The mammalian basic helix loop helix protein HES-1 binds to and modulates the transactivating function of the runt-related factor Cbfa1
about
MOZ and MORF histone acetyltransferases interact with the Runt-domain transcription factor Runx2The proline-rich homeodomain protein recruits members of the Groucho/Transducin-like enhancer of split protein family to co-repress transcription in hematopoietic cellsOverexpression of the Notch target genes Hes in vivo induces lymphoid and myeloid alterationsMutations in NOTCH1 cause aortic valve diseaseThe winged-helix protein brain factor 1 interacts with groucho and hes proteins to repress transcriptionHey1 basic helix-loop-helix protein plays an important role in mediating BMP9-induced osteogenic differentiation of mesenchymal progenitor cellsGbx2 and Otx2 interact with the WD40 domain of Groucho/Tle corepressorsHes6 promotes cortical neurogenesis and inhibits Hes1 transcription repression activity by multiple mechanismsHES6 acts as a transcriptional repressor in myoblasts and can induce the myogenic differentiation programCell Fate and Differentiation of Bone Marrow Mesenchymal Stem CellsNotch regulation of bone development and remodeling and related skeletal disordersAML1 interconnected pathways of leukemogenesisPhysical interaction of the activator protein-1 factors c-Fos and c-Jun with Cbfa1 for collagenase-3 promoter activationAP-1 and Cbfa/runt physically interact and regulate parathyroid hormone-dependent MMP13 expression in osteoblasts through a new osteoblast-specific element 2/AP-1 composite elementA molecular insight of Hes5-dependent inhibition of myelin gene expression: old partners and new playersThe Notch-responsive transcription factor Hes-1 attenuates osteocalcin promoter activity in osteoblastic cellsGrowth defect in Grg5 null mice is associated with reduced Ihh signaling in growth platesAntagonistic effects of Grg6 and Groucho/TLE on the transcription repression activity of brain factor 1/FoxG1 and cortical neuron differentiation.The Groucho-related gene family regulates the gonadotropin-releasing hormone gene through interaction with the homeodomain proteins MSX1 and OCT1Groucho oligomerization is required for repression in vivoCellular corepressor TLE2 inhibits replication-and-transcription- activator-mediated transactivation and lytic reactivation of Kaposi's sarcoma-associated herpesvirus.Notch and the skeleton.Transcriptional regulation of the human growth hormone receptor (hGHR) gene V2 promoter by transcriptional activators and repressor.Molecular characterization of the mouse superior lateral parabrachial nucleus through expression of the transcription factor Runx1.Cooperation between the GATA and RUNX factors Serpent and Lozenge during Drosophila hematopoiesis.The corepressor Tle4 is a novel regulator of murine hematopoiesis and bone development.A role for cell cycle-regulated phosphorylation in Groucho-mediated transcriptional repression.Establishment of motor neuron-V3 interneuron progenitor domain boundary in ventral spinal cord requires Groucho-mediated transcriptional corepression.AES/GRG5: more than just a dominant-negative TLE/GRG family memberAML1 and the AML1-ETO fusion protein in the pathogenesis of t(8;21) AML.Common themes in the pathogenesis of acute myeloid leukemia.Role for Hes1-induced phosphorylation in Groucho-mediated transcriptional repression.HES1 (hairy and enhancer of split 1) is a determinant of bone massDifferent effects of BMP-2 on marrow stromal cells from human and rat bone.Hairless is a cofactor for Runt-dependent transcriptional regulationOsteogenic oxysterol, 20(S)-hydroxycholesterol, induces notch target gene expression in bone marrow stromal cells.The orphan nuclear receptor SHP is a positive regulator of osteoblastic bone formation.Jagged1 functions downstream of Twist1 in the specification of the coronal suture and the formation of a boundary between osteogenic and non-osteogenic cellsRUNX1 mutations in clonal myeloid disorders: from conventional cytogenetics to next generation sequencing, a story 40 years in the makingSignaling networks that control the lineage commitment and differentiation of bone cells.
