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Unraveling heterochromatin
scientific article published in March 2002
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scholarly article
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title
Unraveling heterochromatin
(English)
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author
Scott D Briggs
object named as
Scott D. Briggs
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1
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Brian D Strahl
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Brian D. Strahl
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2
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language of work or name
English
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publication date
March 2002
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published in
Nature Genetics
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volume
30
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page(s)
241-242
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issue
3
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exact match
https://scigraph.springernature.com/pub.10.1038/ng0302-241
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cites work
The language of covalent histone modifications
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https://api.crossref.org/works/10.1038%2FNG0302-241
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7 January 2021
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Translating the Histone Code
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https://api.crossref.org/works/10.1038%2FNG0302-241
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7 January 2021
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Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNG0302-241
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7 January 2021
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Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability
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https://api.crossref.org/works/10.1038%2FNG0302-241
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7 January 2021
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Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3.
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https://api.crossref.org/works/10.1038%2FNG0302-241
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7 January 2021
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Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
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https://api.crossref.org/works/10.1038%2FNG0302-241
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7 January 2021
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Regulation of chromatin structure by site-specific histone H3 methyltransferases
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reference URL
https://api.crossref.org/works/10.1038%2FNG0302-241
retrieved
7 January 2021
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Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNG0302-241
retrieved
7 January 2021
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Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2FNG0302-241
retrieved
7 January 2021
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Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNG0302-241
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Chromodomains are protein-RNA interaction modules
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNG0302-241
retrieved
7 January 2021
based on heuristic
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Differentially methylated forms of histone H3 show unique association patterns with inactive human X chromosomes
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNG0302-241
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Histone H3 lysine 9 methylation is an epigenetic imprint of facultative heterochromatin.
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2FNG0302-241
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Methylation of histone H3 at Lys-9 is an early mark on the X chromosome during X inactivation
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reference URL
https://api.crossref.org/works/10.1038%2FNG0302-241
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7 January 2021
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Identifiers
DOI
10.1038/NG0302-241
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PubMed ID
11919553
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