Evidence map›Paper›PMID 22995500›Full record

ArticleBiophysical journal2012

Thick-to-thin filament surface distance modulates cross-bridge kinetics in Drosophila flight muscle.

Bertrand C W Tanner, Gerrie P Farman, Thomas C Irving, David W Maughan, Bradley M Palmer, Mark S Miller

Abstract read
In one paragraph

Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Review
  3. Developmental remodelling ofOpen biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Cardiac troponin T N-domain variant destabilizes the actin interface resulting in disturbed myofilament function.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Structural and functional impact of troponin C-mediated CaJournal of molecular and cellular cardiology · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

6 authors.

Bertrand C W TannerDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont, USA.
Gerrie P Farman
Thomas C Irving
David W Maughan
Bradley M Palmer
Mark S Miller

Funding

X-RAY STUDIES OF NEUROFIBRILLARY TANGLES IN ALZHEIMER'S DISEASE BRAIN TISSUEP41RR008630 · NCRR · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2001 to 2011
$14.4M
Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
POST-DOCTORAL CARDIOVASCULAR RESEARCH TRAINING PROGRAMT32HL007647 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI LEWINTER, MARTIN M · 1988 to 2013
$3.3M
Myosin-based kinetic differences between muscle typesR01AR049425 · NIAMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI MAUGHAN, DAVID WAYNE · 2003 to 2006
$1.1M
Single Skeletal Muscle Fiber Mechanics and Myosin Kinetics in Human AgingK01AG031303 · NIA · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI MILLER, MARK STUART · 2008 to 2012
$611k
NCRR NIH HHS 2P41RR008630-17NCRR NIH HHS P41 RR008630NHLBI NIH HHS T32 HL007647NIAMS NIH HHS AR-049425NIAMS NIH HHS R01 AR049425NIA NIH HHS AG-031303NIA NIH HHS K01 AG031303NIGMS NIH HHS 9 P41 GM103622-17NIGMS NIH HHS P41 GM103622
6 · The paper itself

Abstract

The demembranated (skinned) muscle fiber preparation is widely used to investigate muscle contraction because the intracellular ionic conditions can be precisely controlled. However, plasma membrane removal results in a loss of osmotic regulation, causing abnormal hydration of the myofilament lattice and its proteins. We investigated the structural and functional consequences of varied myofilament lattice spacing and protein hydration on cross-bridge rates of force development and detachment in Drosophila melanogaster indirect flight muscle, using x-ray diffraction to compare the lattice spacing of dissected, osmotically compressed skinned fibers to native muscle fibers in living flies. Osmolytes of different sizes and exclusion properties (Dextran T-500 and T-10) were used to differentially alter lattice spacing and protein hydration. At in vivo lattice spacing, cross-bridge attachment time (t(on)) increased with higher osmotic pressures, consistent with a reduced cross-bridge detachment rate as myofilament protein hydration decreased. In contrast, in the swollen lattice, t(on) decreased with higher osmotic pressures. These divergent responses were reconciled using a structural model that predicts t(on) varies inversely with thick-to-thin filament surface distance, suggesting that cross-bridge rates of force development and detachment are modulated more by myofilament lattice geometry than protein hydration. Generalizing these findings, our results suggest that cross-bridge cycling rates slow as thick-to-thin filament surface distance decreases with sarcomere lengthening, and likewise, cross-bridge cycling rates increase during sarcomere shortening. Together, these structural changes may provide a mechanism for altering cross-bridge performance throughout a contraction-relaxation cycle.

Indexed as

Flight, AnimalActinsAnimalsBiomechanical PhenomenaDextransDrosophila melanogasterKineticsMuscle, SkeletalMyofibrilsMyosinsOsmosisSurface PropertiesActinsDextransMyosins

Identifiers

PMID22995500
PMCPMC3447602

What OpenQuestion holds

Textmetadata
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Registered trials

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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.