Evidence map›Paper›PMID 19450484›Full record

ArticleBiophysical journal2009

Alternative S2 hinge regions of the myosin rod affect myofibrillar structure and myosin kinetics.

Mark S Miller, Corey M Dambacher, Aileen F Knowles, Joan M Braddock, Gerrie P Farman, Thomas C Irving, Douglas M Swank, Sanford I Bernstein, David W Maughan

Abstract read
In one paragraph

Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Myosin: Formation and maintenance of thick filaments.Animal science journal = Nihon chikusan Gakkaiho · 2019
    Review
  3. Myosin II sequences for Lethocerus indicus.Journal of muscle research and cell motility · 2017
    Article
  4. To understand muscle you must take it apart.Frontiers in physiology · 2014
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
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

9 authors.

Mark S MillerDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont, USA. Mark.Miller@uvm.edu
Corey M Dambacher
Aileen F Knowles
Joan M Braddock
Gerrie P Farman
Thomas C Irving
Douglas M Swank
Sanford I Bernstein
David W Maughan

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
Myosin Hinge Region In ContractionR01AR043396 · NIAMS · SAN DIEGO STATE UNIVERSITY · PI BERNSTEIN, SANFORD I · 1996 to 2005
$1.6M
Myosin structural and kinetic mechanisms that differentiate fast and slow muscle R01AR055611 · NIAMS · RENSSELAER POLYTECHNIC INSTITUTE · PI SWANK, DOUGLAS M · 2007 to 2012
$1.6M
Myosin-based kinetic differences between muscle typesR01AR049425 · NIAMS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI MAUGHAN, DAVID WAYNE · 2003 to 2006
$1.1M
NCRR NIH HHS P41 RR008630NCRR NIH HHS RR-08630NIAMS NIH HHS R01 AR043396NIAMS NIH HHS R01 AR049425NIAMS NIH HHS R01 AR055611
6 · The paper itself

Abstract

The subfragment 2/light meromyosin "hinge" region has been proposed to significantly contribute to muscle contraction force and/or speed. Transgenic replacement of the endogenous fast muscle isovariant hinge A (exon 15a) in Drosophila melanogaster indirect flight muscle with the slow muscle hinge B (exon 15b) allows examination of the structural and functional changes when only this region of the myosin molecule is different. Hinge B was previously shown to increase myosin rod length, increase A-band and sarcomere length, and decrease flight performance compared to hinge A. We applied additional measures to these transgenic lines to further evaluate the consequences of modifying this hinge region. Structurally, the longer A-band and sarcomere lengths found in the hinge B myofibrils appear to be due to the longitudinal addition of myosin heads. Functionally, hinge B, although a significant distance from the myosin catalytic domain, alters myosin kinetics in a manner consistent with this region increasing myosin rod length. These structural and functional changes combine to decrease whole fly wing-beat frequency and flight performance. Our results indicate that this hinge region plays an important role in determining myosin kinetics and in regulating thick and thin filament lengths as well as sarcomere length.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAnimalsAnimals, Genetically ModifiedBiomechanical PhenomenaDrosophila melanogasterDrosophila ProteinsFlight, AnimalHumansKineticsMicroscopy, ElectronMolecular Sequence DataMuscle Fibers, SkeletalMyofibrilsMyosin SubfragmentsMyosin Type IIAdenosine TriphosphatasesDrosophila ProteinsMyosin SubfragmentsMyosin Type II

Identifiers

PMID19450484
PMCPMC2712142

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.