Evidence map›Paper›PMID 33572777›Full record

ArticleInternational journal of molecular sciences2021

The Puzzling Problem of Cardiolipin Membrane-Cytochrome c Interactions: A Combined Infrared and Fluorescence Study.

Francesca Ripanti, Almerinda Di Venere, Mariangela Cestelli Guidi, Martina Romani, Alessandra Filabozzi, Marina Carbonaro, Maria Cristina Piro, Federica Sinibaldi, Alessandro Nucara, Giampiero Mei

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Structural dynamics and pH-regulated membrane binding of the TRAF2-NC trimer.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Article
  4. Composition of the CytochromeMolecules (Basel, Switzerland) · 2023
    Article
  5. Article
  6. 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

10 authors.

Francesca RipantiDepartment of Physics, Sapienza University of Rome, P.le A. Moro 5, 00185 Rome, Italy.
Almerinda Di VenereDepartment of Experimental Medicine, Tor Vergata University of Rome, Via Montpellier 1, 00133 Rome, Italy.
Mariangela Cestelli GuidiINFN-Laboratori Nazionali di Frascati, Via Enrico Fermi 40, 00044 Frascati, Italy.ORCID 0000-0002-6884-3915
Martina RomaniINFN-Laboratori Nazionali di Frascati, Via Enrico Fermi 40, 00044 Frascati, Italy.ORCID 0000-0003-4366-3405
Alessandra FilabozziDepartment of Physics, Tor Vergata University of Rome, Via della Ricerca Scientifica 1, 00133 Rome, Italy.
Marina CarbonaroCouncil for Agricultural Research and Economics (CREA), Research Centre for Food and Nutrition, Via Ardeatina 546, 00178 Rome, Italy.
Maria Cristina PiroDepartment of Experimental Medicine, Tor Vergata University of Rome, Via Montpellier 1, 00133 Rome, Italy.
Federica SinibaldiDepartment of Experimental Medicine, Tor Vergata University of Rome, Via Montpellier 1, 00133 Rome, Italy.
Alessandro NucaraDepartment of Physics, Sapienza University of Rome, P.le A. Moro 5, 00185 Rome, Italy.
Giampiero MeiDepartment of Experimental Medicine, Tor Vergata University of Rome, Via Montpellier 1, 00133 Rome, Italy.

Funding

Università degli Studi di Roma Tor Vergata E84I20000560005
6 · The paper itself

Abstract

The interaction of cytochrome c (cyt c) with natural and synthetic membranes is known to be a complex phenomenon, involving both protein and lipid conformational changes. In this paper, we combined infrared and fluorescence spectroscopy to study the structural transformation occurring to the lipid network of cardiolipin-containing large unilamellar vesicles (LUVs). The data, collected at increasing protein/lipid ratio, demonstrate the existence of a multi-phase process, which is characterized by: (i) the interaction of cyt c with the lipid polar heads; (ii) the lipid anchorage of the protein on the membrane surface; and (iii) a long-distance order/disorder transition of the cardiolipin acyl chains. Such effects have been quantitatively interpreted introducing specific order parameters and discussed in the frame of the models on cyt c activity reported in literature.

Indexed as

AnimalsCardiolipinsCell MembraneCytochromes cHorsesSpectrometry, FluorescenceSpectrophotometry, InfraredUnilamellar LiposomesCardiolipinsCytochromes cUnilamellar Liposomescardiolipincytochrome cmembrane disorderprotein-membrane binding

Identifiers

PMID33572777
PMCPMC7866282

What OpenQuestion holds

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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.