Evidence map›Paper›PMID 24375677›Full record

ReviewEMBO reports2014

The IκB kinase complex in NF-κB regulation and beyond.

Michael Hinz, Claus Scheidereit

Open access · greenAbstract readReview
In one paragraph

Review in EMBO reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 324 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
324citing papers in PubMed, 1 pooled it
10.8field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

324 citing papers in PubMed, 1 synthesis or guideline pooled it, 544 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Aging and cancer: current understandings and future perspectives.Signal transduction and targeted therapy · 2026
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The roles of IKKα in normal physiology and cancer.Cell communication and signaling : CCS · 2026
    Review
  16. Biology · 2026
    Article
  17. Review
  18. Article
  19. Article
  20. Article

264 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Michael HinzMax Delbrück Center for Molecular Medicine, Berlin, Germany.
Claus Scheidereit
Max Delbrück Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The IκB kinase (IKK) complex is the signal integration hub for NF-κB activation. Composed of two serine-threonine kinases (IKKα and IKKβ) and the regulatory subunit NEMO (also known as IKKγ), the IKK complex integrates signals from all NF-κB activating stimuli to catalyze the phosphorylation of various IκB and NF-κB proteins, as well as of other substrates. Since the discovery of the IKK complex components about 15 years ago, tremendous progress has been made in the understanding of the IKK architecture and its integration into signaling networks. In addition to the control of NF-κB, IKK subunits mediate the crosstalk with other pathways, thereby extending the complexity of their biological function. This review summarizes recent advances in IKK biology and focuses on emerging aspects of IKK structure, regulation and function.

Indexed as

UbiquitinationAnimalsFeedback, PhysiologicalHumansI-kappa B KinaseNF-kappa BPhosphorylationProtein Interaction MapsProtein MultimerizationSignal TransductionUbiquitinI-kappa B KinaseNF-kappa BUbiquitin

Identifiers

PMID24375677
PMCPMC4303448
OpenAlexW2075962202

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.