PTEN catalysis of phospholipid dephosphorylation reaction follows a two-step mechanism in which the conserved aspartate-92 does not function as the general acid — Mechanistic analysis of a familial Cowden disease-associated PTEN mutation
Author:
Publisher
Elsevier BV
Subject
Cell Biology
Cited by 28 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. Classification of PTEN missense VUS through exascale simulations;Briefings in Bioinformatics;2023-09-22
2. Comparative Protein Structural Network Analysis Reveals C-Terminal Tail Phosphorylation Structural Communication Fingerprint in PTEN-Associated Mutations in Autism and Cancer;The Journal of Physical Chemistry B;2023-01-10
3. Structural and Dynamic Effects of PTEN C-Terminal Tail Phosphorylation;Journal of Chemical Information and Modeling;2022-08-24
4. A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop;Nature Communications;2022-04-25
5. Genetic analysis of daf-18/PTEN missense mutants for starvation resistance and developmental regulation during Caenorhabditis elegans L1 arrest;G3 Genes|Genomes|Genetics;2022-04-22
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