Evidence map›Paper›PMID 9635759›Full record

ArticleBiophysical journal1998

ATP analogs and muscle contraction: mechanics and kinetics of nucleoside triphosphate binding and hydrolysis.

M Regnier, D M Lee, E Homsher

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

52 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Fueling the heartbeat: Dynamic regulation of intracellular ATP during excitation-contraction coupling in ventricular myocytes.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Structural OFF/ON transitions of myosin in relaxed porcine myocardium predict calcium-activated force.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. Review
  11. Modulation of post-powerstroke dynamics in myosin II by 2'-deoxy-ADP.Archives of biochemistry and biophysics · 2021
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Cardiac myosin activation with 2-deoxy-ATP via increased electrostatic interactions with actin.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Molecular mechanisms underlying deoxy-ADP.Pi activation of pre-powerstroke myosin.Protein science : a publication of the Protein Society · 2017
    Article
  18. Review
  19. 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

3 authors at 1 institution in 1 country.

M RegnierDepartment of Physiology, School of Medicine, University of California, Los Angeles 90095, USA.
D M Lee
E Homsher
University of California, Los Angeles · US

Funding

MUSCLE ENERGETICS AND CHEMOMECHANICAL TRANSDUCTIONR01AR030988 · NIAMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HOMSHER, EARL E · 1986 to 2007
$1.9M
NIAMS NIH HHS AR 30988
6 · The paper itself

Abstract

The mechanical behavior of skinned rabbit psoas muscle fiber contractions and in vitro motility of F-actin (Vf) have been examined using ATP, CTP, UTP, or their 2-deoxy forms (collectively designated as nucleotide triphosphates or NTPs) as contractile substrates. Measurements of actin-activated heavy meromyosin (HMM) NTPase, the rates of NTP binding to myosin and actomyosin, NTP-mediated acto-HMM dissociation, and NTP hydrolysis by acto-HMM were made for comparison to the mechanical results. The data suggest a very similar mechanism of acto-HMM NTP hydrolysis. Whereas all NTPs studied support force production and stiffness that vary by a factor 2 or less, the unloaded shortening velocity (Vu) of muscle fibers varies by almost 10-fold. 2-Deoxy ATP (dATP) was unique in that Vu was 30% greater than with ATP. Parallel behavior was observed between Vf and the steady-state maximum actin-activated HMM ATPase rate. Further comparisons suggest that the variation in force correlates with the rate and equilibrium constant for NTP cleavage; the variations in Vu or Vf are related to the rate of cross-bridge dissociation caused by NTP binding or to the rate(s) of product release.

Indexed as

Acid Anhydride HydrolasesActomyosinAdenosine TriphosphateAnimalsFemaleHydrolysisIn Vitro TechniquesIsometric ContractionKineticsMuscle Fibers, SkeletalMuscle, SkeletalMyosinsMyosin SubfragmentsNucleoside-TriphosphataseRabbitsRibonucleotidesAcid Anhydride HydrolasesActomyosinAdenosine TriphosphateMyosinsMyosin SubfragmentsNucleoside-TriphosphataseRibonucleotides

Identifiers

PMID9635759
PMCPMC1299646
OpenAlexW2164668862

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.