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Tomas Majtan

Researcher at Anschutz Medical Campus

Publications -  66
Citations -  1619

Tomas Majtan is an academic researcher from Anschutz Medical Campus. The author has contributed to research in topics: Cystathionine beta synthase & Homocystinuria. The author has an hindex of 21, co-authored 61 publications receiving 1302 citations. Previous affiliations of Tomas Majtan include Slovak Academy of Sciences & University of Colorado Boulder.

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Identification of Cystathionine β‐Synthase Inhibitors Using a Hydrogen Sulfide Selective Probe

TL;DR: A hydrogen sulfide selective fluorogenic probe, 7-azido-4-methylcoumarin (AzMC), serves as a highly sensitive assay for cystathionine β-synthase activity, and is suitable for the high-throughput discovery of novel enzyme inhibitors.
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Cystathionine-β-Synthase: Molecular Regulation and Pharmacological Inhibition.

TL;DR: Among the small-molecule CBS inhibitors, the review highlights the specificity and selectivity problems related to many of the commonly used “CBS inhibitors” and provides a comprehensive review of their pharmacological actions under physiological conditions and in various disease models.
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Structural basis of regulation and oligomerization of human cystathionine β-synthase, the central enzyme of transsulfuration

TL;DR: The absence of large conformational changes and the crystal structure of the partially activated pathogenic D444N mutant suggest that the rotation of CBS motifs and relaxation of loops delineating the entrance to the catalytic site represent the most likely molecular mechanism of CBS activation by S-adenosyl-l-methionine.
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Structural insight into the molecular mechanism of allosteric activation of human cystathionine β-synthase by S-adenosylmethionine

TL;DR: The crystal structure of an engineered human CBS construct bound to S-adenosylmethionine (AdoMet) reveals the unique binding site of the allosteric activator and the architecture of the human CBS enzyme in its activated conformation, paving the way for the rational design of compounds modulating hCBS activity and thus transsulfuration, redox status, and H2S biogenesis.