Evidence map›Paper›PMID 30530661›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Exploiting correlated molecular-dynamics networks to counteract enzyme activity-stability trade-off.

Haoran Yu, Paul A Dalby

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 118 citations in OpenAlex.

  1. Porcine serum maltase-glucoamylase: structure, kinetics, and inhibition.Journal of enzyme inhibition and medicinal chemistry · 2026
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  16. Computational design of α-amylase fromComputational and structural biotechnology journal · 2024
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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

2 authors at 1 institution in 1 country.

Haoran YuDepartment of Biochemical Engineering, University College London, WC1H 0AH London, United Kingdom.
Paul A DalbyDepartment of Biochemical Engineering, University College London, WC1H 0AH London, United Kingdom p.dalby@ucl.ac.uk.ORCID 0000-0002-0980-8167
University College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The directed evolution of enzymes for improved activity or substrate specificity commonly leads to a trade-off in stability. We have identified an activity-stability trade-off and a loss in unfolding cooperativity for a variant (3M) of

Indexed as

AldehydesCatalytic DomainEnzyme StabilityEscherichia coliEscherichia coli ProteinsKineticsMolecular Dynamics SimulationProtein ConformationProtein EngineeringSubstrate SpecificityTransketolaseAldehydesEscherichia coli ProteinsTransketolasedynamicsprotein engineeringstabilitytrade-offtransketolase

Identifiers

PMID30530661
PMCPMC6310800
OpenAlexW2904326962

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.