Identification of the sequence determinants of protein N-terminal acetylation through a decision tree approach
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1471-2105
- 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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Identification of the sequence determinants of protein N-terminal acetylation through a decision tree approach ; volume:18 ; number:1 ; day:2 ; month:6 ; year:2017 ; pages:1-8 ; date:12.2017
BMC bioinformatics ; 18, Heft 1 (2.6.2017), 1-8, 12.2017
- Classification
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Biowissenschaften, Biologie
- Creator
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Yamada, Kazunori D.
- Contributor
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Omori, Satoshi
Nishi, Hafumi
Miyagi, Masaru
SpringerLink (Online service)
- DOI
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10.1186/s12859-017-1699-4
- URN
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urn:nbn:de:1111-20170702365
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:33 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
- Yamada, Kazunori D.
- Omori, Satoshi
- Nishi, Hafumi
- Miyagi, Masaru
- SpringerLink (Online service)
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N-terminal acetylation can stabilize proteins independent of their ubiquitination
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Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity
Control of protein degradation by N-terminal acetylation and the N-end rule pathway
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
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
News insights into PEXEL-mediated protein export in Plasmodium falciparum : the role of N-terminal acetylation
Spotlight on protein N-terminal acetylation
N-terminal acetylation can stabilize proteins independent of their ubiquitination
N-terminal cysteine acetylation and oxidation patterns may define protein stability
N-terminal sequence-based prediction of subcellular location
Dual lysine and N‐terminal acetyltransferases reveal the complexity underpinning protein acetylation
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity
Control of protein degradation by N-terminal acetylation and the N-end rule pathway
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
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates