RET finger protein is a transcriptional repressor and interacts with enhancer of polycomb that has dual transcriptional functions (Q24290200)

Tripartite motif containing 27

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positive regulation of transcription by RNA polymerase II

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Enhancer of polycomb homolog 1

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Tripartite motif-containing 27

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Journal of Biological Chemistry

Y Shimono

1

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author name string

H Murakami

series ordinal

2

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Y Hasegawa

series ordinal

3

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M Takahashi

series ordinal

4

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language of work or name

English

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publication date

15 December 2000

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published in

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volume

275

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issue

50

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page(s)

39411-9

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cites work

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A novel zinc finger coiled-coil domain in a family of nuclear proteins

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B30.2-like domain proteins: update and new insights into a rapidly expanding family of proteins

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RFP is a DNA binding protein associated with the nuclear matrix

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RING domains: master builders of molecular scaffolds?

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RING fingers and B-boxes: zinc-binding protein-protein interaction domains

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Does this have a familiar RING?

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The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control

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Identification and characterization of interactions between the vertebrate polycomb-group protein BMI1 and human homologs of polyhomeotic

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RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor

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RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity

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Molecular analysis of acute promyelocytic leukemia breakpoint cluster region on chromosome 17

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The PML-RARα fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR

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A RING finger motif regulates transforming activity of the rfp/ret fusion gene

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Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RARα with a novel putative transcription factor, PML

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Activation of a novel human transforming gene, ret, by DNA rearrangement

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Functions of mammalian Polycomb group and trithorax group related genes

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PcG complexes and chromatin silencing

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Polycomb group protein complexes: do different complexes regulate distinct target genes?

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Genetic interactions and dosage effects of Polycomb group genes of Drosophila.

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Mammalian homologues of the Polycomb-group gene Enhancer of zeste mediate gene silencing in Drosophila heterochromatin and at S. cerevisiae telomeres

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Characterization of the promoter region of the human RFP gene

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HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and has transcriptional repression properties

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Transcriptional repression by Drosophila and mammalian Polycomb group proteins in transfected mammalian cells

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Identification of a novel nuclear domain

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PML-containing nuclear bodies: their spatial distribution in relation to other nuclear components

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A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein

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Nuclear dots: actors on many stages

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Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body.

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Promyelocytic leukemia (PML) nuclear bodies are protein structures that do not accumulate RNA

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ret transforming gene encodes a fusion protein homologous to tyrosine kinases

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The Drosophila esc and E(z) proteins are direct partners in polycomb group-mediated repression

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Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation

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Different nuclear/cytoplasmic distributions of RET finger protein in different cell types

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mel-18 negatively regulates cell cycle progression upon B cell antigen receptor stimulation through a cascade leading to c-myc/cdc25

21 January 2018

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The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes

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inferred from DOI database lookup

7 January 2021

based on heuristic

The Polycomb-group gene, extra sex combs, encodes a nuclear member of the WD-40 repeat family.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M006585200

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1074/JBC.M006585200

1 reference

Consolidated OpenCitations Corpus – April 2017

3162337

3162337

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference