(Q33761102)

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An Ash2L/RbBP5 heterodimer stimulates the MLL1 methyltransferase activity through coordinated substrate interactions with the MLL1 SET domain

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scholarly article

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Europe PubMed Central

PubMed publication ID

29 July 2017

An Ash2L/RbBP5 heterodimer stimulates the MLL1 methyltransferase activity through coordinated substrate interactions with the MLL1 SET domain (English)

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Europe PubMed Central

PubMed publication ID

29 July 2017

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Yong Chen

2

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author name string

Fang Cao

1

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Europe PubMed Central

PubMed publication ID

29 July 2017

Tomasz Cierpicki

3

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Europe PubMed Central

PubMed publication ID

29 July 2017

Yifan Liu

4

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Europe PubMed Central

PubMed publication ID

29 July 2017

Venkatesha Basrur

5

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Europe PubMed Central

PubMed publication ID

29 July 2017

Ming Lei

6

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Europe PubMed Central

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29 July 2017

Yali Dou

7

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29 July 2017

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publication date

23 November 2010

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Europe PubMed Central

PubMed publication ID

29 July 2017

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Europe PubMed Central

PubMed publication ID

29 July 2017

5

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Europe PubMed Central

PubMed publication ID

29 July 2017

11

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Europe PubMed Central

PubMed publication ID

29 July 2017

e14102

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Europe PubMed Central

PubMed publication ID

29 July 2017

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Creative Commons Attribution 4.0 International

23 November 2010

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April 2022 Public Data File from Crossref

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1 reference

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1 reference

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Universal screening methods and applications of ThermoFluor

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Protein interactions within the Set1 complex and their roles in the regulation of histone 3 lysine 4 methylation

1 reference

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1 reference

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Relationship between SPRY and B30.2 protein domains. Evolution of a component of immune defence?

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CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex

1 reference

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The SET-domain protein superfamily: protein lysine methyltransferases

1 reference

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Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF

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WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development

1 reference

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Global and Hox-specific roles for the MLL1 methyltransferase

1 reference

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inferred from PubMed ID database lookup

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10.1371/JOURNAL.PONE.0014102

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

2010PLoSO...514102C

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PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 July 2017

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