ReviewNucleic acids research2014
Molecular recognition by the KIX domain and its role in gene regulation.
Review in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 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
59 citing papers in PubMed, 110 citations in OpenAlex.
- Targeting a Leukemia-Relevant Protein-Protein Interface: N-Aryl Anthranilic Acids as Disruptors of the c-Myb-CBP/p300 KIX Interaction.Chemical biology & drug design · 2026Article
- De Novo Design of Multivalent α/β-Peptides Mimicking Transcription Factors Targeting the CBP KIX Domain.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Article
- Fluorine-Thiol Displacement Stapling on the Disordered αSynlett : accounts and rapid communications in synthetic organic chemistry · 2025Article
- Collaboration between DELLA proteins and the Mediator subunit MED15 to regulate transcription in plants.Journal of experimental botany · 2025Article
- Article
- High-throughput affinity measurements of direct interactions between activation domains and co-activators.bioRxiv : the preprint server for biology · 2024Article
- DELLA proteins recruit the Mediator complex subunit MED15 to coactivate transcription in land plants.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Inhibition of CREB Binding and Function with a Dual-Targeting Ligand.Biochemistry · 2024Article
- Garcinolic Acid Distinguishes Between GACKIX Domains and Modulates Interaction Networks.Chembiochem : a European journal of chemical biology · 2023Article
- Genome-wide analysis of KIX gene family for organ size regulation in soybean (Frontiers in plant science · 2023Article
- CBP-HSF2 structural and functional interplay in Rubinstein-Taybi neurodevelopmental disorder.Nature communications · 2022Article
- Article
- Allostery in the dynamic coactivator domain KIX occurs through minor conformational micro-states.PLoS computational biology · 2022Article
- Cryo-EM, Protein Engineering, and Simulation Enable the Development of Peptide Therapeutics against Acute Myeloid Leukemia.ACS central science · 2022Article
- Peptide Tethering: Pocket-Directed Fragment Screening for Peptidomimetic Inhibitor Discovery.Journal of the American Chemical Society · 2022Article
- SlKIX8 and SlKIX9 are negative regulators of leaf and fruit growth in tomato.Plant physiology · 2022Article
- The auto-inhibition mechanism of transcription factor Ets-1 induced by phosphorylation on the intrinsically disordered region.Computational and structural biotechnology journal · 2022Article
- Emerging Role of CREB in Epithelial to Mesenchymal Plasticity of Pancreatic Cancer.Frontiers in oncology · 2022Review
- A Dual-Site Inhibitor of CBP/p300 KIX is a Selective and Effective Modulator of Myb.Journal of the American Chemical Society · 2021Article
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 at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The kinase-inducible domain interacting (KIX) domain is a highly conserved independently folding three-helix bundle that serves as a docking site for transcription factors, whereupon promoter activation and target specificity are achieved during gene regulation. This docking event is a harbinger of an intricate multi-protein assembly at the transcriptional apparatus and is regulated in a highly precise manner in view of the critical role it plays in multiple cellular processes. KIX domains have been characterized in transcriptional coactivators such as p300/CREB-binding protein and mediator of RNA polymerase II transcription subunit 15, and even recQ protein-like 5 helicases in various organisms. Their targets are often intrinsically disordered regions within the transactivation domains of transcription factors that attain stable secondary structure only upon complexation with KIX. In this article, we review the KIX domain in terms of its sequence and structure and present the various implications of its ability to act as a transcriptional switch, the mechanistic basis of molecular recognition by KIX, its binding specificity, target promiscuity, combinatorial potential and unique mode of regulation via allostery. We also discuss the possible roles of KIX domains in plants and hope that this review will accelerate scientific interest in KIX and pave the way for novel avenues of research on this critical domain.
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.