Evidence map›Paper›PMID 23445323›Full record

ArticleThe journal of physical chemistry. B2013

Solution NMR and computational methods for understanding protein allostery.

Gregory Manley, Ivan Rivalta, J Patrick Loria

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2013. 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. Article
  2. Article
  3. Article
  4. Self-organization, entropy and allostery.Biochemical Society transactions · 2018
    Review
  5. Article
  6. Article
  7. Review
  8. Altering the allosteric pathway in IGPS suppresses millisecond motions and catalytic activity.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Unidirectional allostery in the regulatory subunit RIα facilitates efficient deactivation of protein kinase A.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Article
  12. Review
  13. Article
  14. NMR Methods to Study Dynamic Allostery.PLoS computational biology · 2016
    Review
  15. Article
  16. Review
  17. Review
  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.

Gregory ManleyDepartment of Chemistry, Yale University, New Haven, Connecticut 06520, United States.
Ivan Rivalta
J Patrick Loria

Funding

PREDOCTORAL PROGRAM IN BIOPHYSICST32GM008283 · NIGMS · YALE UNIVERSITY · PI XIONG, YONG · 1988 to 2022
$10.5M
NIGMS NIH HHS T32 GM008283
6 · The paper itself

Abstract

Allosterism is an essential biological regulatory mechanism. In enzymes, allosteric regulation results in an activation or inhibition of catalytic turnover. The mechanisms by which this is accomplished are unclear and vary significantly depending on the enzyme. It is commonly the case that a metabolite binds to the enzyme at a site distant from the catalytic site, yet its binding is coupled to and sensed by the active site. This coupling can manifest in changes in structure, dynamics, or both at the active site. These interactions between the allosteric and active site, which are often quite distant from one another, involve numerous atoms as well as complex conformational rearrangements of the protein secondary and tertiary structure. Interrogation of this complex biological phenomenon necessitates multiple experimental approaches. In this article, we outline a combined solution NMR spectroscopic and computational approach using molecular dynamics and network models to uncover mechanistic aspects of allostery in the enzyme imidazole glycerol phosphate synthase.

Indexed as

Allosteric RegulationAminohydrolasesCatalytic DomainHydrogen BondingHydrophobic and Hydrophilic InteractionsMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProtein BindingProteinsAminohydrolasesimidazole glycerol phosphate synthaseProteins

Identifiers

PMID23445323
PMCPMC4084788

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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.