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Modulations of hMOF autoacetylation by SIRT1 regulate hMOF recruitment and activities on the chromatin
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3193486
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29 January 2020
title
Modulations of hMOF autoacetylation by SIRT1 regulate hMOF recruitment and activities on the chromatin
(English)
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3193486
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29 January 2020
author
De-Pei Liu
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5
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3193486
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29 January 2020
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Lu Lu
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1
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3193486
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29 January 2020
Lei Li
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2
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29 January 2020
Xiang Lv
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3
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29 January 2020
Xue-Song Wu
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4
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3193486
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29 January 2020
Chih-Chuan Liang
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6
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3193486
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29 January 2020
publication date
19 April 2011
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29 January 2020
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Cell Research
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3193486
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29 January 2020
volume
21
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3193486
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29 January 2020
issue
8
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3193486
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29 January 2020
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1182-1195
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3193486
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29 January 2020
exact match
https://scigraph.springernature.com/pub.10.1038/cr.2011.71
0 references
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Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1
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PubMed Central
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MOF and histone H4 acetylation at lysine 16 are critical for DNA damage response and double-strand break repair
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12 July 2018
SIRT1 regulates autoacetylation and histone acetyltransferase activity of TIP60
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SIRT1 suppresses activator protein-1 transcriptional activity and cyclooxygenase-2 expression in macrophages
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12 July 2018
Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex
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12 July 2018
Two mammalian MOF complexes regulate transcription activation by distinct mechanisms
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MYST family histone acetyltransferases take center stage in stem cells and development.
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Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes
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Lysine acetylation targets protein complexes and co-regulates major cellular functions
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Lysine acetylation: codified crosstalk with other posttranslational modifications
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SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation
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Automethylation of G9a and its implication in wider substrate specificity and HP1 binding
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The diverse biological roles of MYST histone acetyltransferase family proteins.
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SIRT1 interacts with p73 and suppresses p73-dependent transcriptional activity
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SirT2 is a histone deacetylase with preference for histone H4 Lys 16 during mitosis
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Inhibition of SIRT1 reactivates silenced cancer genes without loss of promoter DNA hypermethylation
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Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila
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Histone H4-K16 acetylation controls chromatin structure and protein interactions
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A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16
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12 July 2018
hMOF histone acetyltransferase is required for histone H4 lysine 16 acetylation in mammalian cells
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PubMed Central
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12 July 2018
Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF
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12 July 2018
Involvement of human MOF in ATM function
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12 July 2018
SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1
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12 July 2018
Human SirT1 interacts with histone H1 and promotes formation of facultative heterochromatin
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12 July 2018
Lysine acetylation and the bromodomain: a new partnership for signaling
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12 July 2018
Functional integration of the histone acetyltransferase MOF into the dosage compensation complex
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PubMed Central
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12 July 2018
Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase
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12 July 2018
Mechanisms of P/CAF auto-acetylation
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12 July 2018
Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state
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12 July 2018
Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1- and HEY2-mediated transcriptional repression
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Tip60 acetyltransferase activity is controlled by phosphorylation
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12 July 2018
hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3193486
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12 July 2018
The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition
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12 July 2018
Acetylation: a regulatory modification to rival phosphorylation?
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12 July 2018
The amino-terminal tails of the core histones and the translational position of the TATA box determine TBP/TFIIA association with nucleosomal DNA.
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12 July 2018
The nonspecific lethal complex is a transcriptional regulator in Drosophila
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3193486
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26 September 2018
Partitioning of histone H3-H4 tetramers during DNA replication-dependent chromatin assembly
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26 September 2018
MSL complex is attracted to genes marked by H3K36 trimethylation using a sequence-independent mechanism
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26 September 2018
Acetylation of the p53 DNA-binding domain regulates apoptosis induction
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26 September 2018
A mechanism for coordinating chromatin modification and preinitiation complex assembly.
1 reference
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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3193486
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26 September 2018
NAD+-dependent modulation of chromatin structure and transcription by nucleosome binding properties of PARP-1.
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PubMed Central
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26 September 2018
Activation of transcription through histone H4 acetylation by MOF, an acetyltransferase essential for dosage compensation in Drosophila.
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3193486
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26 September 2018
Targeting of MOF, a putative histone acetyl transferase, to the X chromosome of Drosophila melanogaster.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3193486
retrieved
26 September 2018
Identifiers
DOI
10.1038/CR.2011.71
1 reference
stated in
Europe PubMed Central
PMCID
3193486
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21502975%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 January 2020
PMCID
3193486
1 reference
stated in
Europe PubMed Central
PMCID
3193486
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21502975%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 January 2020
PubMed ID
21502975
1 reference
stated in
Europe PubMed Central
PMCID
3193486
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21502975%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 January 2020
ResearchGate publication ID
51060695
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