Evidence map›Paper›PMID 18441030›Full record

ArticleBiophysical journal2008

Cooperativity and specificity in enzyme kinetics: a single-molecule time-based perspective.

Hong Qian

Abstract read
In one paragraph

Article in Biophysical journal, 2008. 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. Trade-offs and thermodynamics of energy-relay proofreading.Journal of the Royal Society, Interface · 2024
    Article
  2. A suicidal and extensively disordered luciferase with a bright luminescence.Protein science : a publication of the Protein Society · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Quantifying the flux as the driving force for nonequilibrium dynamics and thermodynamics in non-Michaelis-Menten enzyme kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Structural conditions on complex networks for the Michaelis-Menten input-output response.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  9. Article
  10. Statistics and Related Topics in Single-Molecule Biophysics.Annual review of statistics and its application · 2014
    Article
  11. Article
  12. Article
  13. Michaelis-Menten relations for complex enzymatic networks.The Journal of chemical physics · 2011
    Article
  14. Metallic-Nanostructure-Enhanced Fluorescence of Single Flavin Cofactor and Single Flavoenzyme Molecules.The journal of physical chemistry. C, Nanomaterials and interfaces · 2011
    Article
  15. Review
  16. Rate theories for biologists.Quarterly reviews of biophysics · 2010
    Review
  17. Review
  18. Article
  19. 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

1 author.

Hong QianDepartment of Applied Mathematics, University of Washington, Seattle, Washington, USA. qian@amath.washington.edu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An alternative theoretical approach to enzyme kinetics that is particularly applicable to single-molecule enzymology is presented. The theory, originated by Van Slyke and Cullen in 1914, develops enzyme kinetics from a "time perspective" rather than the traditional "rate perspective" and emphasizes the nonequilibrium steady-state nature of enzymatic reactions and the significance of small copy numbers of enzyme molecules in living cells. Sigmoidal cooperative substrate binding to slowly fluctuating, monomeric enzymes is shown to arise from association pathways with very small probability but extremely long passage time, which would be disregarded in the traditional rate perspective: A single enzyme stochastically takes alternative pathways in serial order rather than different pathways in parallel. The theory unifies dynamic cooperativity and Hopfield-Ninio's kinetic proofreading mechanism for specificity amplification.

Indexed as

Models, ChemicalModels, MolecularComputer SimulationEnzyme ActivationEnzymesKineticsSubstrate SpecificityEnzymes

Identifiers

PMID18441030
PMCPMC2426636

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.