Identification of the sequence determinants of protein N-terminal acetylation through a decision tree approach
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1471-2105
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
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
- Klassifikation
-
Biowissenschaften, Biologie
- Urheber
-
Yamada, Kazunori D.
- Beteiligte Personen und Organisationen
-
Omori, Satoshi
Nishi, Hafumi
Miyagi, Masaru
SpringerLink (Online service)
- DOI
-
10.1186/s12859-017-1699-4
- URN
-
urn:nbn:de:1111-20170702365
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:33 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Yamada, Kazunori D.
- Omori, Satoshi
- Nishi, Hafumi
- Miyagi, Masaru
- SpringerLink (Online service)
Ähnliche Objekte (12)
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
Control of protein degradation by N-terminal acetylation and the N-end rule pathway
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity
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
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
Stablization of ACOs by NatB mediated N-terminal acetylation is required for ethylene homeostasis
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
Control of protein degradation by N-terminal acetylation and the N-end rule pathway
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity
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
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
Stablization of ACOs by NatB mediated N-terminal acetylation is required for ethylene homeostasis
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
Control of protein degradation by N-terminal acetylation and the N-end rule pathway
N-terminal acetylation shields proteins from degradation and promotes age-dependent motility and longevity
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
Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
Stablization of ACOs by NatB mediated N-terminal acetylation is required for ethylene homeostasis