Evidence map›Paper›PMID 29380452›Full record

ReviewProtein science : a publication of the Protein Society2018

Engineered control of enzyme structural dynamics and function.

David D Boehr, Rebecca N D'Amico, Kathleen F O'Rourke

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Catalyst-based biomolecular logic gates.Catalysts (Basel, Switzerland) · 2022
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Harnessing Conformational Plasticity to Generate Designer Enzymes.Journal of the American Chemical Society · 2020
    Review
  18. Single-molecule FRET methods to study the dynamics of proteins at work.Current opinion in biomedical engineering · 2019
    Article
  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.

David D BoehrDepartment of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, 16802, USA.
Rebecca N D'AmicoDepartment of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, 16802, USA.
Kathleen F O'RourkeDepartment of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, 16802, USA.

Funding

Watching Conformational Rearrangements in Poliovirus RNA-Dependent RNA PolymeraseR01AI104878 · NIAID · PENNSYLVANIA STATE UNIVERSITY, THE · PI BOEHR, DAVID DOUGLAS · 2014 to 2024
$3.0M
NIAID NIH HHS R01 AI104878
6 · The paper itself

Abstract

Enzymes undergo a range of internal motions from local, active site fluctuations to large-scale, global conformational changes. These motions are often important for enzyme function, including in ligand binding and dissociation and even preparing the active site for chemical catalysis. Protein engineering efforts have been directed towards manipulating enzyme structural dynamics and conformational changes, including targeting specific amino acid interactions and creation of chimeric enzymes with new regulatory functions. Post-translational covalent modification can provide an additional level of enzyme control. These studies have not only provided insights into the functional role of protein motions, but they offer opportunities to create stimulus-responsive enzymes. These enzymes can be engineered to respond to a number of external stimuli, including light, pH, and the presence of novel allosteric modulators. Altogether, the ability to engineer and control enzyme structural dynamics can provide new tools for biotechnology and medicine.

Indexed as

EnzymesModels, MolecularProtein ConformationProtein DomainsProtein EngineeringProtein Processing, Post-TranslationalEnzymesallosteryenzyme catalysisexternal stimulusnetworksprotein dynamicsprotein engineeringstimulus-responsive materialstructural dynamics

Identifiers

PMID29380452
PMCPMC5867014

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.