Delta-like 3 is silenced by HBx via histone acetylation in HBV-associated HCCs
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2045-2322
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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online resource.
- Erschienen in
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Delta-like 3 is silenced by HBx via histone acetylation in HBV-associated HCCs ; volume:8 ; number:1 ; day:19 ; month:3 ; year:2018 ; pages:1-11 ; date:12.2018
Scientific reports ; 8, Heft 1 (19.3.2018), 1-11, 12.2018
- Urheber
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Hamamoto, Hiroki
- Beteiligte Personen und Organisationen
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Maemura, Kentaro
Matsuo, Kentaro
Taniguchi, Kohei
Tanaka, Yoshihisa
Futaki, Sugiko
Takeshita, Atsushi
Asai, Akira
Hayashi, Michihiro
Hirose, Yoshinobu
Kondo, Yoichi
Uchiyama, Kazuhisa
SpringerLink (Online service)
- DOI
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10.1038/s41598-018-23318-1
- URN
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urn:nbn:de:1111-201805176966
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:51 MESZ
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Beteiligte
- Hamamoto, Hiroki
- Maemura, Kentaro
- Matsuo, Kentaro
- Taniguchi, Kohei
- Tanaka, Yoshihisa
- Futaki, Sugiko
- Takeshita, Atsushi
- Asai, Akira
- Hayashi, Michihiro
- Hirose, Yoshinobu
- Kondo, Yoichi
- Uchiyama, Kazuhisa
- SpringerLink (Online service)
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Cancer cell histone density links global histone acetylation, mitochondrial proteome and histone acetylase inhibitor sensitivity
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Histone acetylation and expression of corresponding histone actyltransferases in human abdominal aortic aneurysm
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A new approach to the function of histone acetylation
Histone chaperone exploits intrinsic disorder to switch acetylation specificity
Systematic analysis of histone acetylation regulators across human cancers
Differential patterns of histone acetylation in inflammatory bowel diseases
Histone acetylation in neuronal (dys) function
Transcription shapes genome-wide histone acetylation patterns
Nitric oxide affects histone acetylation by inhibiting histone deacetylase activity in Arabidopsis
Histone acetylation and the role of histone deacetylases in normal cyclic endometrium
Cancer cell histone density links global histone acetylation, mitochondrial proteome and histone acetylase inhibitor sensitivity
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Histone chaperone exploits intrinsic disorder to switch acetylation specificity
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