Evidence map›Paper›PMID 27070509›Full record

ArticleThe journal of physical chemistry. B2016

Statistical Mechanics of Allosteric Enzymes.

Tal Einav, Linas Mazutis, Rob Phillips

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed.

  1. Article
  2. A computational dynamic model of combination treatment for type II inhibitors with asciminib.Protein science : a publication of the Protein Society · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Allosteric crosstalk in modular proteins: Function fine-tuning and drug design.Computational and structural biotechnology journal · 2023
    Review
  7. Review
  8. Allostery and Kinetic Proofreading.The journal of physical chemistry. B · 2019
    Article
  9. Article
  10. 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.

Tal EinavDepartment of Physics, California Institute of Technology , Pasadena, California 91125, United States.
Linas MazutisInstitute of Biotechnology, Vilnius University , Vilnius, 02241 Lithuania.
Rob PhillipsDepartment of Applied Physics and Division of Biology, California Institute of Technology , Pasadena, California 91125, United States.

Funding

NIH Director's Pioneer Award (RMI)DP1OD000217 · OD · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI PHILLIPS, ROB · 2004 to 2008
$4.0M
Single-Molecule and Single-Cell Analysis of Transcription Factor-DNA ComplexesR01GM085286 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI PHILLIPS, ROB · 2009 to 2015
$2.8M
Physiology: Modern Cell Biology Using Microscopic, Biochemical and Computational ApproachesR13GM085967 · NIGMS · MARINE BIOLOGICAL LABORATORY · PI FLETCHER, DANIEL A, HYMAN, LINDA E · 2008 to 2019
$1.7M
NIGMS NIH HHS R01 GM085286NIGMS NIH HHS R13 GM085967NIH HHS DP1 OD000217Wellcome Trust
6 · The paper itself

Abstract

The concept of allostery in which macromolecules switch between two different conformations is a central theme in biological processes ranging from gene regulation to cell signaling to enzymology. Allosteric enzymes pervade metabolic processes, yet a simple and unified treatment of the effects of allostery in enzymes has been lacking. In this work, we take a step toward this goal by modeling allosteric enzymes and their interaction with two key molecular players-allosteric regulators and competitive inhibitors. We then apply this model to characterize existing data on enzyme activity, comment on how enzyme parameters (such as substrate binding affinity) can be experimentally tuned, and make novel predictions on how to control phenomena such as substrate inhibition.

Indexed as

Models, ChemicalAllosteric RegulationAllosteric SiteBinding, CompetitiveBinding SitesBiocatalysisCatalytic DomainEnzyme InhibitorsEnzymesHumansHydrolysisKineticsProtein BindingThermodynamicsEnzyme InhibitorsEnzymes

Identifiers

PMID27070509
PMCPMC5452729

What OpenQuestion holds

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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.