The oncogenic capacity of HRX-ENL requires the transcriptional transactivation activity of ENL and the DNA binding motifs of HRX.
about
AF5q31, a newly identified AF4-related gene, is fused to MLL in infant acute lymphoblastic leukemia with ins(5;11)(q31;q13q23)Cloning of a mammalian transcriptional activator that binds unmethylated CpG motifs and shares a CXXC domain with DNA methyltransferase, human trithorax, and methyl-CpG binding domain protein 1.The nuclear factor SPBP contains different functional domains and stimulates the activity of various transcriptional activatorsProtein interactions of the MLL PHD fingers modulate MLL target gene regulation in human cells.The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemiaLeukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expressionCBX8, a polycomb group protein, is essential for MLL-AF9-induced leukemogenesisOverexpression of the Notch target genes Hes in vivo induces lymphoid and myeloid alterationsA higher-order complex containing AF4 and ENL family proteins with P-TEFb facilitates oncogenic and physiologic MLL-dependent transcriptionAssociation of SET domain and myotubularin-related proteins modulates growth controlNew insight into the molecular mechanisms of MLL-associated leukemiaMLL-AFX requires the transcriptional effector domains of AFX to transform myeloid progenitors and transdominantly interfere with forkhead protein functionThe elongation domain of ELL is dispensable but its ELL-associated factor 1 interaction domain is essential for MLL-ELL-induced leukemogenesisMLL and CREB bind cooperatively to the nuclear coactivator CREB-binding proteinLeukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteinsHoxa9 and Meis1 are key targets for MLL-ENL-mediated cellular immortalizationRetrovirus-mediated gene transfer of MLL-ELL transforms primary myeloid progenitors and causes acute myeloid leukemias in miceMLL repression domain interacts with histone deacetylases, the polycomb group proteins HPC2 and BMI-1, and the corepressor C-terminal-binding proteinPotent inhibition of DOT1L as treatment of MLL-fusion leukemiaThe synovial sarcoma associated protein SYT interacts with the acute leukemia associated protein AF10The polycomb protein MPc3 interacts with AF9, an MLL fusion partner in t(9;11)(p22;q23) acute leukemiasThe ENL moiety of the childhood leukemia-associated MLL-ENL oncoprotein recruits human Polycomb 3Misguided transcriptional elongation causes mixed lineage leukemiaMouse Af9 is a controller of embryo patterning, like Mll, whose human homologue fuses with Af9 after chromosomal translocation in leukemiaStructure of AF3p21, a new member of mixed lineage leukemia (MLL) fusion partner proteins-implication for MLL-induced leukemogenesis.ENL, the MLL fusion partner in t(11;19), binds to the c-Abl interactor protein 1 (ABI1) that is fused to MLL in t(10;11)+.Disordered epigenetic regulation in MLL-related leukemia.MLL protects CpG clusters from methylation within the Hoxa9 gene, maintaining transcript expression.GPHN, a novel partner gene fused to MLL in a leukemia with t(11;14)(q23;q24).Intrinsic structural disorder confers cellular viability on oncogenic fusion proteinsSelective killing of mixed lineage leukemia cells by a potent small-molecule DOT1L inhibitor.Tumorigenesis in mice with a fusion of the leukaemia oncogene Mll and the bacterial lacZ gene.Mll fusions generated by Cre-loxP-mediated de novo translocations can induce lineage reassignment in tumorigenesisSelf-association mediated by the Ras association 1 domain of AF6 activates the oncogenic potential of MLL-AF6.MLL5, a homolog of Drosophila trithorax located within a segment of chromosome band 7q22 implicated in myeloid leukemia.A novel chromosomal inversion at 11q23 in infant acute myeloid leukemia fuses MLL to CALM, a gene that encodes a clathrin assembly protein.Developmentally induced Mll1 loss reveals defects in postnatal haematopoiesisValproic acid induces differentiation and transient tumor regression, but spares leukemia-initiating activity in mouse models of APL.MLL fusion partners AF4 and AF9 interact at subnuclear foci.The role of the MLL gene in infant leukemia.
