ArticleBiochemistry2019
Inter-Active Site Communication Mediated by the Dimer Interface β-Sheet in the Half-the-Sites Enzyme, Thymidylate Synthase.
Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Carglumic acid and mesalazine as potential anti-mycobacterial agents: a spectroscopic study for repurposing drugs againstMicrobiology spectrum · 2025Article
- An Assessment of Quaternary Structure Functionality in Homomer Protein Complexes.Molecular biology and evolution · 2023Article
- Known allosteric proteins have central roles in genetic disease.PLoS computational biology · 2022Article
- Caught in Action: X-ray Structure of Thymidylate Synthase with Noncovalent Intermediate Analog.Biochemistry · 2021Article
- Weakening of interaction networks with aging in tip-link protein induces hearing loss.The Biochemical journal · 2021Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Thymidylate synthase (TS) is a dimeric enzyme conserved in all life forms that exhibits the allosteric feature of half-the-sites activity. Neither the reason for nor the mechanism of this phenomenon is understood. We used a combined nuclear magnetic resonance (NMR) and molecular dynamics approach to study a stable intermediate preceding hydride transfer, which is the rate-limiting and half-the-sites step. In NMR titrations with ligands leading to this intermediate, we measured chemical shifts of the apoenzyme (lig
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