Hochschulschrift
Dynamics of H4 K16 acetylation by the SAS-I complex in Saccharomyces cerevisiae
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
Berlin, Humboldt Universität zu Berlin, Diss., 2014
- Klassifikation
-
Biowissenschaften, Biologie
- Ereignis
-
Veröffentlichung
- (wo)
-
Berlin
- (wer)
-
Lebenswissenschaftliche Fakultät
- (wann)
-
2014
- Urheber
- Beteiligte Personen und Organisationen
-
Ehrenhofer-Murray, Ann
Schmitz-Linneweber, Christian
Sers, Christine
- URN
-
urn:nbn:de:kobv:11-100220583
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:46 MESZ
Datenpartner
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Objekttyp
- Hochschulschrift
Beteiligte
- Reiter, Christian
- Ehrenhofer-Murray, Ann
- Schmitz-Linneweber, Christian
- Sers, Christine
- Lebenswissenschaftliche Fakultät
Entstanden
- 2014
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The silencing complex SAS-I links histone acetylation to the assembly of repessed chromatin by CAF-I and Asf1 in saccharomyces cerevisiae
Statistical assessment of the global regulatory role of histone acetylation in Saccharomyces cerevisiae
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Analysis of the role of N-terminal acetylation of newly synthesized proteins in Saccharomyces cerevisiae
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Genome-wide control of H4 K16 acetylation by the SAS-I complex in Saccharomyces cerevisiae
Protein acetylation regulates xylose metabolism during adaptation of Saccharomyces cerevisiae
Physiological role and funcion of Nα-terminal acetylation in Saccharomyces cerevisiae
Nano-electrospray tandem mass spectrometric analysis of the acetylation state of histones H3 and H4 in stationary phase in Saccharomyces cerevisiae
The silencing complex SAS-I links histone acetylation to the assembly of repessed chromatin by CAF-I and Asf1 in saccharomyces cerevisiae
Statistical assessment of the global regulatory role of histone acetylation in Saccharomyces cerevisiae
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Analysis of the role of N-terminal acetylation of newly synthesized proteins in Saccharomyces cerevisiae
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