylation and oxidation patterns may define protein stability
Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
CRL2ZER1/ZYG11B recognizes small N-terminal residues for degradation
Analysis of the role of N-terminal acetylation of newly synthesized proteins in Saccharomyces cerevisiae
Analysis of the role of N-terminal acetylation of newly synthesized proteins in Saccharomyces cerevisiae
Stablization of ACOs by NatB mediated N-terminal acetylation is required for ethylene homeostasis
Identification of the sequence determinants of protein N-terminal acetylation through a decision tree approach
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
Efficient N-Terminal Glycoconjugation of Proteins by the N-End Rule
Spotlight on protein N-terminal acetylation
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity
N-terminal acetylation can stabilize proteins independent of their ubiquitination
N-terminal cysteine acetylation and oxidation patterns may define protein stability
Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
CRL2ZER1/ZYG11B recognizes small N-terminal residues for degradation
Analysis of the role of N-terminal acetylation of newly synthesized proteins in Saccharomyces cerevisiae
Analysis of the role of N-terminal acetylation of newly synthesized proteins in Saccharomyces cerevisiae
Stablization of ACOs by NatB mediated N-terminal acetylation is required for ethylene homeostasis
Identification of the sequence determinants of protein N-terminal acetylation through a decision tree approach
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates