Evidence map›Paper›PMID 25645586›Full record

ArticleAging cell2015

Aberrant post-translational modifications compromise human myosin motor function in old age.

Meishan Li, Hannah Ogilvie, Julien Ochala, Konstantin Artemenko, Hiroyuki Iwamoto, Naoto Yagi, Jonas Bergquist, Lars Larsson

Registry-linked trialOpen access · goldAbstract read
In one paragraph

Article in Aging cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT07089667 (The Effect of Virtual Reality Exergame on Physical Activity and Fitness in The Elderly), which is not on this map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.9field-weighted citation impact, top 6% 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.

NCT07089667 nacompletednot on this mapstarted 2024, after this paper: background citation

The Effect of Virtual Reality Exergame on Physical Activity and Fitness in The Elderly

TypeinterventionalSponsorHasanuddin UniversityRan2024 to 2024Enrolled40ConditionsHealthy ElderlyArmsvirtual reality exergame, Conventional
3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 65 citations in OpenAlex.

  1. Alterations of actin in aging.Journal of cell science · 2026
    Review
  2. Article
  3. Article
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  6. Mechanisms of Biological Aging with Special Reference to the Skeletal Muscle.Advances in experimental medicine and biology · 2025
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
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  19. Predominant myosin superrelaxed state in canine myocardium with naturally occurring dilated cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2023
    Article
  20. 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

8 authors at 4 institutions in 3 countries.

Meishan LiDepartment of Physiology and Pharmacology, Karolinska Institutet, SE-171 77, Stockholm, Sweden; Department of Clinical Neuroscience, Clinical Neurophysiology, Karolinska Institutet, SE-171 77, Stockholm, Sweden.
Hannah Ogilvie
Julien Ochala
Konstantin Artemenko
Hiroyuki Iwamoto
Naoto Yagi
Jonas Bergquist
Lars Larsson
Karolinska Institutet · SEJapan Synchrotron Radiation Research Institute · JPScience for Life Laboratory · SEKing's College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Novel experimental methods, including a modified single fiber in vitro motility assay, X-ray diffraction experiments, and mass spectrometry analyses, have been performed to unravel the molecular events underlying the aging-related impairment in human skeletal muscle function at the motor protein level. The effects of old age on the function of specific myosin isoforms extracted from single human muscle fiber segments, demonstrated a significant slowing of motility speed (P < 0.001) in old age in both type I and IIa myosin heavy chain (MyHC) isoforms. The force-generating capacity of the type I and IIa MyHC isoforms was, on the other hand, not affected by old age. Similar effects were also observed when the myosin molecules extracted from muscle fibers were exposed to oxidative stress. X-ray diffraction experiments did not show any myofilament lattice spacing changes, but unraveled a more disordered filament organization in old age as shown by the greater widths of the 1, 0 equatorial reflections. Mass spectrometry (MS) analyses revealed eight age-specific myosin post-translational modifications (PTMs), in which two were located in the motor domain (carbonylation of Pro79 and Asn81) and six in the tail region (carbonylation of Asp900, Asp904, and Arg908; methylation of Glu1166; deamidation of Gln1164 and Asn1168). However, PTMs in the motor domain were only observed in the IIx MyHC isoform, suggesting PTMs in the rod region contributed to the observed disordering of myosin filaments and the slowing of motility speed. Hence, interventions that would specifically target these PTMs are warranted to reverse myosin dysfunction in old age.

Indexed as

Protein Processing, Post-TranslationalAdultAgedAged, 80 and overAge FactorsAgingHumansMaleMuscle, SkeletalMyosinsProtein IsoformsYoung AdultMyosinsProtein Isoformsagingfunctionmyosinpost-translational modificationskeletal muscle

Identifiers

PMID25645586
PMCPMC4364835
OpenAlexW2165462192

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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.