Cited by 74Protein Structure and DynamicsLipid Membrane Structure and BehaviorCell death mechanisms and regulation

Structural transformations of cytochrome c upon interaction with cardiolipin

Open access
Muenzner, Julia, Pletneva, Ekaterina V.·2014·Chemistry and Physics of Lipids

Abstract

Interactions of cytochrome c (cyt c) with cardiolipin (CL) play a critical role in early stages of apoptosis. Upon binding to CL, cyt c undergoes changes in secondary and tertiary structure that lead to a dramatic increase in its peroxidase activity. Insertion of the protein into membranes, insertion of CL acyl chains into the protein interior, and extensive unfolding of cyt c after adsorption to the membrane have been proposed as possible modes for interaction of cyt c with CL. Dissociation of Met80 is accompanied by opening of the heme crevice and binding of another heme ligand. Fluorescence studies have revealed conformational heterogeneity of the lipid-bound protein ensemble with distinct polypeptide conformations that vary in the degree of protein unfolding. We correlate these recent findings to other biophysical observations and rationalize the role of experimental conditions in defining conformational properties and peroxidase activity of the cyt c ensemble. Latest time-resolved studies propose the trigger and the sequence of cardiolipin-induced structural transitions of cyt c.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1016/j.chemphyslip.2013.11.002

Cites

105 of 105 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • During early apoptosis, cytochrome c changes conformation through interactions with cardiolipin, contributing to cytosolic cytochrome c release and caspase activation.

    “Furthermore, during early apoptosis, cytochrome c undergoes conformational changes owing to interactions with cardiolipin, contributing to the subsequent cytosolic release of cytochrome c and caspase activation194.”

    From The role of mitochondria in rheumatic diseases (2022) · cites this paper as [194]

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Cited by

Sorted by citations

Authors
Muenzner, J., & Pletneva, E. V.
Affiliations
Dartmouth College (US)
Corresponding author
Pletneva, Ekaterina V.
Venue
Chemistry and Physics of Lipids
Publisher
Elsevier BV
Published
2014-04
Volume
179
Pages
57-63
ISSN
0009-3084 (ISSN-L)
OpenAlex
W2049774523
Cited by
74
References
105
Citations by year
2026: 1 · 2025: 6 · 2024: 4 · 2023: 2 · 2022: 5 · 2021: 6 · 2020: 8 · 2019: 6 · 2018: 5 · 2017: 13 · 2016: 5 · 2015: 9 · 2014: 3 · 2013: 1
FWCI
0.56
Type
journal article
Language
en
Open access
Locations
  • Chemistry and Physics of Lipids (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institutes of Health (RO1 - GM098502)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Keywords
cytochrome c, cardiolipin, protein-lipid interactions, apoptosis, peroxidase activity, protein unfolding, conformational heterogeneity, heme crevice, membrane insertion, time-resolved spectroscopy
MeSH terms
Animals, Cardiolipins, Cell Membrane Permeability, Free Radicals, Heme, Humans, Protein Binding, Cytochromes c

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review