Evidence map›Paper›PMID 19670908›Full record

ArticleBiochemistry2009

Mapping the interaction of pro-apoptotic tBID with pro-survival BCL-XL.

Yong Yao, Andrey A Bobkov, Leigh A Plesniak, Francesca M Marassi

Abstract readComparative Study
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Review
  3. Apoptotic mitochondrial poration by a growing list of pore-forming BCL-2 family proteins.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Conformation of BCL-XL upon Membrane Integration.Journal of molecular biology · 2015
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Apoptotic regulation by MCL-1 through heterodimerization.The Journal of biological chemistry · 2010
    Article
  17. Intrinsically disordered proteins in bcl-2 regulated apoptosis.International journal of molecular sciences · 2010
    Review
  18. BAX and BAK caught in the act.Molecular cell · 2009
    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

4 authors at 2 institutions in 1 country.

Yong YaoBurnham Institute for Medical Research, 10901 North Torrey Pines Road, La Jolla, California 92037, USA.
Andrey A Bobkov
Leigh A Plesniak
Francesca M Marassi
Sanford Burnham Prebys Medical Discovery Institute · USUniversity of San Diego · US

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI Michael Jackson · 1985 to 2026
$107.2M
Structures of membrane-bound Bcl-2 apoptotic proteinsR01GM065374 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MARASSI, FRANCESCA M · 2005 to 2009
$1.3M
Bim structure and apoptosisR21AI063563 · NIAID · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MARASSI, FRANCESCA M · 2005 to 2006
$507k
Hunter-Killer Peptides &Their Membrane InteractionsR15GM068431 · NIGMS · UNIVERSITY OF SAN DIEGO · PI PLESNIAK, LEIGH A · 2003 to 2007
$311k
NCI NIH HHS CA030199NCI NIH HHS P30 CA030199NIAID NIH HHS R21 AI063563NIGMS NIH HHS R01 GM065374NIGMS NIH HHS R15 GM068431
6 · The paper itself

Abstract

The BH3-only BCL-2 family protein BID is activated by caspase-8 cleavage upon engagement of cell surface death receptors. The resulting 15 kDa C-terminal fragment, tBID, translocates to mitochondria, triggering the release of cytotoxic molecules and cell death. The pro-apoptotic activity of tBID is regulated by its interactions with pro-survival BCL-XL and pro-death BAX, both in the cytosol and at the mitochondrial membrane. In this study, we characterize the molecular interactions between full-length tBID and BCL-XL using NMR spectroscopy and isothermal titration calorimetry (ITC). In aqueous solution, tBID adopts an alpha-helical but dynamically disordered conformation; however, the three-dimensional conformation is stabilized when tBID engages its BH3 domain in the BH3-binding hydrophobic groove of BCL-XL to form a stable heterodimeric complex. Characterization of the binding thermodynamics by ITC reveals that the interaction between tBID and BCL-XL is driven by enthalpy but disfavored by the entropy associated with the conformational order induced in tBID upon binding BCL-XL.

Indexed as

EntropyAmino Acid SequenceApoptosis Regulatory Proteinsbcl-X ProteinBH3 Interacting Domain Death Agonist ProteinCell SurvivalDimerizationHumansMolecular Sequence DataProtein BindingApoptosis Regulatory ProteinsBCL2L1 protein, humanbcl-X ProteinBH3 Interacting Domain Death Agonist ProteinBID protein, human

Identifiers

PMID19670908
PMCPMC2762941
OpenAlexW2049826293

What OpenQuestion holds

Textmetadata
LicenceTDM
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.