Evidence map›Paper›PMID 36385923›Full record

ArticleACS medicinal chemistry letters2022

Binding versus Enzymatic Processing of ε-Trimethyllysine Dioxygenase Substrate Analogues.

Diana Zelencova-Gopejenko, Aiga Grandane, Einars Loza, Daina Lola, Anda Sipola, Edgars Liepinsh, Pavel Arsenyan, Kristaps Jaudzems

Open access · greenAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 90% 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

2 citing papers in PubMed, 0 citations in OpenAlex.

  1. A Revised Model for Muscarine Biosynthesis Involving Lysine Trimethylation.Angewandte Chemie (International ed. in English) · 2026
    Article
  2. 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 1 institution in 1 country.

Diana Zelencova-GopejenkoLatvian Institute of Organic Synthesis, Aizkraukles 21, Riga LV-1006, Latvia.ORCID https://orcid.org/0000-0002-6931-2294
Aiga GrandaneLatvian Institute of Organic Synthesis, Aizkraukles 21, Riga LV-1006, Latvia.
Einars LozaLatvian Institute of Organic Synthesis, Aizkraukles 21, Riga LV-1006, Latvia.
Daina LolaLatvian Institute of Organic Synthesis, Aizkraukles 21, Riga LV-1006, Latvia.
Anda SipolaLatvian Institute of Organic Synthesis, Aizkraukles 21, Riga LV-1006, Latvia.
Edgars LiepinshLatvian Institute of Organic Synthesis, Aizkraukles 21, Riga LV-1006, Latvia.
Pavel ArsenyanLatvian Institute of Organic Synthesis, Aizkraukles 21, Riga LV-1006, Latvia.ORCID https://orcid.org/0000-0001-5875-2799
Kristaps JaudzemsLatvian Institute of Organic Synthesis, Aizkraukles 21, Riga LV-1006, Latvia.ORCID https://orcid.org/0000-0003-3922-2447
Latvijas Organiskās Sintēzes Institūts · LV

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ε-Trimethyllysine dioxygenase (TMLD) is a non-heme Fe(II) and α-ketoglutarate dependent oxygenase that catalyzes the stereospecific hydroxylation of ε-trimethyl-

Identifiers

PMID36385923
PMCPMC9661700
OpenAlexW4307030307

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.