(Q28609769)

4

0 references

Paul Tempst

5

object named as

Paul Tempst

0 references

Yi Zhang

object named as

Yi Zhang

7

0 references

Huck Hui Ng

3

object named as

Huck Hui Ng

1 reference

3 February 2017

Qin Feng

1

1 reference

3 February 2017

Hengbin Wang

2

1 reference

3 February 2017

Kevin Struhl

The language of covalent histone modifications

6

1 reference

3 February 2017

language of work or name

English

0 references

publication date

25 June 2002

1 reference

3 February 2017

1 reference

3 February 2017

12

1 reference

3 February 2017

1052–1058

1 reference

3 February 2017

12

1 reference

3 February 2017

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Translating the Histone Code

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Histone methylation in transcriptional control

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Regulation of chromatin structure by site-specific histone H3 methyltransferases

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and methylates histone 3 lysine 4

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Molecular cloning of ESET, a novel histone H3-specific methyltransferase that interacts with ERG transcription factor

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

A trithorax-group complex purified from Saccharomyces cerevisiae is required for methylation of histone H3

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Evidence that Set1, a factor required for methylation of histone H3, regulates rDNA silencing in S. cerevisiae by a Sir2-independent mechanism

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression.

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Crystal structure of the nucleosome core particle at 2.8 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Chromatin silencing protein and pachytene checkpoint regulator Dot1p has a methyltransferase fold

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Role for the silencing protein Dot1 in meiotic checkpoint control

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Stem-loop binding protein, the protein that binds the 3' end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021

Tuning of an electrospray ionization source for maximum peptide-ion transmission into a mass spectrometer

1 reference

https://api.crossref.org/works/10.1016%2FS0960-9822%2802%2900901-6

7 January 2021