Histone deacetylase 3 indirectly modulates tubulin acetylation

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Microtubule dynamics decoded by the epigenetic state of centromeric chromatin.Tubastatin ameliorates pulmonary fibrosis by targeting the TGFβ-PI3K-Akt pathway.HDAC3 promotes meiotic apparatus assembly in mouse oocytes by modulating tubulin acetylation.

P2860

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P2860

Histone deacetylase 3 indirectly modulates tubulin acetylation

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2015年論文

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2015年論文

@zh-hk

2015年論文

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name

Histone deacetylase 3 indirectly modulates tubulin acetylation

@en

Histone deacetylase 3 indirectly modulates tubulin acetylation

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label

Histone deacetylase 3 indirectly modulates tubulin acetylation

@en

Histone deacetylase 3 indirectly modulates tubulin acetylation

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Histone deacetylase 3 indirectly modulates tubulin acetylation

@en

Histone deacetylase 3 indirectly modulates tubulin acetylation

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P1154

2-s2.0-84955456212

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P1433

Biochemical Journal

P1476

Histone deacetylase 3 indirectly modulates tubulin acetylation

@en

P2093

Caroline Seiler

http://www.w3.org/2001/XMLSchema#string

Peter Watson

http://www.w3.org/2001/XMLSchema#string

Ronald Grigg

http://www.w3.org/2001/XMLSchema#string

P2860

Histone deacetylases specifically down-regulate p53-dependent gene activation

Enzymatic activity associated with class II HDACs is dependent on a multiprotein complex containing HDAC3 and SMRT/N-CoR

The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase

HDAC6 is a microtubule-associated deacetylase

Histone deacetylase 3 localizes to the mitotic spindle and is required for kinetochore-microtubule attachment.

Expression of histone deacetylase 8, a class I histone deacetylase, is restricted to cells showing smooth muscle differentiation in normal human tissues

Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex

EB1 recognizes the nucleotide state of tubulin in the microtubule lattice

Structure of HDAC3 bound to co-repressor and inositol tetraphosphate

Class I HDACs Share a Common Mechanism of Regulation by Inositol Phosphates

P304

367-377

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P31

scholarly article

P356

10.1042/BJ20150660

http://www.w3.org/2001/XMLSchema#string

P407

English

P433

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P478

472

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P5530

4736927

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P577

2015-10-08T00:00:00Z

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P6179

1007120983

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P6366

2180646329

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26450925

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4661566

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92047/