The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins.
about
Oncogenic homeodomain transcription factor E2A-Pbx1 activates a novel WNT gene in pre-B acute lymphoblastoid leukemiaFunctional cloning and characterization of a novel nonhomeodomain protein that inhibits the binding of PBX1-HOX complexes to DNAPrep2: cloning and expression of a new prep family memberThe AD1 and AD2 transactivation domains of E2A are essential for the antiapoptotic activity of the chimeric oncoprotein E2A-HLFPrep1, a novel functional partner of Pbx proteins.The novel homeoprotein Prep1 modulates Pbx-Hox protein cooperativityPBX and MEIS as non-DNA-binding partners in trimeric complexes with HOX proteinsAbdB-like Hox proteins stabilize DNA binding by the Meis1 homeodomain proteinsMeis1 and pKnox1 bind DNA cooperatively with Pbx1 utilizing an interaction surface disrupted in oncoprotein E2a-Pbx1Lock and key binding of the HOX YPWM peptide to the PBX homeodomainStructure of HoxA9 and Pbx1 bound to DNA: Hox hexapeptide and DNA recognition anterior to posteriorTALE homeoproteins as HOX11-interacting partners in T-cell leukemiaEvolutionary 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 HOXA1Characterization of the DNA-binding properties of the Mohawk homeobox transcription factorMeis proteins are major in vivo DNA binding partners for wild-type but not chimeric Pbx proteinsMinimization of a protein-DNA dimerizerAn 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 evolutionHox 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 motifEngrailed 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 heterodimerControlling 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 cellsConformational changes induced in Hoxb-8/Pbx-1 heterodimers in solution and upon interaction with specific DNAA 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
Q22010579-46884CF5-A330-41C6-9F88-F7F0C6851FCAQ22254126-796C75F4-89BF-405C-9ECF-390F841F105FQ24315315-10C104C5-5B82-4519-B784-1A0DFEE1D006Q24522770-2A13DA8D-F5AA-4E09-B84F-E89B24F982EFQ24533175-4CE1D7A6-2CE1-458C-8879-132644BD4514Q24533177-E65AC3F8-7C28-4053-83C5-F4951871DBFCQ24554397-0DBC319E-CC9E-4184-A0B6-C55C7920CD96Q24644374-8B2A450C-1291-4773-B8A4-CCAE6395FEEDQ24646482-BF7E5133-EA8E-4E7E-B260-D42884B27EEEQ27639896-9AB6B7D8-9CB9-4D5D-99CE-F0581CF5F63BQ27641842-3A568FCD-A678-4E64-AC1B-3124FD6F51CCQ28187803-253310C4-1574-43A4-9C55-B9C4B9BC5239Q28239928-A4B8572F-64B8-4244-9BB3-5D879666ACB5Q28270511-A05DEA1D-3044-436E-9B19-2EA2A1D7B71EQ28508122-D215BDE0-8EC5-42D2-8F85-7D474CDE2A7BQ28588001-87E74D6E-B5E3-4D71-9067-5AA2CDDCFAB4Q30829624-2943B821-9C73-4F08-A5FE-9F5214985A8EQ32036980-319956FE-ED7D-4F0B-B182-C42D39C7CEC0Q32874802-86B5E473-0B08-47DE-8D7F-8F613B9562D8Q33607453-DA3B858C-A48A-40BA-8315-84664A111BFDQ34241617-B03A2DB6-C62F-43E1-BD79-9ACAC96F1CB3Q34321007-53A44056-289D-4896-A870-F70023B6C5BAQ34405471-319481F5-E872-4636-A079-EBE93B4738EBQ34591843-D6AC5EA8-1092-4AB4-8537-5532CC8B71ECQ35647889-FFA3BCAD-E726-41A2-82F3-1A9CF2A76019Q35745756-00F8D105-ACEC-439A-9CD8-FE83B6719E35Q35850266-05032F81-7E46-405C-BE1F-DBC456CC24FCQ35900314-0674281D-E593-497B-94D4-03B325D96437Q36558712-8D51C85B-B682-48FD-948D-D6F98D0079D0Q36564617-46F10946-4DE7-433A-AF24-377538B82EEEQ36570588-2B85E757-FF03-49C3-90AE-EE5B6F04D77DQ37468603-1AA39C48-02BB-4D38-AC2C-F0B77DCE65B4Q37580602-B83321A6-0B02-44BC-95B4-5ECA69C86AD8Q38118219-F8151E12-9A8F-48C1-972F-88C45A1DCE7DQ38154625-1A905905-11D2-4494-8D6D-CAC71B5620DAQ39900581-3C5721B7-C3CC-44CC-9BA4-3126E2FFDD54Q40023342-4716ED9E-26C1-47F3-A309-90E29C0373C1Q40768248-1A0FA97B-DA02-49AF-8B16-A679B1B80BCDQ40863557-53C79D9C-D23F-4792-A775-85694A0DA470Q40955969-0A081846-0AD7-4A5C-AE79-7162C1219DCE
P2860
The hexapeptide LFPWMR in Hoxb-8 is required for cooperative DNA binding with Pbx1 and Pbx2 proteins.
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
P2093
P2860
P356
P1476
The hexapeptide LFPWMR in Hoxb ...... g with Pbx1 and Pbx2 proteins.
@en
P2093
Neuteboom ST
Peltenburg LT
van Dijk MA
P2860
P304
P356
10.1073/PNAS.92.20.9166
P407
P577
1995-09-01T00:00:00Z