Evidence map›Paper›PMID 22190488›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Conformational properties of cardiolipin-bound cytochrome c.

Jonas Hanske, Jason R Toffey, Anna M Morenz, Amber J Bonilla, Katherine H Schiavoni, Ekaterina V Pletneva

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

86 citing papers in PubMed, 199 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Cardiolipin Membranes Promote CytochromeMolecules (Basel, Switzerland) · 2024
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Alkaline State of the Domain-Swapped Dimer of Human CytochromeJournal of the American Chemical Society · 2022
    Article
  19. De novo sequencing and construction of a unique antibody for the recognition of alternative conformations of cytochromeProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Article

26 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

6 authors at 1 institution in 1 country.

Jonas HanskeDepartment of Chemistry, Dartmouth College, Hanover, NH 03755, USA.
Jason R Toffey
Anna M Morenz
Amber J Bonilla
Katherine H Schiavoni
Ekaterina V Pletneva
Dartmouth College · US

Funding

Conformational Properties of Cytochromes in DiseaseR01GM098502 · NIGMS · DARTMOUTH COLLEGE · PI PLETNEVA, EKATERINA · 2011 to 2023
$2.9M
NIGMS NIH HHS GM098502NIGMS NIH HHS R01 GM098502
6 · The paper itself

Abstract

Interactions of cytochrome c (cyt c) with cardiolipin (CL) are important for both electron transfer and apoptotic functions of this protein. A sluggish peroxidase in its native state, when bound to CL, cyt c catalyzes CL peroxidation, which contributes to the protein apoptotic release. The heterogeneous CL-bound cyt c ensemble is difficult to characterize with traditional structural methods and ensemble-averaged probes. We have employed time-resolved FRET measurements to evaluate structural properties of the CL-bound protein in four dansyl (Dns)-labeled variants of horse heart cyt c. The Dns decay curves and extracted Dns-to-heme distance distributions P(r) reveal a conformational diversity of the CL-bound cyt c ensemble with distinct populations of the polypeptide structures that vary in their degree of protein unfolding. A fraction of the ensemble is substantially unfolded, with Dns-to-heme distances resembling those in the guanidine hydrochloride-denatured state. These largely open cyt c structures likely dominate the peroxidase activity of the CL-bound cyt c ensemble. Site variations in P(r) distributions uncover structural features of the CL-bound cyt c, rationalize previous findings, and implicate the prime role of electrostatic interactions, particularly with the protein C terminus, in the CL-induced unfolding.

Indexed as

AnimalsCardiolipinsCytochromes cFluorescence PolarizationFluorescence Resonance Energy TransferHorsesModels, MolecularMutant ProteinsOsmolar ConcentrationProtein BindingProtein ConformationCardiolipinsCytochromes cMutant Proteins

Identifiers

PMID22190488
PMCPMC3252944
OpenAlexW2002621746

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.