Evidence map›Paper›PMID 30036448›Full record

ArticleBiotechnology and bioengineering2018

A tailor-made, self-sufficient and recyclable monooxygenase catalyst based on coimmobilized cytochrome P450 BM3 and glucose dehydrogenase.

Donya Valikhani, Juan M Bolivar, Alexander Dennig, Bernd Nidetzky

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biotechnology and bioengineering, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

5 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. 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

4 authors at 1 institution in 1 country.

Donya ValikhaniInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, Graz, Austria.
Juan M BolivarInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, Graz, Austria.
Alexander DennigInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, Graz, Austria.
Bernd NidetzkyInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, Graz, Austria.ORCID 0000-0002-5030-2643
Graz University of Technology · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cytochrome P450 monooxygenases (P450s) promote hydroxylations in a broad variety of substrates. Their prowess in C-H bond functionalization renders P450s promising catalysts for organic synthesis. However, operating P450 reactions involve complex management of the main substrates, O

Indexed as

BiocatalysisBacillus megateriumBacterial ProteinsCytochrome P-450 Enzyme SystemEnzymes, ImmobilizedGlucose 1-DehydrogenaseNADPNADPH-Ferrihemoprotein ReductaseOxidation-ReductionBacterial ProteinsCytochrome P-450 Enzyme SystemEnzymes, Immobilizedflavocytochrome P450 BM3 monoxygenasesGlucose 1-DehydrogenaseNADPNADPH-Ferrihemoprotein Reductasecytochrome P450fatty acidsglucose dehydrogenaseheterogeneous biocatalysisimmobilization

Identifiers

PMID30036448
PMCPMC6836874
OpenAlexW2883466567

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.