Correction for “Mechanistic Studies of Fatty Acid Activation by CYP152 Peroxygenases Reveal Unexpected Desaturase Activity”

IF 11.3 1区 化学 Q1 CHEMISTRY, PHYSICAL
Mathias Pickl, Sara Kurakin, Fabián G. Cantú Reinhard, Philipp Schmid, Alexander Pöcheim, Christoph K. Winkler, Wolfgang Kroutil, Sam P. de Visser, Kurt Faber
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引用次数: 0

Abstract

The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acscatal.5c02070. Detailed characterization data for DFV890 ((R)-1) and (R)-21; preclinical pharmacokinetic profiles of CRID3 and (R)-21; preparation of sulfonamide intermediates; summary of coupling and deprotection conditions for the preparation of additional sulfonimidamide NLRP3 antagonists; chiral HPLC conditions for resolution of sulfonimidamide NLRP3 antagonists and characterization data for active enantiomers of sulfonimidamide NLRP3 antagonists discussed in this manuscript; additional information from X-ray crystal structure studies; general procedures for pharmacokinetic studies in preclinical species; cross species PK data for CRID3; in vitro potency, ADME and PK data for (R)-21; additional procedures for preclinical in vitro and in vivo biological studies (PDF) Correction for “Mechanistic Studies of Fatty Acid Activation by CYP152 Peroxygenases Reveal Unexpected Desaturase Activity” 3 views 0 shares 0 downloads Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html. This article has not yet been cited by other publications.
修正了“脂肪酸被CYP152过氧酶激活的机制研究揭示了意想不到的去饱和酶活性”
支持信息可在https://pubs.acs.org/doi/10.1021/acscatal.5c02070免费获取。DFV890 ((R)-1)和(R)-21的详细表征数据;CRID3和(R)-21的临床前药代动力学特征;磺胺中间体的制备;磺胺类NLRP3拮抗剂的偶联和脱保护条件综述本文讨论了磺胺类NLRP3拮抗剂的手性高效液相色谱拆分条件和活性对映体的表征数据;来自x射线晶体结构研究的额外信息;临床前物种药代动力学研究的一般程序;CRID3的跨种PK数据;(R)-21的体外效价、ADME和PK数据;临床前体外和体内生物学研究的附加程序(PDF)“CYP152过氧酶对脂肪酸活化的机制研究揭示了意想不到的去饱和活性”的更正3次观看0次分享0次下载大多数电子支持信息文件无需订阅ACS网络版即可获得。这些文件可以通过文章下载用于研究用途(如果相关文章有公共使用许可链接,该许可可以允许其他用途)。如有其他用途,可通过RightsLink权限系统http://pubs.acs.org/page/copyright/permissions.html向ACS申请。这篇文章尚未被其他出版物引用。
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来源期刊
ACS Catalysis
ACS Catalysis CHEMISTRY, PHYSICAL-
CiteScore
20.80
自引率
6.20%
发文量
1253
审稿时长
1.5 months
期刊介绍: ACS Catalysis is an esteemed journal that publishes original research in the fields of heterogeneous catalysis, molecular catalysis, and biocatalysis. It offers broad coverage across diverse areas such as life sciences, organometallics and synthesis, photochemistry and electrochemistry, drug discovery and synthesis, materials science, environmental protection, polymer discovery and synthesis, and energy and fuels. The scope of the journal is to showcase innovative work in various aspects of catalysis. This includes new reactions and novel synthetic approaches utilizing known catalysts, the discovery or modification of new catalysts, elucidation of catalytic mechanisms through cutting-edge investigations, practical enhancements of existing processes, as well as conceptual advances in the field. Contributions to ACS Catalysis can encompass both experimental and theoretical research focused on catalytic molecules, macromolecules, and materials that exhibit catalytic turnover.
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