Evidence map›Paper›PMID 28127810›Full record

ArticleProtein science : a publication of the Protein Society2017

Crystallographic and mutational analyses of cystathionine β-synthase in the H

Yasuyuki Matoba, Tomoki Yoshida, Hisae Izuhara-Kihara, Masafumi Noda, Masanori Sugiyama

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. pH-dependent regulation of an acidophilicApplied and environmental microbiology · 2024
    Article
  3. Article
  4. Article
  5. Role of Hydrogen Sulfide in Oral Disease.Oxidative medicine and cellular longevity · 2022
    Review
  6. Review
  7. Structural insight into the unique conformation of cystathionine β-synthase fromComputational and structural biotechnology journal · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. A timeline of hydrogen sulfide (HBiochemical pharmacology · 2018
    Review
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.

Yasuyuki MatobaGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Tomoki YoshidaGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Hisae Izuhara-KiharaGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Masafumi NodaGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Masanori SugiyamaGraduate School of Biomedical and Health Sciences, Hiroshima University, Kasumi 1-2-3, Minami-ku, Hiroshima, 734-8551, Japan.
Hiroshima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cystathionine β-synthase (CBS) catalyzes the formation of l-cystathionine from l-serine and l-homocysteine. The resulting l-cystathionine is decomposed into l-cysteine, ammonia, and α-ketobutylic acid by cystathionine γ-lyase (CGL). This reverse transsulfuration pathway, which is catalyzed by both enzymes, mainly occurs in eukaryotic cells. The eukaryotic CBS and CGL have recently been recognized as major physiological enzymes for the generation of hydrogen sulfide (H

Indexed as

Bacterial ProteinsCystathionine beta-SynthaseLactiplantibacillus plantarumMultigene FamilyMutation, MissenseAmino Acid SubstitutionBinding SitesCrystallography, X-RayCystathionineHydrogen SulfideHydrolasesBacterial ProteinsCystathionineCystathionine beta-SynthasehomocysteinaseHydrogen SulfideHydrolasesamino acidcrystal structurecystathionine β-synthasehydrogen sulfideLactobacillus plantarum

Identifiers

PMID28127810
PMCPMC5368070
OpenAlexW2582812841

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.