Evidence map›Paper›PMID 23630499›Full record

ArticleFrontiers in physiology2013

Cytoskeleton and regulation of mitochondrial function: the role of beta-tubulin II.

Andrey V Kuznetsov, Sabzali Javadov, Rita Guzun, Michael Grimm, Valdur Saks

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Myocardial Cytoskeletal Adaptations in Advanced Kidney Disease.Journal of the American Heart Association · 2022
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Mitochondrial mechanosensor in cardiovascular diseases.Vascular biology (Bristol, England) · 2020
    Review
  17. Review
  18. Review
  19. Review
  20. Mitochondrial Deformation During the Cardiac Mechanical Cycle.Anatomical record (Hoboken, N.J. : 2007) · 2019
    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

5 authors at 4 institutions in 3 countries.

Andrey V KuznetsovCardiac Surgery Research Laboratory, Department of Cardiac Surgery, Innsbruck Medical University Innsbruck, Tirol, Austria.
Sabzali Javadov
Rita Guzun
Michael Grimm
Valdur Saks
Innsbruck Medical University · ATInserm · FRLaboratory of Fundamental and Applied Bioenergetics · FRUniversity of Puerto Rico System · PR

Funding

Mitochondrial Permeability Transition as a Target for Cardioprotection in Heart FSC1HL118669 · NHLBI · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI JAVADOV, SABZALI · 2012 to 2016
$1.3M
Austrian Science Fund FWF P 22080NHLBI NIH HHS SC1 HL118669
6 · The paper itself

Abstract

The control of mitochondrial function is a cardinal issue in the field of cardiac bioenergetics, and the analysis of mitochondrial regulations is central to basic research and in the diagnosis of many diseases. Interaction between cytoskeletal proteins and mitochondria can actively participate in mitochondrial regulation. Potential candidates for the key roles in this regulation are the cytoskeletal proteins plectin and tubulin. Analysis of cardiac cells has revealed regular arrangement of β-tubulin II, fully co-localized with mitochondria. β-Tubulin IV demonstrated a characteristic staining of branched network, β-tubulin III was matched with Z-lines, and β-tubulin I was diffusely spotted and fragmentary polymerized. In contrast, HL-1 cells were characterized by the complete absence of β-tubulin II. Comparative analysis of cardiomyocytes and HL-1 cells revealed a dramatic difference in the mechanisms of mitochondrial regulation. In the heart, colocalization of β-tubulin isotype II with mitochondria suggests that it can participate in the coupling of ATP-ADP translocase (ANT), mitochondrial creatine kinase (MtCK), and VDAC (ANT-MtCK-VDAC). This mitochondrial supercomplex is responsible for the efficient intracellular energy transfer via the phosphocreatine pathway. Existing data suggest that cytoskeletal proteins may control the VDAC, contributing to maintenance of mitochondrial and cellular physiology.

Indexed as

beta tubulin isotypescardiomyocytesconfocal microscopycreatine kinaseHL-1 cellsmitochondria-cytoskeleton interactionsmitochondrial regulationVDAC

Identifiers

PMID23630499
PMCPMC3631707
OpenAlexW2105095482

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.