Evidence map›Paper›PMID 31894608›Full record

ArticleAngewandte Chemie (International ed. in English)2020

Oxalyl-CoA Decarboxylase Enables Nucleophilic One-Carbon Extension of Aldehydes to Chiral α-Hydroxy Acids.

Simon Burgener, Niña Socorro Cortina, Tobias J Erb

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Enzymatic Conversion of COChemical reviews · 2023
    Review
  10. Article
  11. Review
  12. Article
  13. Enzyme engineering andSynthetic biology (Oxford, England) · 2021
    Article
  14. Article
  15. 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 at 2 institutions in 1 country.

Simon BurgenerDepartment of Biochemistry & Synthetic Metabolism, Max-Planck-Institute for terrestrial Microbiology, Karl-von-Frisch-Str. 10, 35043, Marburg, Germany.ORCID 0000-0003-3703-168X
Niña Socorro CortinaDepartment of Biochemistry & Synthetic Metabolism, Max-Planck-Institute for terrestrial Microbiology, Karl-von-Frisch-Str. 10, 35043, Marburg, Germany.ORCID 0000-0002-0930-660X
Tobias J ErbDepartment of Biochemistry & Synthetic Metabolism, Max-Planck-Institute for terrestrial Microbiology, Karl-von-Frisch-Str. 10, 35043, Marburg, Germany.ORCID 0000-0003-3685-0894
Max Planck Institute for Terrestrial Microbiology · DELoewe Center for Synthetic Microbiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The synthesis of complex molecules from simple, renewable carbon units is the goal of a sustainable economy. Here we explored the biocatalytic potential of the thiamine-diphosphate-dependent (ThDP) oxalyl-CoA decarboxylase (OXC)/2-hydroxyacyl-CoA lyase (HACL) superfamily that naturally catalyzes the shortening of acyl-CoA thioester substrates through the release of the C

Indexed as

AldehydesBiocatalysisCarboxy-LyasesHumansHydroxy AcidsKineticsMethylobacteriaceaeMutagenesis, Site-DirectedRecombinant ProteinsStereoisomerismSubstrate SpecificityThiamine PyrophosphateAldehydesCarboxy-LyasesHydroxy Acidsoxalyl CoA decarboxylaseRecombinant ProteinsThiamine PyrophosphatebiocatalysisC1 building blocksC−C couplingoxalyl-CoA decarboxylasethiamine diphosphate

Identifiers

PMID31894608
PMCPMC7154664
OpenAlexW2998308014

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.