Evidence map›Paper›PMID 26457518›Full record

ArticleActa crystallographica. Section F, Structural biology communications2015

The structure of the death receptor 4-TNF-related apoptosis-inducing ligand (DR4-TRAIL) complex.

Vidhyashankar Ramamurthy, Aaron P Yamniuk, Eric J Lawrence, Wei Yong, Lumelle A Schneeweis, Lin Cheng, Melissa Murdock, Martin J Corbett, Michael L Doyle, Steven Sheriff

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

21 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Trial
  3. Article
  4. Article
  5. Article
  6. Article
  7. Observational
  8. Article
  9. Article
  10. TRAIL-Sensitizing Effects of Flavonoids in Cancer.International journal of molecular sciences · 2023
    Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. RIP-1/c-FLIPL Induce Hepatic Cancer Cell Apoptosis Through Regulating Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand (TRAIL).Medical science monitor : international medical journal of experimental and clinical research · 2017
    Article
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

10 authors.

Vidhyashankar RamamurthyMolecular Structure and Design, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
Aaron P YamniukProtein Science, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
Eric J LawrenceProtein Science, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
Wei YongMolecular Structure and Design, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
Lumelle A SchneeweisProtein Science, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
Lin ChengProtein Science, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
Melissa MurdockProtein Science, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
Martin J CorbettProtein Science, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
Michael L DoyleProtein Science, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.
Steven SheriffMolecular Structure and Design, Bristol-Myers Squibb R&D, PO Box 4000, Princeton, NJ 08543-4000, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structure of death receptor 4 (DR4) in complex with TNF-related apoptosis-inducing ligand (TRAIL) has been determined at 3 Å resolution and compared with those of previously determined DR5-TRAIL complexes. Consistent with the high sequence similarity between DR4 and DR5, the overall arrangement of the DR4-TRAIL complex does not differ substantially from that of the DR5-TRAIL complex. However, subtle differences are apparent. In addition, solution interaction studies were carried out that show differences in the thermodynamics of binding DR4 or DR5 with TRAIL.

Indexed as

Amino Acid SequenceCalorimetryCrystallizationCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataProtein BindingReceptors, TNF-Related Apoptosis-Inducing LigandThermodynamicsTNF-Related Apoptosis-Inducing LigandReceptors, TNF-Related Apoptosis-Inducing LigandTNF-Related Apoptosis-Inducing LigandTNFRSF10A protein, humanTNFSF10 protein, humandeath receptor 4death receptor 5TNF-related apoptosis-inducing ligand

Identifiers

PMID26457518
PMCPMC4601591

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.