Evidence map›Paper›PMID 10047983›Full record

ArticleJournal of muscle research and cell motility1998

A 7-amino-acid insert in the heavy chain nucleotide binding loop alters the kinetics of smooth muscle myosin in the laser trap.

A M Lauzon, M J Tyska, A S Rovner, Y Freyzon, D M Warshaw, K M Trybus

Abstract read
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In one paragraph

Article in Journal of muscle research and cell motility, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

64 citing papers in PubMed, 133 citations in OpenAlex.

  1. Article
  2. Article
  3. Alpha and beta myosin isoforms and human atrial and ventricular contraction.Cellular and molecular life sciences : CMLS · 2021
    Review
  4. Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021
    Review
  5. Article
  6. The Huxley crossbridge model as the basic mechanism for airway smooth muscle contraction.American journal of physiology. Lung cellular and molecular physiology · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Velocities of unloaded muscle filaments are not limited by drag forces imposed by myosin cross-bridges.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  11. Kinetic characterization of the sole nonmuscle myosin-2 from the model organism Drosophila melanogaster.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
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4 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

6 authors at 1 institution in 1 country.

A M LauzonDepartment of Molecular Physiology and Biophysics, University of Vermont, Burlington 05405, USA.
M J Tyska
A S Rovner
Y Freyzon
D M Warshaw
K M Trybus
University of Vermont · US

Funding

MOLECULAR MECHANICS OF MUTANT SMOOTH MUSCLE MYOSINSR01HL054568 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI TRYBUS, KATHLEEN M · 1996 to 2000
$691k
NHLBI NIH HHS HL54568
6 · The paper itself

Abstract

Two smooth muscle myosin heavy chain isoforms differ by a 7-amino-acid insert in a flexible surface loop located near the nucleotide binding site. The non-inserted isoform is predominantly found in tonic muscle, while the inserted isoform is mainly found in phasic muscle. The inserted isoform has twice the actin-activated ATPase activity and actin filament velocity in the in vitro motility assay as the non-inserted isoform. We used the laser trap to characterize the molecular mechanics and kinetics of the inserted isoform ((+)insert) and of a mutant lacking the insert ((-)insert), analogous to the isoform found in tonic muscle. The constructs were expressed as heavy meromyosin using the baculovirus/insect cell system. Unitary displacement (d) was similar for both constructs (approximately 10 nm) but the attachment time (t(on) for the (-)insert was twice as long as for the (+)insert regardless of the [MgATP]. Both the relative average isometric force (Favg(-insert)/Favg(+insert) = 1.1 +/- 0.2 (mean +/- SE) using the in vitro motility mixture assay, and the unitary force (F approximately 1 pN) using the laser trap, showed no difference between the two constructs. However, as under unloaded conditions, t(on) under loaded conditions was longer for the (-)insert compared with the (+)insert construct at limiting [MgATP]. These data suggest that the insert in this surface loop does not affect the mechanics but rather the kinetics of the cross-bridge cycle. Through comparisons of t(on) from d measurements to various [MgATP], we conclude that the insert affects two specific steps in the cross-bridge cycle, that is, MgADP release and MgATP binding.

Indexed as

LasersActinsAdenosine TriphosphateAmino Acid SequenceAnimalsChickensKineticsMolecular Motor ProteinsMuscle ContractionMuscle, SmoothMyosin Heavy ChainsPhotochemistryProtein Structure, TertiaryStress, MechanicalActinsAdenosine TriphosphateMolecular Motor ProteinsMyosin Heavy Chains

Identifiers

PMID10047983
OpenAlexW280126174

What OpenQuestion holds

Texttitle and abstract
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.