Evidence map›Paper›PMID 22240119›Full record

ArticleThe Biochemical journal2012

Novel structural arrangement of nematode cystathionine β-synthases: characterization of Caenorhabditis elegans CBS-1.

Roman Vozdek, Aleš Hnízda, Jakub Krijt, Marta Kostrouchová, Viktor Kožich

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. The coralScience advances · 2022
    Article
  4. Structural insight into the unique conformation of cystathionine β-synthase fromComputational and structural biotechnology journal · 2021
    Article
  5. Article
  6. eLife · 2020
    Article
  7. Lifespan and healthspan benefits of exogenous HNPJ aging and mechanisms of disease · 2020
    Article
  8. Article
  9. A timeline of hydrogen sulfide (HBiochemical pharmacology · 2018
    Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Purification, crystallization and preliminary crystallographic analysis of human cystathionine β-synthase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  17. Purification, crystallization and preliminary crystallographic analysis of the full-length cystathionine β-synthase from Apis mellifera.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  18. 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 1 institution in 1 country.

Roman VozdekInstitute of Inherited Metabolic Disorders, Charles University in Prague, First Faculty of Medicine and General University Hospital, Praha, Czech Republic.
Aleš Hnízda
Jakub Krijt
Marta Kostrouchová
Viktor Kožich
Charles University · CZ

Funding

Wellcome Trust 070255/Z/03/Z
6 · The paper itself

Abstract

CBSs (cystathionine β-synthases) are eukaryotic PLP (pyridoxal 5 *-phosphate)-dependent proteins that maintain cellular homocysteine homoeostasis and produce cystathionine and hydrogen sulfide. In the present study, we describe a novel structural arrangement of the CBS enzyme encoded by the cbs-1 gene of the nematode Caenorhabditis elegans. The CBS-1 protein contains a unique tandem repeat of two evolutionarily conserved catalytic regions in a single polypeptide chain. These repeats include a catalytically active C-terminal module containing a PLP-binding site and a less conserved N-terminal module that is unable to bind the PLP cofactor and cannot catalyse CBS reactions, as demonstrated by analysis of truncated variants and active-site mutant proteins. In contrast with other metazoan enzymes, CBS-1 lacks the haem and regulatory Bateman domain essential for activation by AdoMet (S-adenosylmethionine) and only forms monomers. We determined the tissue and subcellular distribution of CBS-1 and showed that cbs-1 knockdown by RNA interference leads to delayed development and to an approximately 10-fold elevation of homocysteine concentrations in nematode extracts. The present study provides the first insight into the metabolism of sulfur amino acids and hydrogen sulfide in C. elegans and shows that nematode CBSs possess a structural feature that is unique among CBS proteins.

Indexed as

Amino Acid SequenceAnimalsBiocatalysisCaenorhabditis elegansConserved SequenceCystathionine beta-SynthaseCytoplasmHomeostasisHomocysteineHumansModels, MolecularMolecular Sequence DataOrgan SpecificityProtein Structure, QuaternaryProtein Structure, TertiarySequence AlignmentCystathionine beta-SynthaseHomocysteine

Identifiers

PMID22240119
PMCPMC3316156
OpenAlexW2065797144

What OpenQuestion holds

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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.