The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins. - Wikidata - awgldk - TriplyDB

The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins.

The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins.

http://www.wikidata.org/entity/Q33889933

about

Oncogenic homeodomain transcription factor E2A-Pbx1 activates a novel WNT gene in pre-B acute lymphoblastoid leukemia Functional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNA Prep2: cloning and expression of a new prep family member The AD1 and AD2 transactivation domains of E2A are essential for the antiapoptotic activity of the chimeric oncoprotein E2A-HLF Prep1, a novel functional partner of Pbx proteins.The novel homeoprotein Prep1 modulates Pbx-Hox protein cooperativity PBX and MEIS as non-DNA-binding partners in trimeric complexes with HOX proteins AbdB-like Hox proteins stabilize DNA binding by the Meis1 homeodomain proteins Meis1 and pKnox1 bind DNA cooperatively with Pbx1 utilizing an interaction surface disrupted in oncoprotein E2a-Pbx1 Lock and key binding of the HOX YPWM peptide to the PBX homeodomain Structure of HoxA9 and Pbx1 bound to DNA: Hox hexapeptide and DNA recognition anterior to posterior TALE homeoproteins as HOX11-interacting partners in T-cell leukemia Evolutionary silencing of the human elastase I gene (ELA1)A conserved C-terminal domain in PBX increases DNA binding by the PBX homeodomain and is not a primary site of contact for the YPWM motif of HOXA1 Characterization of the DNA-binding properties of the Mohawk homeobox transcription factor Meis proteins are major in vivo DNA binding partners for wild-type but not chimeric Pbx proteins Minimization of a protein-DNA dimerizer An endocrine-exocrine switch in the activity of the pancreatic homeodomain protein PDX1 through formation of a trimeric complex with PBX1b and MRG1 (MEIS2).The Abd-B-like Hox homeodomain proteins can be subdivided by the ability to form complexes with Pbx1a on a novel DNA target.Hox specificity unique roles for cofactors and collaborators.Surprising flexibility in a conserved Hox transcription factor over 550 million years of evolution Hox proteins display a common and ancestral ability to diversify their interaction mode with the PBC class cofactors.The role of E2A-PBX1 in leukemogenesis.Hox homeodomain proteins exhibit selective complex stabilities with Pbx and DNA.Homeobox genes in obsessive-compulsive disorder.Pbx proteins cooperate with Engrailed to pattern the midbrain-hindbrain and diencephalic-mesencephalic boundaries.An extradenticle-induced conformational change in a HOX protein overcomes an inhibitory function of the conserved hexapeptide motif Engrailed and Hox homeodomain proteins contain a related Pbx interaction motif that recognizes a common structure present in Pbx.Pbx modulation of Hox homeodomain amino-terminal arms establishes different DNA-binding specificities across the Hox locus.The Hox cooperativity motif of the chimeric oncoprotein E2a-Pbx1 is necessary and sufficient for oncogenesis.Pbx raises the DNA binding specificity but not the selectivity of antennapedia Hox proteins.Non-homeodomain regions of Hox proteins mediate activation versus repression of Six2 via a single enhancer site in vivo.A structural model for a homeotic protein-extradenticle-DNA complex accounts for the choice of HOX protein in the heterodimer Controlling Hox gene expression and activity to build the vertebrate axial skeleton.Glutamate drugs and pharmacogenetics of OCD: a pathway-based exploratory approach.The truncated Hoxa1 protein interacts with Hoxa1 and Pbx1 in stem cells Conformational changes induced in Hoxb-8/Pbx-1 heterodimers in solution and upon interaction with specific DNA A nuclear antagonistic mechanism of inhibitory Smads in transforming growth factor-beta signaling.Gtx, an oligodendrocyte-specific homeodomain protein, has repressor activity.Control of brain patterning by Engrailed paracrine transfer: a new function of the Pbx interaction domain.

P2860

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P2860

The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins.

http://www.wikidata.org/entity/Q33889933

description

1995 nî lūn-bûn

@nan

1995 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

1995年の論文

@ja

1995年論文

@yue

1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

@wuu

name

The hexapeptide LFPWMR in Hoxb ...... g with Pbx1 and Pbx2 proteins.

@ast

The hexapeptide LFPWMR in Hoxb ...... g with Pbx1 and Pbx2 proteins.

@en

type

label

The hexapeptide LFPWMR in Hoxb ...... g with Pbx1 and Pbx2 proteins.

@ast

The hexapeptide LFPWMR in Hoxb ...... g with Pbx1 and Pbx2 proteins.

@en

prefLabel

The hexapeptide LFPWMR in Hoxb ...... g with Pbx1 and Pbx2 proteins.

@ast

The hexapeptide LFPWMR in Hoxb ...... g with Pbx1 and Pbx2 proteins.

@en

P1433

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P1476

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P2860

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P932

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P356

PNAS.92.20.9166

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

The hexapeptide LFPWMR in Hoxb ...... g with Pbx1 and Pbx2 proteins.

@en

P2093

Murre C

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

Neuteboom ST

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Peltenburg LT

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van Dijk MA

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P2860

PBX2 and PBX3, new homeobox genes with extensive homology to the human proto-oncogene PBX1

Pbx1 is converted into a transcriptional activator upon acquiring the N-terminal region of E2A in pre-B-cell acute lymphoblastoid leukemia

Structural relationships among genes that control development: sequence homology between the Antennapedia, Ultrabithorax, and fushi tarazu loci of Drosophila

Fusion with E2A converts the Pbx1 homeodomain protein into a constitutive transcriptional activator in human leukemias carrying the t(1;19) translocation

A new homeobox gene contributes the DNA binding domain of the t(1;19) translocation protein in pre-B ALL

Pbx proteins display hexapeptide-dependent cooperative DNA binding with a subset of Hox proteins

Hox genes in vertebrate development

Sequence of a Drosophila segmentation gene: protein structure homology with DNA-binding proteins.

A conserved DNA sequence in homoeotic genes of the Drosophila Antennapedia and bithorax complexes.

Extradenticle protein is a selective cofactor for the Drosophila homeotics: role of the homeodomain and YPWM amino acid motif in the interaction

P304

9166-9170

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P31

scholarly article

P356

10.1073/PNAS.92.20.9166

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P407

P433

20

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P478

92

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P577

1995-09-01T00:00:00Z

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P5875

15631212

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P698

7568094

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P932

40945

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