Evidence map›Paper›PMID 11159452›Full record

ArticleBiophysical journal2001

Mechanical fatigue in repetitively stretched single molecules of titin.

M S Kellermayer, S B Smith, C Bustamante, H L Granzier

Abstract read
In one paragraph

Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

  1. Trial
  2. Article
  3. Cardiac myofibril networks induce shear stress.NPJ systems biology and applications · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Mechanical Properties of Viruses.Sub-cellular biochemistry · 2024
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Muscle thixotropy-where are we now?Journal of applied physiology (Bethesda, Md. : 1985) · 2019
    Review
  14. Article
  15. Mechanical and thermodynamic properties of AβBeilstein journal of nanotechnology · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Mechanical properties of respiratory muscles.Comprehensive Physiology · 2013
    Review
  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

4 authors.

M S KellermayerDepartment of Biophysics, Pécs University Medical School, Pécs, H-7624 Hungary.
S B Smith
C Bustamante
H L Granzier

Funding

THE PHYSICAL CHEMISTRY OF NUCLEIC ACIDSR01GM032543 · NIGMS · UNIVERSITY OF OREGON · PI CARLOS Jose BUSTAMANTE · 1985 to 2026
$6.4M
Function of Giant Sarcomere Matrix Proteins in MuscleR01HL062881 · NHLBI · WASHINGTON STATE UNIVERSITY · PI GRANZIER, HENK L. · 1999 to 2018
$6.4M
TITIN AND HEART FUNCTION AND DISEASE (INDIVIDUAL)R01HL061497 · NHLBI · WASHINGTON STATE UNIVERSITY · PI GRANZIER, HENK L. · 1998 to 2007
$3.3M
PHYSICAL CHEMISTRY OF NUCLEIC ACIDSR37GM032543 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BUSTAMANTE, CARLOS JOSE · 1999 to 2008
$2.4M
NHLBI NIH HHS HL61497NHLBI NIH HHS HL62881NIGMS NIH HHS GM-32543
6 · The paper itself

Abstract

Relaxed striated muscle cells exhibit mechanical fatigue when exposed to repeated stretch and release cycles. To understand the molecular basis of such mechanical fatigue, single molecules of the giant filamentous protein titin, which is the main determinant of sarcomeric elasticity, were repetitively stretched and released while their force response was characterized with optical tweezers. During repeated stretch-release cycles titin becomes mechanically worn out in a process we call molecular fatigue. The process is characterized by a progressive shift of the stretch-force curve toward increasing end-to-end lengths, indicating that repeated mechanical cycles increase titin's effective contour length. Molecular fatigue occurs only in a restricted force range (0-25 pN) during the initial part of the stretch half-cycle, whereas the rest of the force response is repeated from one mechanical cycle to the other. Protein-folding models fail to explain molecular fatigue on the basis of an incomplete refolding of titin's globular domains. Rather, the process apparently derives from the formation of labile nonspecific bonds cross-linking various sites along a pre-unfolded titin segment. Because titin's molecular fatigue occurs in a physiologically relevant force range, the process may play an important role in dynamically adjusting muscle's response to the recent history of mechanical perturbations.

Indexed as

AnimalsBiomechanical PhenomenaBiophysical PhenomenaBiophysicsConnectinHumansIn Vitro TechniquesMicroscopy, ConfocalMicrospheresModels, BiologicalMuscle FatigueMuscle Fibers, SkeletalMuscle ProteinsProtein FoldingProtein KinasesRabbitsConnectinMuscle ProteinsProtein KinasesTTN protein, human

Identifiers

PMID11159452
PMCPMC1301283

What OpenQuestion holds

Textmetadata
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.