Evidence map›Paper›PMID 22562794›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Allosteric inhibition of individual enzyme molecules trapped in lipid vesicles.

Hubert M Piwonski, Mila Goomanovsky, David Bensimon, Amnon Horovitz, Gilad Haran

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 76 citations in OpenAlex.

  1. Review
  2. Review
  3. Single-Molecule FRET of Membrane Transport Proteins.Chembiochem : a European journal of chemical biology · 2021
    Review
  4. Review
  5. Bioinspired Molecular Factories with Architecture and In Vivo Functionalities as Cell Mimics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Slow domain reconfiguration causes power-law kinetics in a two-state enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Review
  14. Review
  15. Principles of allosteric interactions in cell signaling.Journal of the American Chemical Society · 2014
    Review
  16. Review
  17. Enzyme molecules in solitary confinement.Molecules (Basel, Switzerland) · 2014
    Review
  18. Article
  19. Review
  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

5 authors at 2 institutions in 3 countries.

Hubert M PiwonskiDepartment of Chemical Physics, Weizmann Institute of Science, Rehovot 76100, Israel.
Mila Goomanovsky
David Bensimon
Amnon Horovitz
Gilad Haran
Weizmann Institute of Science · ILUniversity of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymatic inhibition by product molecules is an important and widespread phenomenon. We describe an approach to study product inhibition at the single-molecule level. Individual HRP molecules are trapped within surface-tethered lipid vesicles, and their reaction with a fluorogenic substrate is probed. While the substrate readily penetrates into the vesicles, the charged product (resorufin) gets trapped and accumulates inside the vesicles. Surprisingly, individual enzyme molecules are found to stall when a few tens of product molecules accumulate. Bulk enzymology experiments verify that the enzyme is noncompetitively inhibited by resorufin. The initial reaction velocity of individual enzyme molecules and the number of product molecules required for their complete inhibition are broadly distributed and dynamically disordered. The two seemingly unrelated parameters, however, are found to be substantially correlated with each other in each enzyme molecule and over long times. These results suggest that, as a way to counter disorder, enzymes have evolved the means to correlate fluctuations at structurally distinct functional sites.

Indexed as

Allosteric RegulationAlgorithmsAllosteric SiteEnzymesFluorescent DyesHorseradish PeroxidaseKineticsLipidsModels, ChemicalModels, MolecularMolecular StructureOxazinesProtein BindingProtein Structure, TertiaryEnzymesFluorescent DyesHorseradish PeroxidaseLipidsOxazinesresorufin

Identifiers

PMID22562794
PMCPMC3365166
OpenAlexW2027958475

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.