Catalysis by acetylcholinesterase: evidence that the rate-limiting step for acylation with certain substrates precedes general acid-base catalysis.-Reference-Cited by-同舟云学术

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Catalysis by acetylcholinesterase: evidence that the rate-limiting step for acylation with certain substrates precedes general acid-base catalysis.

Published:1975-10-01 Issue:10 Volume:72 Page:3834-3838
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Rosenberry T. L.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Cited by 104 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

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2. Connectivity between surface and interior in catalytic subunits of acetylcholinesterases inferred from their X‐ray structures;Journal of Neurochemistry;2023-03-19

3. Novel activity of human BChE: Lipid hydrolysis;Biochimie;2023-01

4. Mixed bilayers of phosphatidylcholine with dialkylaminostyrylhetarene dyes for AChE-assisted fluorescent sensing of paraoxon;Journal of Molecular Liquids;2022-11

5. Kinetic solvent viscosity effects uncover an internal isomerization of the enzyme-substrate complex in Pseudomonas aeruginosa PAO1 NADH:Quinone oxidoreductase;Archives of Biochemistry and Biophysics;2022-09

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