ArticleCell reports2016
Structural Basis for the Activation of IKK1/α.
Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 64 citations in OpenAlex.
- Epithelial TRIM27 Inhibits Intestinal Inflammation in Ulcerative Colitis by the USP7/TRIM27-IKK Double Negative-Feedback.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- NF-κB signaling pathway mediates the anti-tumor effect of Ginsenoside Rg1 in glioblastoma.Biochemistry and biophysics reports · 2026Article
- An HHEX/IKKα positive feedback loop promotes intestinal inflammation.The Journal of clinical investigation · 2026Article
- The roles of IKKα in normal physiology and cancer.Cell communication and signaling : CCS · 2026Review
- Regulatory mechanisms of deer antler extracellular vesicles in multilevel tissue repair: a state-of-the-art review.Frontiers in pharmacology · 2026Review
- Comparative analysis of curcuminoid content, antioxidant capacity, and target-specific molecular docking of turmeric extracts sourced from Thailand.Food chemistry. Molecular sciences · 2025Article
- Double trouble: cytosolic and nuclear IKKα in cancer.Open biology · 2025Review
- Article
- Advances in the structures, mechanisms and targeting of molecular chaperones.Signal transduction and targeted therapy · 2025Review
- Mutations disrupting the kinase domain of IKKα lead to immunodeficiency and immune dysregulation in humans.The Journal of experimental medicine · 2025Article
- Clinical observations and mechanistic insights of traditional Chinese medicine in the management of diabetic retinopathy.Pharmaceutical biology · 2024Review
- Defective kinase activity of IKKα leads to combined immunodeficiency and disruption of immune tolerance in humans.Nature communications · 2024Article
- HDX-MS Analysis of Catalytic Activation of IKK2 in the IκB Kinase Complex.Biochemistry · 2024Article
- Molecular mechanism of IKK catalytic dimer docking to NF-κB substrates.Nature communications · 2024Article
- Design and Synthesis of Novel Aminoindazole-pyrrolo[2,3-Molecules (Basel, Switzerland) · 2024Article
- Cimicifugoside H-2 as an Inhibitor of IKK1/Alpha: A Molecular Docking and Dynamic Simulation Study.Biomolecules · 2024Article
- NFκB signalling in colorectal cancer: Examining the central dogma of IKKα and IKKβ signalling.Heliyon · 2024Review
- The host antiviral protein SAMHD1 suppresses NF-κB activation by interacting with the IKK complex during inflammatory responses and viral infection.The Journal of biological chemistry · 2023Article
- Article
- Novel biochemical, structural, and systems insights into inflammatory signaling revealed by contextual interaction proteomics.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Distinct signaling pathways activate the NF-κB family of transcription factors. The canonical NF-κB-signaling pathway is mediated by IκB kinase 2/β (IKK2/β), while the non-canonical pathway depends on IKK1/α. The structural and biochemical bases for distinct signaling by these otherwise highly similar IKKs are unclear. We report single-particle cryoelectron microscopy (cryo-EM) and X-ray crystal structures of human IKK1 in dimeric (∼150 kDa) and hexameric (∼450 kDa) forms. The hexamer, which is the representative form in the crystal but comprises only ∼2% of the particles in solution by cryo-EM, is a trimer of IKK1 dimers. While IKK1 hexamers are not detectable in cells, the surface that supports hexamer formation is critical for IKK1-dependent cellular processing of p100 to p52, the hallmark of non-canonical NF-κB signaling. Comparison of this surface to that in IKK2 indicates significant divergence, and it suggests a fundamental role for this surface in signaling by these kinases through distinct pathways.
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.