ArticleInternational journal of molecular sciences2022
Insights into Domain Organization and Regulatory Mechanism of Cystathionine Beta-Synthase from
Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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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.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Catalytic specificity and crystal structure of cystathionine γ-lyase from Pseudomonas aeruginosa.Scientific reports · 2024Article
- Amino Acid Metabolism and Disease.International journal of molecular sciences · 2023Article
- Structural basis of the inhibition of cystathionine γ-lyase from Toxoplasma gondii by propargylglycine and cysteine.Protein science : a publication of the Protein Society · 2023Article
- Structural Basis for Cyclosporin Isoform-Specific Inhibition of Cyclophilins fromACS infectious diseases · 2023Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Cystathionine beta-synthase (CBS) is a key regulator of homocysteine metabolism. Although eukaryotic CBS have a similar domain architecture with a catalytic core and a C-terminal Bateman module, their regulation varies widely across phyla. In human CBS (HsCBS), the C-terminus has an autoinhibitory effect by acting as a cap that avoids the entry of substrates into the catalytic site. The binding of the allosteric modulator AdoMet to this region alleviates this cap, allowing the protein to progress from a basal toward an activated state. The same activation is obtained by artificial removal or heat-denaturation of the Bateman module. Recently, we reported the crystal structure of CBS from
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Registered trials
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