Evidence map›Paper›PMID 41411686›Full record

ArticleJournal of inorganic biochemistry2026

Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes.

Dong-Woo Shin, Fangfang Zhong, Ekaterina V Pletneva

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of inorganic biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Dong-Woo ShinDepartment of Chemistry, Dartmouth College, Hanover, NH 03755, United States.
Fangfang ZhongDepartment of Chemistry, Dartmouth College, Hanover, NH 03755, United States.
Ekaterina V PletnevaDepartment of Chemistry, Dartmouth College, Hanover, NH 03755, United States. Electronic address: ekaterina.pletneva@dartmouth.edu.

Funding

Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MIERKE, DALE F · 2016 to 2025
$25.9M
Conformational Properties of Cytochromes in DiseaseR01GM098502 · NIGMS · DARTMOUTH COLLEGE · PI PLETNEVA, EKATERINA · 2011 to 2023
$2.9M
NIGMS NIH HHS P20 GM113132NIGMS NIH HHS R01 GM098502
6 · The paper itself

Abstract

The heme in the protein cytochrome (cyt) c is surrounded by loops C and D that differ in their sequences across species. Mutations G41S and Y48H in human (hu) cyt c are associated with thrombocytopenia and have been extensively studied. Herein, we describe effects of the same mutations in horse heart (hh) cyt c and make comparisons to those in the hu protein. While wild-type (WT) hu and hh cyt c proteins have similar global stabilities, unfolding of the hh protein is less cooperative. The differences are further amplified in the mutants. Loop dynamics were probed computationally through MD simulations and experimentally by characterizing the alkaline transition. With G41S and Y48H mutations in hh cyt c, loop C made fewer contacts with loop D and the dynamics of loop D were enhanced. Only the Y48H mutation decreased the reduction potential in hh cyt c, but both G41S and Y48H mutations increased the intrinsic peroxidase activity. The rate constant k

Indexed as

Cytochromes cAnimalsHemeHorsesHumansMolecular Dynamics SimulationMutationCytochromes cHemeAlkaline transitionCytochrome cElectron transferFoldonsPeroxidase activity

Identifiers

PMID41411686
PMCPMC12768443

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Registered trials

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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.