Evidence map›Paper›PMID 21504165›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2011

Single vesicle observations of the cardiolipin-cytochrome C interaction: induction of membrane morphology changes.

Paul A Beales, Chris L Bergstrom, Nienke Geerts, John T Groves, T Kyle Vanderlick

Open access · greenAbstract read
In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Composition of the CytochromeMolecules (Basel, Switzerland) · 2023
    Article
  7. Review
  8. Amphiphilic Aminoglycosides as Medicinal Agents.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Barcoding Biological Reactions with DNA-Functionalized Vesicles.Angewandte Chemie (International ed. in English) · 2019
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

5 authors at 2 institutions in 1 country.

Paul A BealesDepartment of Chemical and Environmental Engineering, Yale University, New Haven, Connecticut 06511, United States.
Chris L Bergstrom
Nienke Geerts
John T Groves
T Kyle Vanderlick
Yale University · USPrinceton University · US

Funding

Molecular Probes of the Mechanisms of Cytocrhome P450R37GM036298 · NIGMS · PRINCETON UNIVERSITY · PI GROVES, JOHN TAYLOR · 2007 to 2016
$3.7M
NIGMS NIH HHS 2R37 GM036298NIGMS NIH HHS R37 GM036298
6 · The paper itself

Abstract

We present a novel platform for investigating the composition-specific interactions of proteins (or other biologically relevant molecules) with model membranes composed of compositionally distinct domains. We focus on the interaction between a mitochondrial-specific lipid, cardiolipin (CL), and a peripheral membrane protein, cytochrome c (cyt c). We engineer vesicles with compositions such that they phase separate into coexisting liquid phases and the lipid of interest, CL, preferentially localizes into one of the domains (the liquid disordered (L(d)) phase). The presence of CL-rich and CL-depleted domains within the same vesicle provides a built-in control experiment to simultaneously observe the behavior of two membrane compositions under identical conditions. We find that cyt c binds strongly to CL-rich domains and observe fascinating morphological transitions within these regions of membrane. CL-rich domains start to form small buds and eventually fold up into a collapsed state. We also observe that cyt c can induce a strong attraction between the CL-rich domains of adjacent vesicles as demonstrated by the development of large osculating regions between these domains. Qualitatively similar behavior is observed when other polycationic proteins or polymers of a similar size and net charge are used instead of cyt c. We argue that these striking phenomena can be simply understood by consideration of colloidal forces between the protein and the membrane. We discuss the possible biological implications of our observations in relation to the structure and function of mitochondria.

Indexed as

AnimalsCardiolipinsCattleCell MembraneCytochromes cMicroscopy, ConfocalMitochondrial MembranesProtein BindingSaccharomyces cerevisiaeUnilamellar LiposomesCardiolipinsCytochromes cUnilamellar Liposomes

Identifiers

PMID21504165
PMCPMC3103708
OpenAlexW2044848883

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.