The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation
about
Novel roles of holocarboxylase synthetase in gene regulation and intermediary metabolismHolocarboxylase synthetase interacts physically with nuclear receptor co-repressor, histone deacetylase 1 and a novel splicing variant of histone deacetylase 1 to repress repeatsHolocarboxylase synthetase interacts physically with euchromatic histone-lysine N-methyltransferase, linking histone biotinylation with methylation events.The role of holocarboxylase synthetase in genome stability is mediated partly by epigenomic synergies between methylation and biotinylation events.
P2860
The polypeptide Syn67 interacts physically with human holocarboxylase synthetase, but is not a target for biotinylation
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年学术文章
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2009年學術文章
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2009年學術文章
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2009年學術文章
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name
The polypeptide Syn67 interact ...... not a target for biotinylation
@en
The polypeptide Syn67 interact ...... not a target for biotinylation
@nl
type
label
The polypeptide Syn67 interact ...... not a target for biotinylation
@en
The polypeptide Syn67 interact ...... not a target for biotinylation
@nl
prefLabel
The polypeptide Syn67 interact ...... not a target for biotinylation
@en
The polypeptide Syn67 interact ...... not a target for biotinylation
@nl
P2093
P2860
P1476
The polypeptide Syn67 interact ...... not a target for biotinylation
@en
P2093
Hideaki Moriyama
Janos Zempleni
Yousef I Hassan
P2860
P356
10.1016/J.ABB.2009.12.017
P407
P577
2009-12-21T00:00:00Z