Evidence map›Paper›PMID 37989876›Full record

ArticleScientific reports2023

Mutation at the entrance of the quinone cavity severely disrupts quinone binding in respiratory complex I.

Jason Tae Yi, Panyue Wang, Alexei A Stuchebrukhov

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed, 1 pooled it
0.6field-weighted citation impact, top 29% 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

2 citing papers in PubMed, 1 synthesis or guideline pooled it, 4 citations in OpenAlex.

  1. Pooled it
  2. 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

3 authors at 1 institution in 1 country.

Jason Tae YiDepartment of Chemistry, University of California at Davis, One Shields Avenue, Davis, CA, 95616, USA.
Panyue WangDepartment of Chemistry, University of California at Davis, One Shields Avenue, Davis, CA, 95616, USA.
Alexei A StuchebrukhovDepartment of Chemistry, University of California at Davis, One Shields Avenue, Davis, CA, 95616, USA. aastuchebrukhov@ucdavis.edu.
University of California, Davis · US

Funding

Theoretical Study of Charge Transfer in Cytochrome C OxidaseR01GM054052 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI STUCHEBRUKHOV, ALEXEI A · 2002 to 2021
$3.3M
THEORETICAL STUDY OF BIOLOGICAL ELECTRON TRANSFERR29GM054052 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI STUCHEBRUKHOV, ALEXEI A · 1996 to 2000
$101k
NIGMS NIH HHS R01 GM054052NIGMS NIH HHS R29 GM054052NIH HHS GM054052
6 · The paper itself

Abstract

In all resolved structures of complex I, there exists a tunnel-like Q-chamber for ubiquinone binding and reduction. The entrance to the Q-chamber in ND1 subunit forms a narrow bottleneck, which is rather tight and requires thermal conformational changes for ubiquinone to get in and out of the binding chamber. The substitution of alanine with threonine at the bottleneck (AlaThr MUT), associated with 3460/ND1 mtDNA mutation in human complex I, is implicated in Leber's Hereditary Optic Neuropathy (LHON). Here, we show the AlaThr MUT further narrows the Q-chamber entrance cross-section area by almost 30%, increasing the activation free energy barrier of quinone passage by approximately 5 kJ mol

Indexed as

Electron Transport Complex IOptic Atrophy, Hereditary, LeberDNA, MitochondrialHumansMitochondriaMutationUbiquinoneWaterDNA, MitochondrialElectron Transport Complex IUbiquinoneWater

Identifiers

PMID37989876
PMCPMC10663621
OpenAlexW4388869209

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.