BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

about

LncRNA ZFAS1 promotes growth and metastasis by regulating BMI1 and ZEB2 in osteosarcoma.BMI1 regulates androgen receptor in prostate cancer independently of the polycomb repressive complex 1.Critical Role of the UBL Domain in Stimulating the E3 Ubiquitin Ligase Activity of UHRF1 toward Chromatin

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P2860

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

Item

http://www.wikidata.org/entity/Q37408672

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

@zh-my

2016年学术文章

@zh-sg

2016年學術文章

@yue

2016年學術文章

@zh

2016年學術文章

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name

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

@en

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

@nl

type

Item

label

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

@en

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

@nl

prefLabel

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

@en

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

@nl

P1476

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

@en

P2093

Ashley Harris

http://www.w3.org/2001/XMLSchema#string

Bohdan Boytsov

http://www.w3.org/2001/XMLSchema#string

Borries Demeler

http://www.w3.org/2001/XMLSchema#string

Elizabeth R Lawlor

http://www.w3.org/2001/XMLSchema#string

Felicia Gray

http://www.w3.org/2001/XMLSchema#string

Hyo Je Cho

http://www.w3.org/2001/XMLSchema#string

Jolanta Grembecka

http://www.w3.org/2001/XMLSchema#string

Shihan He

http://www.w3.org/2001/XMLSchema#string

Shirish Shukla

http://www.w3.org/2001/XMLSchema#string

Tomasz Cierpicki

http://www.w3.org/2001/XMLSchema#string

P2860

Polycomb group targeting through different binding partners of RING1B C-terminal domain

Role of histone H2A ubiquitination in Polycomb silencing

Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b

Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex

Interaction proteomics analysis of polycomb proteins defines distinct PRC1 complexes in mammalian cells

Control of the replicative life span of human fibroblasts by p16 and the polycomb protein Bmi-1

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

BMI-1 promotes ewing sarcoma tumorigenicity independent of CDKN2A repression

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Processing of X-ray diffraction data collected in oscillation mode

P2888

ncomms13343

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13343

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scholarly article

P356

10.1038/NCOMMS13343

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English

P478

http://www.w3.org/2001/XMLSchema#string

P50

Mariusz Jaremko

Łukasz Jaremko

P577

2016-11-09T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

27827373

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P932

5105191

http://www.w3.org/2001/XMLSchema#string

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

about

P2860

P2860

BMI1 regulates PRC1 architecture and activity through homo- and hetero-oligomerization.

description

name

type

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prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P698

P932

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P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P698

P932