ArticleThe journal of physical chemistry. B2022
Comparison of the Role of Protein Dynamics in Catalysis by Dihydrofolate Reductase from
Article in The journal of physical chemistry. B, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
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.
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Who cites it
3 citing papers in PubMed, 9 citations in OpenAlex.
- Interplay of structural preorganization and conformational sampling in UDP-glucuronic acid 4-epimerase catalysis.Nature communications · 2024Article
- Chemical profiling of volatile compounds of the essential oil of grey-leaved rockrose (Frontiers in chemistry · 2024Article
- Protein Dynamics and Enzymatic Catalysis.The journal of physical chemistry. B · 2023Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Dihydrofolate reductase (DHFR) is a well-studied, clinically relevant enzyme known for being highly dynamic over the course of its catalytic cycle. However, the role dynamic motions play in the explicit hydride transfer from the nicotinamide cofactor to the dihydrofolate substrate remains unclear because reaction initiation and direct spectroscopic examination on the appropriate time scale for such femtosecond to picosecond motions is challenging. Here, we employ pre-steady-state kinetics to observe the hydride transfer as directly as possible in two different species of DHFR:
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Registered trials
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