t(8;21)(q22;q22) Fusion proteins preferentially bind to duplicated AML1/RUNX1 DNA-binding sequences to differentially regulate gene expression. - Wikidata - wikimedia - TriplyDB

t(8;21)(q22;q22) Fusion proteins preferentially bind to duplicated AML1/RUNX1 DNA-binding sequences to differentially regulate gene expression.

t(8;21)(q22;q22) Fusion proteins preferentially bind to duplicated AML1/RUNX1 DNA-binding sequences to differentially regulate gene expression.

http://www.wikidata.org/entity/Q33338784

about

A stable transcription factor complex nucleated by oligomeric AML1–ETO controls leukaemogenesis Runx1 binds as a dimeric complex to overlapping Runx1 sites within a palindromic element in the human GM-CSF enhancer AML1/ETO oncoprotein is directed to AML1 binding regions and co-localizes with AML1 and HEB on its targets.Cbfb/Runx1 repression-independent blockage of differentiation and accumulation of Csf2rb-expressing cells by Cbfb-MYH11.RUNX1 repression-independent mechanisms of leukemogenesis by fusion genes CBFB-MYH11 and AML1-ETO (RUNX1-RUNX1T1).Attenuation of AML1-ETO cellular dysregulation correlates with increased leukemogenic potential.MLL fusion proteins preferentially regulate a subset of wild-type MLL target genes in the leukemic genome.The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation.PRMT1 interacts with AML1-ETO to promote its transcriptional activation and progenitor cell proliferative potential RUNX1 and RUNX1-ETO: roles in hematopoiesis and leukemogenesis.RUNX1/AML1 DNA-binding domain and ETO/MTG8 NHR2-dimerization domain are critical to AML1-ETO9a leukemogenesis.Core binding factor at the crossroads: determining the fate of the HSC.New insights into transcriptional and leukemogenic mechanisms of AML1-ETO and E2A fusion proteins.RUNX1: A microRNA hub in normal and malignant hematopoiesis.Runx1 Structure and Function in Blood Cell Development.The impact of TEL-AML1 (ETV6-RUNX1) expression in precursor B cells and implications for leukaemia using three different genome-wide screening methods.AML1-ETO targets and suppresses cathepsin G, a serine protease, which is able to degrade AML1-ETO in t(8;21) acute myeloid leukemia.Acute myeloid leukemia with the t(8;21) translocation: clinical consequences and biological implications.Heterodimerization of AML1/ETO with CBFβ is required for leukemogenesis but not for myeloproliferation.RUNX1 and CBFβ Mutations and Activities of Their Wild-Type Alleles in AML.RUNX1-ETO Leukemia.The Oncogenic Transcription Factor RUNX1/ETO Corrupts Cell Cycle Regulation to Drive Leukemic Transformation

P2860

Q27678844-2EE9401E-B466-4F43-8DB1-5D8736EA37E3 Q28282851-8D9CEC7D-1CCA-4B5D-B51D-5F50152E995C Q33388188-9C5D9D43-929A-468A-AD4F-E24CECE4496B Q33680301-8E843DEE-BD57-4CE3-9026-37C9A3DDD9D4 Q34621037-AAE0610B-5F56-413A-A05B-C43832E2B255 Q34648630-73A31774-0D7C-4A00-9F5D-2172D138D1F4 Q35083272-F2866A32-54FD-4040-9D0E-805BF420F243 Q35650662-41481514-50F6-431A-A86D-4B31181BE623 Q36010294-05343F90-E54B-4B9B-86C0-4458F36D9AFB Q36206674-FC623C44-6EA4-42AB-85B5-265D46A26863 Q37071117-E319C337-ED1D-45B1-AA90-9D7625F9D058 Q37610919-E539426C-2522-4726-ADF7-4C62DB25B24A Q37679748-23116B8B-1311-4AA6-8DF6-49019053E2A0 Q38076281-B7887356-4050-4D0E-93DA-2FD4DD593EF5 Q38904253-13DA15B4-7C99-43D0-A8EE-0A224D7815AD Q39079942-955E914D-A5C7-4D17-9337-BF1F63773CCD Q39340944-F7C02158-C254-4CC4-8354-9C172DE63814 Q41973082-91AF1640-4CF3-4A2F-AD90-3BF23093212F Q47127883-73601D67-D118-4A0A-A207-22030BCF6696 Q51097615-26E53A0C-AA38-4B72-9EF3-92899F17FADB Q51097627-6A413688-A9DA-40CD-892D-ECF5E96DA920 Q57293716-6F723B9A-384B-4A78-ABC1-D58999BBA89B

P2860

t(8;21)(q22;q22) Fusion proteins preferentially bind to duplicated AML1/RUNX1 DNA-binding sequences to differentially regulate gene expression.

http://www.wikidata.org/entity/Q33338784

description

2008 nî lūn-bûn

@nan

2008 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

t

@nl

t(8;21)(q22;q22) Fusion protei ...... ally regulate gene expression.

