A requirement for dimerization of HP1Hsalpha in suppression of breast cancer invasion. (Q40285507)

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20 January 2020

title

A requirement for dimerization of HP1Hsalpha in suppression of breast cancer invasion (English)

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20 January 2020

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20 January 2020

Laura E Norwood

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20 January 2020

Timothy J Moss

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20 January 2020

Naira V Margaryan

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Sara L Cook

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20 January 2020

Lindsay Wright

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Elisabeth A Seftor

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Mary J C Hendrix

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20 January 2020

Dawn A Kirschmann

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20 January 2020

language of work or name

English

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publication date

28 April 2006

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Journal of Biological Chemistry

20 January 2020

number of pages

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based on heuristic

inferred from page(s)

published in

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volume

281

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issue

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page(s)

18668-18676

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The biology of metastatic breast cancer

20 January 2020

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Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin

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Selective interaction between the chromatin-remodeling factor BRG1 and the heterochromatin-associated protein HP1alpha

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Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1.

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Conserved properties of HP1(Hsalpha).

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Functional domain structure of human heterochromatin protein HP1(Hsalpha): involvement of internal DNA-binding and C-terminal self-association domains in the formation of discrete dots in interphase nuclei

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Molecular behavior in living mitotic cells of human centromere heterochromatin protein HPLalpha ectopically expressed as a fusion to red fluorescent protein

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The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain

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Molecular determinants for targeting heterochromatin protein 1-mediated gene silencing: direct chromoshadow domain-KAP-1 corepressor interaction is essential

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21 January 2018

Identifiers

DOI

10.1074/JBC.M512454200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16648629%20AND%20SRC:MED&resulttype=core&format=json

20 January 2020

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