Evidence map›Paper›PMID 36883335›Full record

ArticleProtein science : a publication of the Protein Society2023

Structural basis of the inhibition of cystathionine γ-lyase from Toxoplasma gondii by propargylglycine and cysteine.

Carmen Fernández-Rodríguez, Carolina Conter, Iker Oyenarte, Filippo Favretto, Iban Quintana, Maria Luz Martinez-Chantar, Alessandra Astegno, Luis Alfonso Martínez-Cruz

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

7 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Sulfide regulation and catabolism in health and disease.Signal transduction and targeted therapy · 2025
    Review
  5. Article
  6. Article
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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 3 institutions in 2 countries.

Carmen Fernández-RodríguezCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Spain.
Carolina ConterDepartment of Biotechnology, University of Verona, Verona, Italy.ORCID 0000-0002-5999-8667
Iker OyenarteCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Spain.
Filippo FavrettoDepartment of Biotechnology, University of Verona, Verona, Italy.
Iban QuintanaTEKNIKER, Basque Research and Technology Alliance (BRTA), Eibar, Gipuzkoa, Spain.
Maria Luz Martinez-ChantarCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Spain.
Alessandra AstegnoDepartment of Biotechnology, University of Verona, Verona, Italy.ORCID 0000-0002-7341-0970
Luis Alfonso Martínez-CruzCenter for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Derio, Spain.ORCID 0000-0002-5856-9377
CIC bioGUNE · ESUniversity of Verona · ITTekniker · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cystathionine γ-lyase (CGL) is a PLP-dependent enzyme that catalyzes the last step of the reverse transsulfuration route for endogenous cysteine biosynthesis. The canonical CGL-catalyzed process consists of an α,γ-elimination reaction that breaks down cystathionine into cysteine, α-ketobutyrate, and ammonia. In some species, the enzyme can alternatively use cysteine as a substrate, resulting in the production of hydrogen sulfide (H

Indexed as

Cystathionine gamma-LyaseToxoplasmaAlkynesCystathionineCysteineGlycineHumansAlkynesCystathionineCystathionine gamma-LyaseCysteineGlycinepropargylglycinecrystal structurecystathionine γ-lyasecysteineinhibitorpropargylglycinepyridoxal-5′-phosphatereverse transsulfurationToxoplasma gondii

Identifiers

PMID36883335
PMCPMC10053738
OpenAlexW4323533287

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.