Evidence map›Paper›PMID 20858419›Full record

ArticleBiophysical journal2010

Cytochrome c-lipid interactions: new insights from resonance energy transfer.

Valeriya M Trusova, Galyna P Gorbenko, Julian G Molotkovsky, Paavo K J Kinnunen

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed, 35 citations in OpenAlex.

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  14. Cytochrome c causes pore formation in cardiolipin-containing membranes.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Versatility of non-native forms of human cytochrome c: pH and micellar concentration dependence.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013
    Article
  16. 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 3 institutions in 3 countries.

Valeriya M TrusovaDepartment of Biological and Medical Physics, VN Karazin Kharkov National University, Kharkov, Ukraine.
Galyna P Gorbenko
Julian G Molotkovsky
Paavo K J Kinnunen
Russian Academy of Sciences · RUUniversity of Helsinki · FIV. N. Karazin Kharkiv National University · UA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Resonance energy transfer (RET) from anthrylvinyl-labeled phosphatidylcholine (AV-PC) or cardiolipin (AV-CL) to cytochrome c (cyt c) heme moiety was employed to assess the molecular-level details of protein interactions with lipid bilayers composed of PC with 2.5 (CL2.5), 5 (CL5), 10 (CL10), or 20 (CL20) mol % CL under conditions of varying ionic strength and lipid/protein molar ratio. Monte Carlo analysis of multiple data sets revealed a subtle interplay between 1), exchange of the neutral and acidic lipid in the protein-lipid interaction zone; 2), CL transition into the extended conformation; and 3), formation of the hexagonal phase. The switch between these states was found to be controlled by CL content and salt concentration. At ionic strengths ≥ 40 mM, lipid bilayers with CL fraction not exceeding 5 mol % exhibited the tendency to transform from lamellar to hexagonal phase upon cyt c adsorption, whereas at higher contents of CL, transition into the extended conformation seems to become thermodynamically favorable. At lower ionic strengths, deviations from homogeneous lipid distributions were observed only for model membranes containing 2.5 mol % CL, suggesting the existence of a certain surface potential critical for assembly of lipid lateral domains in protein-lipid systems that may subsequently undergo morphological transformations depending on ambient conditions. These characteristics of cyt c-CL interaction are of great interest, not only from the viewpoint of regulating cyt c electron transfer and apoptotic propensities, but also to elucidate the general mechanisms by which membrane functional activities can be modulated by protein-lipid interactions.

Indexed as

Lipid MetabolismAnimalsCardiolipinsCattleCell MembraneCytochromes cFluorescence Resonance Energy TransferLipid BilayersLiposomesMonte Carlo MethodOsmolar ConcentrationPhosphatidylcholinesProtein BindingProtein Structure, TertiaryStatic ElectricityCardiolipinsCytochromes cLipid BilayersLiposomesPhosphatidylcholines

Identifiers

PMID20858419
PMCPMC2941011
OpenAlexW2112501934

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.