Isothermal Titration Calorimetry Analysis of a Cooperative Riboswitch Using an Interdependent-Sites Binding Model
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Publisher
Springer US
Link
https://link.springer.com/content/pdf/10.1007/978-1-0716-2687-0_5
Reference37 articles.
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3. Schroeder GM, Dutta D, Cavender CE, Jenkins JL, Pritchett EM, Baker CD, Ashton JM, Mathews DH, Wedekind JE (2020) Analysis of a preQ1-I riboswitch in effector-free and bound states reveals a metabolite-programmed nucleobase-stacking spine that controls gene regulation. Nucleic Acids Res 48(14):1846–1864
4. Chen H, Egger M, Xu X, Flemmich L, Krasheninina O, Sun A, Micura R, Ren A (2020) Structural distinctions between NAD+ riboswitch domains 1 and 2 determine differential folding and ligand binding. Nucleic Acids Res 48(21):12394–12406
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Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Full-Length NAD+-I Riboswitches Bind a Single Cofactor but Cannot Discriminate against Adenosine Triphosphate;Biochemistry;2023-11-10
2. A riboswitch separated from its ribosome-binding site still regulates translation;Nucleic Acids Research;2023-02-10
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