Evidence map›Paper›PMID 29629557›Full record

ArticleMolecules and cells2018

Structural Basis for Recognition of L-lysine, L-ornithine, and L-2,4-diamino Butyric Acid by Lysine Cyclodeaminase.

Kyungjin Min, Hye-Jin Yoon, Atsushi Matsuura, Yong Hwan Kim, Hyung Ho Lee

Open access · greenAbstract read
In one paragraph

Article in Molecules and cells, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 50% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Optimization of the precursor supply for an enhanced FK506 production inFrontiers in bioengineering and biotechnology · 2022
    Article
  4. 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

5 authors at 2 institutions in 1 country.

Kyungjin MinDepartment of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Korea.
Hye-Jin YoonDepartment of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Korea.
Atsushi MatsuuraDepartment of Pharmacy, Dongguk University, Goyang 10326, Korea.
Yong Hwan KimSchool of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Korea.
Hyung Ho LeeDepartment of Chemistry, College of Natural Sciences, Seoul National University, Seoul 08826, Korea.
Seoul National University · KRUlsan National Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

L-pipecolic acid is a non-protein amino acid commonly found in plants, animals, and microorganisms. It is a well-known precursor to numerous microbial secondary metabolites and pharmaceuticals, including anticancer agents, immunosuppressants, and several antibiotics. Lysine cyclodeaminase (LCD) catalyzes β-deamination of L-lysine into L-pipecolic acid using β-nicotinamide adenine dinucleotide as a cofactor. Expression of a human homolog of LCD, μ-crystallin, is elevated in prostate cancer patients. To understand the structural features and catalytic mechanisms of LCD, we determined the crystal structures of

Indexed as

Ammonia-LyasesButyric AcidHumansLysineModels, MolecularOrnithineProtein BindingAmmonia-LyasesButyric AcidLysinelysine cyclodeaminaseOrnithinecrystal structureL-lysine cyclodeaminaseStreptomyces pristinaespiralis

Identifiers

PMID29629557
PMCPMC5935100
OpenAlexW2800784941

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.