@ast

t(8;21)(q22;q22) Fusion protei ...... ally regulate gene expression.

@en

type

label

t

@nl

t(8;21)(q22;q22) Fusion protei ...... ally regulate gene expression.

@ast

t(8;21)(q22;q22) Fusion protei ...... ally regulate gene expression.

@en

prefLabel

t

@nl

t(8;21)(q22;q22) Fusion protei ...... ally regulate gene expression.

@ast

t(8;21)(q22;q22) Fusion protei ...... ally regulate gene expression.

@en

P1433

Q33338784-A295BF6D-4703-441A-81A4-9994E705A05B

P1476

Q33338784-1D682C15-CFF9-4DA1-97F7-243CEE73523A

P2093

Q33338784-09D48F6B-A053-4403-8CBF-F2FF7E5E8228

Q33338784-12FEB09F-FBF3-4AC6-9984-FD5EFBBDDA9F

Q33338784-21848603-6835-4E57-8A37-DCA5C5B0BFB0

Q33338784-2CB1D24F-6B69-4D85-83CC-F6BC7F21CABD

Q33338784-3EA1687A-7F61-4B3E-A9F8-247A0E2FB11A

P2860

Q33338784-01D400B3-0137-440A-AABE-CD25EAA6AF35

Q33338784-0E91FCAC-6AA8-4BC1-9908-F3A2C664EE33

Q33338784-0F0A343D-89D2-4DD7-816F-ECF30CC9C170

Q33338784-14A109DB-FE12-4CCE-A821-1DCD3DAC7F8C

Q33338784-1797B6D8-A4B7-47E8-A32E-36D0C2FABD72

Q33338784-17DB7B6A-F8B2-45DD-891E-7DD1AF0C1304

Q33338784-1CA5EF97-0011-41BB-BF55-D65D7B576F05

Q33338784-2083FD67-B3D5-4A1A-9381-68EEA09120C2

Q33338784-2114D27A-4D42-47F2-981A-71818267C9CA

Q33338784-2FFBB136-DA21-4BA0-B770-D9E51AC12A8E

P304

Q33338784-9709F697-B3D1-4766-B261-31FDD9595C56

P31

Q33338784-5B1248AB-A5E6-4313-B67B-08AA3A793725

P356

Q33338784-3E9416A4-7DA6-42E2-A3FA-617E971D0398

P407

Q33338784-42AF9EBF-D761-4DFE-9443-FD9C230B95B2

P433

Q33338784-30D1CFD9-2AE8-439F-9431-8901E887BE6B

P478

Q33338784-6B66F64F-87D6-4BCE-B625-FD86B5DA8EC0

P577

Q33338784-5ECB4AA7-2357-4377-9F5E-4F740686BAEA

P5875

Q33338784-0ACCE5BF-1037-4FD5-904B-EB013719E681

P698

Q33338784-14A1193B-E162-4E2A-B0E7-27BFBD9A6D5A

P932

Q33338784-3CC44DA9-1E93-4A8B-954D-D4BE0DEEEA68

P356

BLOOD-2007-11-124735

P1433

P1476

t(8;21)(q22;q22) Fusion protei ...... ally regulate gene expression.

@en

P2093

Akiko J Okumura

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

Anita Boyapati

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

Dong-Er Zhang

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

Fumihiko Okumura

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

Luke F Peterson

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

P2860

Processing, localization, and requirement of human separase for normal anaphase progression

STAT3 and MITF cooperatively induce cellular transformation through upregulation of c-fos expression

The tetramer structure of the Nervy homology two domain, NHR2, is critical for AML1/ETO's activity

Identification of AML-1 and the (8;21) translocation protein (AML-1/ETO) as sequence-specific DNA-binding proteins: the runt homology domain is required for DNA binding and protein-protein interactions

ETO, a target of t(8;21) in acute leukemia, interacts with the N-CoR and mSin3 corepressors

The t(8;21) translocation in acute myeloid leukemia results in production of an AML1-MTG8 fusion transcript

Disruption of the Cbfa2 gene causes necrosis and hemorrhaging in the central nervous system and blocks definitive hematopoiesis

Analysis of promoter binding by the E2F and pRB families in vivo: distinct E2F proteins mediate activation and repression

Sequence specificity of the core-binding factor

ETO, fusion partner in t(8;21) acute myeloid leukemia, represses transcription by interaction with the human N-CoR/mSin3/HDAC1 complex

P304

1392-1401

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

P31

scholarly article

P356

10.1182/BLOOD-2007-11-124735

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

P407

P433

4

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

P478

112

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

P577

2008-05-29T00:00:00Z

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

P5875

5338756

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

P698

18511808

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

P932

2515118

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