Evidence map›Paper›PMID 21562225›Full record

ArticleMolecular biology of the cell2011

Vimentin intermediate filaments modulate the motility of mitochondria.

Oxana E Nekrasova, Melissa G Mendez, Ivan S Chernoivanenko, Pyotr A Tyurin-Kuzmin, Edward R Kuczmarski, Vladimir I Gelfand, Robert D Goldman, Alexander A Minin

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

89 citing papers in PubMed, 144 citations in OpenAlex.

  1. Review
  2. Article
  3. Vimentin Intermediate Filaments: A Paradigm Shift From Static Structure to Dynamic Cytoplasmic Network.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  4. The innate immune mediator group IIA secreted phospholipase AFrontiers in cell and developmental biology · 2026
    Article
  5. Review
  6. The intermediate filament protein GFAP regulates mitochondrial fission in astrocytes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Colonocyte keratins stabilize mitochondria and contribute to mitochondrial energy metabolism.American journal of physiology. Gastrointestinal and liver physiology · 2024
    Article
  18. Article
  19. Review
  20. Article

29 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 2 countries.

Oxana E NekrasovaGroup of Cell Biology, Institute of Protein Research, Russian Academy of Sciences, Moscow 119988, Russia.
Melissa G Mendez
Ivan S Chernoivanenko
Pyotr A Tyurin-Kuzmin
Edward R Kuczmarski
Vladimir I Gelfand
Robert D Goldman
Alexander A Minin
Northwestern University · USInstitute of Protein Research · RUKoltzov Institute of Developmental Biology · RU

Funding

REGULATION OF MYOSIN DRIVEN ORGANELLE TRANSPORTR01GM052111 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GELFAND, VLADIMIR I · 1999 to 2018
$8.3M
INTERMEDIATE FILAMENT CELL SURFACE INTERACTIONSR37GM036806 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOLDMAN, ROBERT D · 1999 to 2008
$3.9M
INTERMEDIATE FILAMENT-CELL SURFACE INTERACTIONSR01GM036806 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOLDMAN, ROBERT D · 1986 to 2010
$795k
MICROTUBULE MOTORS--SPECIFICITY AND REGULATIONR55GM052111 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GELFAND, VLADIMIR I · 1995 to 1995
–
NIGMS NIH HHS GM 036806NIGMS NIH HHS GM 52111NIGMS NIH HHS R01 GM036806NIGMS NIH HHS R01 GM052111NIGMS NIH HHS R37 GM036806
6 · The paper itself

Abstract

Interactions with vimentin intermediate filaments (VimIFs) affect the motility, distribution, and anchorage of mitochondria. In cells lacking VimIFs or in which VimIF organization is disrupted, the motility of mitochondria is increased relative to control cells that express normal VimIF networks. Expression of wild-type VimIF in vimentin-null cells causes mitochondrial motility to return to normal (slower) rates. In contrast, expressing vimentin with mutations in the mid-region of the N-terminal non-α-helical domain (deletions of residues 41-96 or 45-70, or substitution of Pro-57 with Arg) did not inhibit mitochondrial motility even though these mutants retain their ability to assemble into VimIFs in vivo. It was also found that a vimentin peptide consisting of residues 41-94 localizes to mitochondria. Taken together, these data suggest that VimIFs bind directly or indirectly to mitochondria and anchor them within the cytoplasm.

Indexed as

3T3 CellsActinsAnimalsCell LineCell MovementCytoplasmHumansIntermediate FilamentsMiceMitochondriaModels, MolecularMutationProtein Structure, SecondaryVimentinActinsVimentin

Identifiers

PMID21562225
PMCPMC3128530
OpenAlexW2113046312

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.