Evidence map›Paper›PMID 21639858›Full record

ArticleThe Biochemical journal2011

Structural changes in the BH3 domain of SOUL protein upon interaction with the anti-apoptotic protein Bcl-xL.

Emmanuele Ambrosi, Stefano Capaldi, Michele Bovi, Gianmaria Saccomani, Massimiliano Perduca, Hugo L Monaco

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. The Structural Biology of Bcl-xInternational journal of molecular sciences · 2019
    Review
  4. Thermodynamic Characterization of the CaInternational journal of molecular sciences · 2018
    Article
  5. Article
  6. Article
  7. Transglutaminase 2 Inhibitor KCC009 Induces p53-Independent Radiosensitization in Lung Adenocarcinoma Cells.Medical science monitor : international medical journal of experimental and clinical research · 2016
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

6 authors at 1 institution in 1 country.

Emmanuele AmbrosiBiocrystallography Laboratory, Department of Biotechnology, University of Verona, Italy.
Stefano Capaldi
Michele Bovi
Gianmaria Saccomani
Massimiliano Perduca
Hugo L Monaco
University of Verona · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SOUL protein is known to induce apoptosis by provoking the mitochondrial permeability transition, and a sequence homologous with the BH3 (Bcl-2 homology 3) domains has recently been identified in the protein, thus making it a potential new member of the BH3-only protein family. In the present study, we provide NMR, SPR (surface plasmon resonance) and crystallographic evidence that a peptide spanning residues 147-172 in SOUL interacts with the anti-apoptotic protein Bcl-xL. We have crystallized SOUL alone and the complex of its BH3 domain peptide with Bcl-xL, and solved their three-dimensional structures. The SOUL monomer is a single domain organized as a distorted β-barrel with eight anti-parallel strands and two α-helices. The BH3 domain extends across 15 residues at the end of the second helix and eight amino acids in the chain following it. There are important structural differences in the BH3 domain in the intact SOUL molecule and the same sequence bound to Bcl-xL.

Indexed as

ApoptosisAmino Acid Sequencebcl-X ProteinCrystallography, X-RayHeme-Binding ProteinsHemeproteinsHeminHumansModels, MolecularMolecular Sequence DataPeptidesPregnancy ProteinsProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryStructure-Activity Relationshipbcl-X ProteinHEBP2 protein, humanHeme-Binding ProteinsHemeproteinsHeminPeptidesPregnancy Proteins

Identifiers

PMID21639858
PMCPMC3174058
OpenAlexW2153472874

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.