ArticleScientific reports2018
Heme interaction of the intrinsically disordered N-terminal peptide segment of human cystathionine-β-synthase.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Heme regulates protein interactions and phosphorylation of BACH2 intrinsically disordered region in humoral response.iScience · 2025Article
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- The coralScience advances · 2022Article
- Regulation of protein function and degradation by heme, heme responsive motifs, and CO.Critical reviews in biochemistry and molecular biology · 2022Review
- Structural Basis for Allostery in PLP-dependent Enzymes.Frontiers in molecular biosciences · 2022Review
- An Analysis of the Multifaceted Roles of Heme in the Pathogenesis of Cancer and Related Diseases.Cancers · 2021Review
- Cysteine metabolic circuitries: druggable targets in cancer.British journal of cancer · 2021Review
- Article
- Review
- Hydrogen Sulfide Metabolism and Signaling in the Tumor Microenvironment.Advances in experimental medicine and biology · 2020Review
- Structural insights into heme binding to IL-36α proinflammatory cytokine.Scientific reports · 2019Article
- Assessing computational predictions of the phenotypic effect of cystathionine-beta-synthase variants.Human mutation · 2019Article
- The molecular basis of transient heme-protein interactions: analysis, concept and implementation.Bioscience reports · 2019Review
- Hydrogen Sulfide Biochemistry and Interplay with Other Gaseous Mediators in Mammalian Physiology.Oxidative medicine and cellular longevity · 2018Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cystathionine-β-synthase (CBS) belongs to a large family of pyridoxal 5'-phosphate (PLP)-dependent enzymes, responsible for the sulfur metabolism. The heme-dependent protein CBS is part of regulatory pathways also involving the gasotransmitter hydrogen sulfide. Malfunction of CBS can lead to pathologic conditions like cancer, cardiovascular and neurodegenerative disorders. Truncation of residues 1-40, absent in X-ray structures of CBS, reduces but does not abolish the activity of the enzyme. Here we report the NMR resonance assignment and heme interaction studies for the N-terminal peptide stretch of CBS. We present NMR-spectral evidence that residues 1-40 constitute an intrinsically disordered region in CBS and interact with heme via a cysteine-proline based motif.
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Registered trials
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.