The DNA-bending protein HMG-1 enhances progesterone receptor binding to its target DNA sequences.
about
Isolation of cDNAs encoding novel transcription coactivators p52 and p75 reveals an alternate regulatory mechanism of transcriptional activationA tissue-specific coactivator of steroid receptors, identified in a functional genetic screenThe nuclear factor SPBP contains different functional domains and stimulates the activity of various transcriptional activatorsHMGB1 and HMGB2 cell-specifically down-regulate the p53- and p73-dependent sequence-specific transactivation from the human Bax gene promoterInteractions between p53, hMSH2-hMSH6 and HMG I(Y) on Holliday junctions and bulged basesA direct beta-catenin-independent interaction between androgen receptor and T cell factor 4High mobility group protein-1 (HMG-1) is a unique activator of p53Association of chromatin proteins high mobility group box (HMGB) 1 and HMGB2 with mitotic chromosomesHigh-mobility group chromatin proteins 1 and 2 functionally interact with steroid hormone receptors to enhance their DNA binding in vitro and transcriptional activity in mammalian cellsThe RAG1 homeodomain recruits HMG1 and HMG2 to facilitate recombination signal sequence binding and to enhance the intrinsic DNA-bending activity of RAG1-RAG2HMG1 interacts with HOX proteins and enhances their DNA binding and transcriptional activationHigh mobility group protein 2 functionally interacts with the POU domains of octamer transcription factorsFunctional roles of the transcription factor Oct-2A and the high mobility group protein I/Y in HLA-DRA gene expressionThe implication and potential applications of high-mobility group box 1 protein in breast cancerHigh mobility group protein 1: A collaborator in nucleosome dynamics and estrogen-responsive gene expressionInteraction with p53 enhances binding of cisplatin-modified DNA by high mobility group 1 proteinHMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequencesHigh mobility group box 1 protein interacts with multiple Toll-like receptorsIdentification of a novel transcription factor, ELYS, expressed predominantly in mouse foetal haematopoietic tissuesHMG1 protein stimulates DNA end joining by promoting association of DNA molecules via their endsHigh mobility group B1 protein interacts with its receptor RAGE in tumor cells but not in normal tissuesRoles of adeno-associated virus Rep protein and human chromosome 19 in site-specific recombinationHMGA1 is a novel downstream nuclear target of the insulin receptor signaling pathwayCharacterization and potential function of a novel testis-specific nucleoporin BS-63.Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins.Role of histone H1 as an architectural determinant of chromatin structure and as a specific repressor of transcription on Xenopus oocyte 5S rRNA genesHigh mobility group chromosomal protein 1 binds to the adeno-associated virus replication protein (Rep) and promotes Rep-mediated site-specific cleavage of DNA, ATPase activity and transcriptional repression.SRY interacts with and negatively regulates androgen receptor transcriptional activity.Multiple layers of cooperativity regulate enhanceosome-responsive RNA polymerase II transcription complex assembly.Control of progesterone receptor transcriptional synergy by SUMOylation and deSUMOylation.Estrogen receptor interaction with estrogen response elementsHMGB1 in health and disease.Functional interactions between a phage histone-like protein and a transcriptional factor in regulation of phi29 early-late transcriptional switch.Interactions between an HMG-1 protein and members of the Rel family.Steroid hormones induce HMG1 overexpression and sensitize breast cancer cells to cisplatin and carboplatin.Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function.11q23 translocations split the "AT-hook" cruciform DNA-binding region and the transcriptional repression domain from the activation domain of the mixed-lineage leukemia (MLL) gene.Down-regulation of HMGB1 expression by shRNA constructs inhibits the bioactivity of urothelial carcinoma cell lines via the NF-κB pathwayHigh mobility group 1 protein is not stably associated with the chromosomes of somatic cells.Nucleosome dynamics: HMGB1 relaxes canonical nucleosome structure to facilitate estrogen receptor binding.
P2860
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P2860
The DNA-bending protein HMG-1 enhances progesterone receptor binding to its target DNA sequences.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
The DNA-bending protein HMG-1 ...... g to its target DNA sequences.
@ast
The DNA-bending protein HMG-1 ...... g to its target DNA sequences.
@en
type
label
The DNA-bending protein HMG-1 ...... g to its target DNA sequences.
@ast
The DNA-bending protein HMG-1 ...... g to its target DNA sequences.
@en
prefLabel
The DNA-bending protein HMG-1 ...... g to its target DNA sequences.
@ast
The DNA-bending protein HMG-1 ...... g to its target DNA sequences.
@en
P2093
P2860
P356
P1476
The DNA-bending protein HMG-1 ...... g to its target DNA sequences.
@en
P2093
D E Pettijohn
D P Edwards
J P Wagner
P Prendergast
P2860
P304
P356
10.1128/MCB.14.5.3376
P407
P577
1994-05-01T00:00:00Z