ArticleProceedings of the National Academy of Sciences of the United States of America1993
Identification of a domain required for oncogenic activity and transcriptional suppression by v-erbA and thyroid-hormone receptor alpha.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 54 citations in OpenAlex.
- Epithelial retinoic acid receptor β regulates serum amyloid A expression and vitamin A-dependent intestinal immunity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Controlling gene networks and cell fate with precision-targeted DNA-binding proteins and small-molecule-based genome readers.The Biochemical journal · 2014Review
- Association of v-ErbA with Smad4 disrupts TGF-beta signaling.Molecular biology of the cell · 2009Article
- Functional evidence for retinoid X receptor (RXR) as a nonsilent partner in the thyroid hormone receptor/RXR heterodimer.Molecular and cellular biology · 2002Article
- Transcriptional regulation in acute promyelocytic leukemia.Oncogene · 2001Review
- Review
- In vivo transcription factor recruitment during thyroid hormone receptor-mediated activation.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Alien, a highly conserved protein with characteristics of a corepressor for members of the nuclear hormone receptor superfamily.Molecular and cellular biology · 1999Article
- Unique forms of human and mouse nuclear receptor corepressor SMRT.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Leukemic transformation by the v-ErbA oncoprotein entails constitutive binding to and repression of an erythroid enhancer in vivo.The EMBO journal · 1998Article
- A role for helix 3 of the TRbeta ligand-binding domain in coactivator recruitment identified by characterization of a third cluster of mutations in resistance to thyroid hormone.The EMBO journal · 1998Article
- The thyroid hormone receptor functions as a ligand-operated developmental switch between proliferation and differentiation of erythroid progenitors.The EMBO journal · 1998Article
- Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: hormone-regulated chromatin disruption is not sufficient for transcriptional activation.The EMBO journal · 1997Article
- Nuclear receptor corepressors activate rather than suppress basal transcription of genes that are negatively regulated by thyroid hormone.Molecular and cellular biology · 1997Article
- Direct modulation of simian virus 40 late gene expression by thyroid hormone and its receptor.Journal of virology · 1997Article
- SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimers.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Specific mutations in the ligand binding domain selectively abolish the silencing function of human thyroid hormone receptor beta.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Genetic dissection of thyroid hormone receptor beta: identification of mutations that separate hormone binding and transcriptional activation.Molecular and cellular biology · 1995Article
- Two silencing sub-domains of v-erbA synergize with each other, but not with RXR.Nucleic acids research · 1994Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
v-erbA, a mutated version of the chicken thyroid hormone (TH) receptor type alpha, can inhibit hormonal induction of target genes. In addition, v-erbA acts as a constitutive repressor of the basal promoter activity. In vivo, v-erbA can arrest the differentiation of erythroid precursor cells and suppresses transcription of erythrocyte-specific genes. We show that the v-erbA protein of the transformation-defective avian erythroblastosis virus mutant (AEVtd359) fails to suppress basal transcription level and exhibits impaired ability in antagonizing the TH and retinoic acid response. The inactivating mutation is a 1-nt change leading to a Pro-->Arg replacement in the "hinge region" of v-erbA protein. Introducing this mutation in the context of TH receptor alpha selectively inactivates the suppressor function, while hormone-binding and transcriptional-activation properties are unaffected. These data suggest that trans-repression rather than a dominant negative block of TH-receptor or retinoic acid-receptor activation may represent the primary molecular property underlying erbA oncogenesis.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.