Evidence map›Paper›PMID 27573242›Full record

ArticleThe Journal of biological chemistry2016

Structural and Functional Studies of Pavine N-Methyltransferase from Thalictrum flavum Reveal Novel Insights into Substrate Recognition and Catalytic Mechanism.

Miguel A Torres, Elesha Hoffarth, Luiz Eugenio, Julia Savtchouk, Xue Chen, Jeremy S Morris, Peter J Facchini, Kenneth K-S Ng

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Methyltransferases: Functions and Applications.Chembiochem : a European journal of chemical biology · 2022
    Review
  11. Article
  12. Tetrahydroisoquinoline N-methyltransferase fromMolecules (Basel, Switzerland) · 2022
    Article
  13. Article
  14. Structure-function studies of tetrahydroprotoberberineThe Journal of biological chemistry · 2019
    Article
  15. Review
  16. AnThe Journal of biological chemistry · 2018
    Article
  17. Structure and Biocatalytic Scope of Coclaurine N-Methyltransferase.Angewandte Chemie (International ed. in English) · 2018
    Article
  18. Article
  19. 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

8 authors at 2 institutions in 1 country.

Miguel A TorresFrom the Department of Biological Sciences and.
Elesha HoffarthFrom the Department of Biological Sciences and.
Luiz EugenioFrom the Department of Biological Sciences and.
Julia SavtchoukFrom the Department of Biological Sciences and.
Xue ChenFrom the Department of Biological Sciences and.
Jeremy S MorrisFrom the Department of Biological Sciences and.
Peter J FacchiniFrom the Department of Biological Sciences and.
Kenneth K-S NgFrom the Department of Biological Sciences and ngk@ucalgary.ca.
Alberta Glycomics Centre · CAUniversity of Calgary · CA

Funding

ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
NCRR NIH HHS P41 RR001209NIGMS NIH HHS P41 GM103393
6 · The paper itself

Abstract

Benzylisoquinoline alkaloids (BIAs) are produced in a wide variety of plants and include many common analgesic, antitussive, and anticancer compounds. Several members of a distinct family of S-adenosylmethionine (SAM)-dependent N-methyltransferases (NMTs) play critical roles in BIA biosynthesis, but the molecular basis of substrate recognition and catalysis is not known for NMTs involved in BIA metabolism. To address this issue, the crystal structure of pavine NMT from Thalictrum flavum was solved using selenomethionine-substituted protein (d

Indexed as

BenzylisoquinolinesBinding SitesCatalytic DomainCrystallography, X-RayIsoquinolinesMethyltransferasesModels, MolecularProtein ConformationS-AdenosylhomocysteineSubstrate SpecificityThalictrumBenzylisoquinolinesIsoquinolineslaudanosineMethyltransferasesreticulineS-AdenosylhomocysteinetetrahydropapaverineBenzylisoquinoline alkaloid biosynthesisenzyme kineticsenzyme mechanismprotein structuresecondary metabolismx-ray crystallography

Identifiers

PMID27573242
PMCPMC5095397
OpenAlexW2517653083

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.