P2860
Q24294814-FF6DE98D-C9C4-4DED-97E6-CF98B4C43A97Q24296022-F09FCE86-71C9-4C95-9A9A-D57A6FA696CEQ24298328-878CCB28-312F-4D4D-9E0B-D53A4C5C4D31Q24307999-839266B6-3C03-47C0-A0EF-CFF7E48F59E9Q24550999-04EAA2F2-6763-4274-8D74-8C29F4AF6382Q24655929-C37B2BC1-1EF6-41CB-BD26-FE6BEB31D4B0Q24674174-711E8A43-7F03-4100-9FA4-5DF0FF24ABC9Q24682396-57C2C972-1C44-46F7-923E-F0AED8391D76Q24685454-2E0F4639-9416-44B5-BB1D-8A6296343FFBQ26746170-6F185FAF-DC47-4B16-8B2A-4AE0A4BE82B7Q27021132-E973F014-1CC7-47CD-8449-509D94275829Q28184349-4F02ABF7-7F63-4019-91BC-0D66B9BE9F7DQ28201036-8956FE98-B512-4748-BF07-581B9665864CQ28207292-0A5DDB54-F8B2-4F79-A1F5-3638B066CB99Q28571754-59F4040B-783C-439C-B06E-27C30766C756Q28581307-67417BA9-0353-4E6A-9447-4511F460C432Q28587801-D7DC4ACC-35F9-4FB6-B2BE-D79C43021738Q28590799-967E4F47-22A9-44D7-BC4A-550F2CE332DBQ28593624-F8982828-515A-47ED-945B-C6132437A17FQ28609105-B4DEAFB8-DFBA-40E9-B254-B3363F02BF57Q30919397-D48BE481-41ED-45B6-B418-43B736CFE74EQ33627230-10EC0D79-5FB8-49D7-808E-A4BCA2BF119AQ33670512-FF230E40-EA83-4140-AD16-273D60F058CAQ33750147-C230FE1B-A3E4-4654-832B-8F87F200DC1CQ34052123-2A65CF54-EDBF-4167-A726-F9CF131DF87AQ34083894-C8F4B034-A2D7-4DEB-ABE5-C5CADA3DC752Q34156059-0C13B32F-1B0E-42CF-98EF-1246D7179C54Q34170575-BAB2CF56-E8A4-41A1-8C9D-EFFE9A116649Q34381620-5F19AC0A-E5E8-4275-9A70-45824461B43FQ34405452-AC72E612-86B3-4C64-B3B6-59FF5E21E78BQ34405458-D8E1DD8D-0785-41CD-9054-5D4B63F333D4Q34440560-F67F0C7E-AD5D-482A-BCDB-D87040510838Q34509386-11D42171-5EBF-4755-B43A-1A27841721C0Q34620442-F39C1F33-2833-4018-A5F0-5893C867CDC5Q34803072-6A55C10C-AEED-4B87-AF20-BCC248895D53Q35156070-3B70131B-5DC3-43EF-B1E8-EF224CD907E9Q35156238-0C0B6944-9DD4-4D05-953E-C4289A2F0410Q35533475-7E4B94F9-8F21-48B0-A880-50AAF27DAA9AQ35642451-D270C654-741B-4192-87D3-4FE562B09AEDQ36082866-2E24D436-2DE3-43D9-B074-CB7D9E054213
P2860
The mammalian basic helix loop helix protein HES-1 binds to and modulates the transactivating function of the runt-related factor Cbfa1
description
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2000
@ast
im Januar 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/01/07)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/01/07)
@nl
наукова стаття, опублікована в січні 2000
@uk
name
The mammalian basic helix loop ...... the runt-related factor Cbfa1
@ast
The mammalian basic helix loop ...... the runt-related factor Cbfa1
@en
The mammalian basic helix loop ...... the runt-related factor Cbfa1
@nl
type
label
The mammalian basic helix loop ...... the runt-related factor Cbfa1
@ast
The mammalian basic helix loop ...... the runt-related factor Cbfa1
@en
The mammalian basic helix loop ...... the runt-related factor Cbfa1
@nl
prefLabel
The mammalian basic helix loop ...... the runt-related factor Cbfa1
@ast
The mammalian basic helix loop ...... the runt-related factor Cbfa1
@en
The mammalian basic helix loop ...... the runt-related factor Cbfa1
@nl
P2093
P2860
P3181
P356
P1476
The mammalian basic helix loop ...... the runt-related factor Cbfa1
@en
P2093
G Karsenty
K Thirunavukkarasu
K W McLarren
P2860
P304
P3181
P356
10.1074/JBC.275.1.530
P407
P577
2000-01-01T00:00:00Z