Evidence map›Paper›PMID 27151821›Full record

ArticleScientific reports2016

Crystal structure of TRAF1 TRAF domain and its implications in the TRAF1-mediated intracellular signaling pathway.

Chang Min Kim, Jae Young Choi, Eijaz Ahmed Bhat, Jae-Hee Jeong, Young-Jin Son, Sunghwan Kim, Hyun Ho Park

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 20% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Salmonella YqiC exerts its function through an oligomeric state.Protein science : a publication of the Protein Society · 2023
    Article
  8. Article
  9. Expansion of the mutation spectrum and phenotype ofFrontiers in molecular neuroscience · 2022
    Article
  10. Article
  11. Mechanistic dissection of spatial organization in NF-κB signaling pathways by hybrid simulations.Integrative biology : quantitative biosciences from nano to macro · 2021
    Article
  12. Review
  13. Saudi journal of biological sciences · 2021
    Article
  14. Article
  15. Comparison of Target Recognition by TRAF1 and TRAF2.International journal of molecular sciences · 2020
    Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review
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

7 authors at 3 institutions in 1 country.

Chang Min KimDepartment of Biochemistry, Yeungnam University, Gyeongsan, 712-749, South Korea.
Jae Young ChoiDepartment of Biochemistry, Yeungnam University, Gyeongsan, 712-749, South Korea.
Eijaz Ahmed BhatDepartment of Biochemistry, Yeungnam University, Gyeongsan, 712-749, South Korea.
Jae-Hee JeongPohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, 790-784, South Korea.
Young-Jin SonNew Drug Development Center, Daegu-Gyungpook Medical Innovation Foundation, Daegu, 701-310, South Korea.
Sunghwan KimNew Drug Development Center, Daegu-Gyungpook Medical Innovation Foundation, Daegu, 701-310, South Korea.
Hyun Ho ParkDepartment of Biochemistry, Yeungnam University, Gyeongsan, 712-749, South Korea.
Yeungnam University · KRDaegu-Gyeongbuk Medical Innovation Foundation · KRPohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TNF-receptor associated factor (TRAF) proteins are key adaptor molecules containing E3 ubiquitin ligase activity that play a critical role in immune cell signaling. TRAF1 is a unique family of TRAF lacking the N-terminal RING finger domain. TRAF1 is an important scaffold protein that participates in TNFR2 signaling in T cells as a negative or positive regulator via direct interaction with TRAF2, which has recently been identified as a pro-apoptotic regulator in neuronal cell death. Here, we report the first crystal structure of the TRAF1 TRAF domain containing both the TRAF-N coiled-coil domain and the TRAF-C domain. Our structure reveals both similarities and differences with other TRAF family members, which may be functionally relevant to TRAFs. We also found that the TRAF-N coiled-coil domain of TRAF1 is critical for the trimer formation and stability of the protein. Finally, we found that conserved surface residues on the TRAF1 TRAF domain that might be binding hot spots that are critical for interaction with signaling molecules.

Indexed as

Signal TransductionCrystallography, X-RayEnterovirusModels, MolecularProtein BindingProtein ConformationProtein DomainsProtein MultimerizationProtein StabilityTNF Receptor-Associated Factor 1Viral StructuresTNF Receptor-Associated Factor 1

Identifiers

PMID27151821
PMCPMC4858697
OpenAlexW2346998345

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.