ArticleMolecular and cellular biology1998
Intramolecular regulation of MyoD activation domain conformation and function.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed.
- MYOD represses gene expression from non-E-box motifs.Genes & development · 2025Article
- E-box independent chromatin recruitment turns MYOD into a transcriptional repressor.bioRxiv : the preprint server for biology · 2024Article
- Integrated requirement of non-specific and sequence-specific DNA binding in Myc-driven transcription.The EMBO journal · 2021Article
- Combination of cell signaling molecules can facilitate MYOD1-mediated myogenic transdifferentiation of pig fibroblasts.Journal of animal science and biotechnology · 2021Article
- Pax7-FKHR transcriptional activity is enhanced by transcriptionally repressed MyoD.Journal of cellular biochemistry · 2011Article
- Structure and functions of powerful transactivators: VP16, MyoD and FoxA.The International journal of developmental biology · 2010Review
- Target identification using drug affinity responsive target stability (DARTS).Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Specificity of Atonal and Scute bHLH factors: analysis of cognate E box binding sites and the influence of Senseless.Genes to cells : devoted to molecular & cellular mechanisms · 2008Article
- Determinants of myogenic specificity within MyoD are required for noncanonical E box binding.Molecular and cellular biology · 2007Article
- MyoD uses overlapping but distinct elements to bind E-box and tetraplex structures of regulatory sequences of muscle-specific genes.Nucleic acids research · 2007Article
- Proteasome-mediated degradation of the coactivator p300 impairs cardiac transcription.Molecular and cellular biology · 2000Article
- Establishment of distinct MyoD, E2A, and twist DNA binding specificities by different basic region-DNA conformations.Molecular and cellular biology · 2000Article
- Reprogramming cells with synthetic proteins.Asian journal of andrologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The MyoD family of basic helix-loop-helix (bHLH) proteins is required for myogenic determination and differentiation. The basic region carries the myogenic code and DNA binding specificity, while the N terminus contains a potent transcriptional activation domain. Myogenic activation is abolished when the basic region, bound to a myogenic E box, carries a mutation of Ala-114. It has been proposed that DNA binding of the MyoD basic region leads to recruitment of a recognition factor that unmasks the activation domain. Here we demonstrate that an A114N mutant exhibits an altered conformation in the basic region and that this local conformational difference can lead to a more global change affecting the conformation of the activation domain. This suggests that the deleterious effects of this class of mutations may result directly from defective conformation. Thus, the activation domain is unmasked only upon DNA binding by the correct basic region. Such a coupled conformational relationship may have evolved to restrict myogenic specificity to a small number of bHLH proteins among many with diverse functions yet with DNA binding specificities known to be similar.
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.