Evidence map›Paper›PMID 10827983›Full record

ArticleBiophysical journal2000

Comparative single-molecule and ensemble myosin enzymology: sulfoindocyanine ATP and ADP derivatives.

K Oiwa, J F Eccleston, M Anson, M Kikumoto, C T Davis, G P Reid, M A Ferenczi, J E Corrie, A Yamada, H Nakayama and 1 more

Abstract read
In one paragraph

Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. A FRET assay to monitor different structural states of human β-cardiac myosin including the interacting-heads motif.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
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  5. Single molecule detection, thermal fluctuation and life.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017
    Review
  6. ATP turnover by individual myosin molecules hints at two conformers of the myosin active site.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  7. Article
  8. Article
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  16. Review
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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

11 authors.

K OiwaKansai Advanced Research Center, Communications Research Laboratory, Kobe 651-2492, Japan.
J F Eccleston
M Anson
M Kikumoto
C T Davis
G P Reid
M A Ferenczi
J E Corrie
A Yamada
H Nakayama
D R Trentham

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-molecule and macroscopic reactions of fluorescent nucleotides with myosin have been compared. The single-molecule studies serve as paradigms for enzyme-catalyzed reactions and ligand-receptor interactions analyzed as individual stochastic processes. Fluorescent nucleotides, called Cy3-EDA-ATP and Cy5-EDA-ATP, were derived by coupling the dyes Cy3.29.OH and Cy5.29.OH (compounds XI and XIV, respectively, in, Bioconjug. Chem. 4:105-111)) with 2'(3')-O-[N-(2-aminoethyl)carbamoyl]ATP (EDA-ATP). The ATP(ADP) analogs were separated into their respective 2'- and 3'-O-isomers, the interconversion rate of which was 30[OH(-)] s(-1) (0.016 h(-1) at pH 7.1) at 22 degrees C. Macroscopic studies showed that 2'(3')-O-substituted nucleotides had properties similar to those of ATP and ADP in their interactions with myosin, actomyosin, and muscle fibers, although the ATP analogs did not relax muscle as well as ATP did. Significant differences in the fluorescence intensity of Cy3-nucleotide 2'- and 3'-O-isomers in free solution and when they interacted with myosin were evident. Single-molecule studies using total internal reflection fluorescence microscopy showed that reciprocal mean lifetimes of the nucleotide analogs interacting with myosin filaments were one- to severalfold greater than predicted from macroscopic data. Kinetic and equilibrium data of nucleotide-(acto)myosin interactions derived from single-molecule microscopy now have a biochemical and physiological framework. This is important for single-molecule mechanical studies of motor proteins.

Indexed as

ActinsActomyosinAdenosine DiphosphateAdenosine TriphosphateAnimalsFluorescent DyesKineticsMuscle ContractionMuscle Fibers, SkeletalMuscle, SkeletalMyosinsMyosin SubfragmentsRabbitsStochastic ProcessesSubstrate SpecificityActinsActomyosinAdenosine DiphosphateAdenosine TriphosphateFluorescent DyesMyosinsMyosin Subfragments

Identifiers

PMID10827983
PMCPMC1300888

What OpenQuestion holds

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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.