Evidence map›Paper›PMID 32270041›Full record

ArticleScience advances2020

A multifunctional surfactant catalyst inspired by hydrolases.

Mitchell D Nothling, Zeyun Xiao, Nicholas S Hill, Mitchell T Blyth, Ayana Bhaskaran, Marc-Antoine Sani, Andrea Espinosa-Gomez, Kevin Ngov, Jonathan White, Tim Buscher and 4 more

Abstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

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  13. Design of supported organocatalysts from a biomass-derived difuran compound and catalytic assessment for lactose hydrolysis.Green chemistry : an international journal and green chemistry resource : GC · 2023
    Article
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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

14 authors.

Mitchell D NothlingDepartment of Chemical and Biomolecular Engineering, The University of Melbourne, Melbourne, VIC 3010, Australia.ORCID 0000-0002-3259-0047
Zeyun XiaoChongqing Institute of Green and Intelligent Technology, Chinese Academy of Sciences, Chongqing 400714, P. R. China.
Nicholas S HillResearch School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.
Mitchell T BlythResearch School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.ORCID 0000-0001-9371-6515
Ayana BhaskaranResearch School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.ORCID 0000-0002-2931-4826
Marc-Antoine SaniSchool of Chemistry, Bio21 Institute, The University of Melbourne, Melbourne, VIC 3010, Australia.ORCID 0000-0003-3284-2176
Andrea Espinosa-GomezDepartment of Chemical and Biomolecular Engineering, The University of Melbourne, Melbourne, VIC 3010, Australia.
Kevin NgovDepartment of Chemical and Biomolecular Engineering, The University of Melbourne, Melbourne, VIC 3010, Australia.ORCID 0000-0002-9395-5476
Jonathan WhiteSchool of Chemistry, Bio21 Institute, The University of Melbourne, Melbourne, VIC 3010, Australia.ORCID 0000-0002-0707-6257
Tim BuscherDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, Santa Barbara, CA 93106, USA.
Frances SeparovicSchool of Chemistry, Bio21 Institute, The University of Melbourne, Melbourne, VIC 3010, Australia.ORCID 0000-0002-6484-2763
Megan L O'MaraResearch School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.ORCID 0000-0002-8764-1585
Michelle L CooteARC Centre of Excellence for Electromaterials Science, Research School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.ORCID 0000-0003-0828-7053
Luke A ConnalResearch School of Chemistry, Australian National University, Canberra, ACT 2601, Australia.ORCID 0000-0001-7519-977X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The remarkable power of enzymes to undertake catalysis frequently stems from their grouping of multiple, complementary chemical units within close proximity around the enzyme active site. Motivated by this, we report here a bioinspired surfactant catalyst that incorporates a variety of chemical functionalities common to hydrolytic enzymes. The textbook hydrolase active site, the catalytic triad, is modeled by positioning the three groups of the triad (-OH, -imidazole, and -CO

Indexed as

Binding SitesCatalysisCatalytic DomainHydrogen BondingHydrolasesHydrolysisHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular ConformationMolecular StructureProtein BindingStructure-Activity RelationshipSurface-Active AgentsHydrolasesSurface-Active Agents

Identifiers

PMID32270041
PMCPMC7112759

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.