P2860
Q22010909-65BA81EB-636C-494F-96D1-2344D49C8B6DQ22253233-74296E05-6F86-49AE-B10C-34CC3AD778F1Q24290281-D720D913-9C56-4BBB-8AFF-3E83E36C4A9DQ24291156-82E72F72-49F0-4B74-A00F-4DB81B81D718Q24291407-BD06AF9A-9BE1-4D3B-BAAA-D057EACA04D8Q24297027-A8A022DA-E2F5-4F38-81F5-E85922E5CAA3Q24297763-A06ECB56-7D25-42E8-89EC-BAF2E927CE12Q24298328-45B22A79-3EB4-4016-8345-F312EB61AED0Q24299122-5F54E0AD-B1FD-4FE3-8A94-091508A45EB4Q24323057-4659223A-284C-4F00-A70A-6AF18BDD2D4CQ24336625-C7494F59-014A-4D79-890C-927794C9B4FEQ24540167-FE17B767-18E8-4A6C-9FF8-EA43D0EA4052Q24550876-DAEAE160-CC8C-4B76-AF9E-E7F856F9F0DAQ24550988-82201928-A830-4564-8F25-398ADDBEA8E4Q24554418-F4A0341D-B651-48A5-97A5-8B59E06BA711Q24603527-4C1BE0C8-7017-4414-AC42-C989860F9A1AQ24647139-4BC54003-9DEE-4A36-A189-37FBD4BACF16Q24679773-84165D8B-F5EB-46A2-857D-8B32CC90747BQ27678800-4A8C29D3-6070-4EEF-9877-B7D188FB2119Q28203521-9AE3F4A3-30E8-45DA-BDA4-40068BD49AD5Q28204897-00BF7D96-7405-4525-990D-E3899EECDDB0Q28213852-E6C5E9A2-C3D9-4B02-9F17-4A50CA50FE87Q28471927-D4D9F7B6-64C9-43D8-A65C-11E22FFFAB1CQ28594037-0FAA1680-CB4F-42EC-8155-17AF917C7368Q30167808-776487B5-62C7-4968-BE5A-6526E6FEC7CBQ30175153-E29DC02E-82DB-48DD-8CF1-67DD2E5A9E5AQ30422159-37BB1EE1-71E3-4262-B87E-A42680C257EFQ30440771-93D14DC9-872D-45AC-8D3F-B709768008E8Q30727023-118AB650-3486-401E-B7D1-585590A9C5BAQ33514873-C5801404-932E-4F9C-A672-5708DE5A1B2CQ33716402-E2307F7E-205A-44E6-A958-5362CBA0FAC8Q33891954-315966C7-B9AF-4980-909B-CE30E5A24985Q33947080-046988BC-5E99-415D-BF39-3932FA18815CQ33997220-762B8109-B602-4D78-9B98-5BF53B8A575FQ34137337-99A50BA6-09A6-4C11-B258-C4EDF87D9C17Q34162245-14434F3A-1678-4257-9519-22CA44EA343EQ34195379-571941A7-997C-476A-B9DB-4B56F82CC151Q34254302-6D3D559C-56A3-4E2C-BFDB-30496666A0CAQ34275143-CDD38363-2357-47B5-98D3-9493986BECC8Q34287512-45445146-BF65-4D21-B903-4B4448D63166
P2860
The oncogenic capacity of HRX-ENL requires the transcriptional transactivation activity of ENL and the DNA binding motifs of HRX.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The oncogenic capacity of HRX- ...... the DNA binding motifs of HRX.
@ast
The oncogenic capacity of HRX- ...... the DNA binding motifs of HRX.
@en
type
label
The oncogenic capacity of HRX- ...... the DNA binding motifs of HRX.
@ast
The oncogenic capacity of HRX- ...... the DNA binding motifs of HRX.
@en
prefLabel
The oncogenic capacity of HRX- ...... the DNA binding motifs of HRX.
@ast
The oncogenic capacity of HRX- ...... the DNA binding motifs of HRX.
@en
P2093
P2860
P356
P1476
The oncogenic capacity of HRX- ...... the DNA binding motifs of HRX.
@en
P2093
P2860
P304
P356
10.1128/MCB.18.1.122
P407
P577
1998-01-01T00:00:00Z