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For: Mahmoodi N, Harijan RK, Schramm VL. Transition-State Analogues of Phenylethanolamine N-Methyltransferase. J Am Chem Soc 2020;142:14222-33. [PMID: 32702980 DOI: 10.1021/jacs.0c05446] [Cited by in Crossref: 3] [Cited by in F6Publishing: 2] [Article Influence: 1.5] [Reference Citation Analysis]
Number Citing Articles
1 Ahmed‐belkacem R, Debart F, Vasseur J. Bisubstrate Strategies to Target Methyltransferases. European J Organic Chem. [DOI: 10.1002/ejoc.202101481] [Reference Citation Analysis]
2 Lu J, Bart AG, Wu Q, Criscione KR, McLeish MJ, Scott EE, Grunewald GL. Structure-Based Drug Design of Bisubstrate Inhibitors of Phenylethanolamine N-Methyltransferase Possessing Low Nanomolar Affinity at Both Substrate Binding Domains1. J Med Chem 2020;63:13878-98. [PMID: 33147410 DOI: 10.1021/acs.jmedchem.0c01475] [Reference Citation Analysis]
3 Zhou Y, Liang Z, Jin Y, Ding J, Huang T, Moore JH, Zheng Z, Huang J. Shared Genetic Architecture and Causal Relationship Between Asthma and Cardiovascular Diseases: A Large-Scale Cross-Trait Analysis. Front Genet 2022;12:775591. [DOI: 10.3389/fgene.2021.775591] [Reference Citation Analysis]
4 Lewis CA Jr, Wolfenden R. The Burden Borne by Protein Methyltransferases: Rates and Equilibria of Non-enzymatic Methylation of Amino Acid Side Chains by SAM in Water. Biochemistry 2021;60:854-8. [PMID: 33667085 DOI: 10.1021/acs.biochem.1c00028] [Cited by in F6Publishing: 1] [Reference Citation Analysis]