A chloroacetamidine-based inactivator of protein arginine methyltransferase 1: Design, synthesis, and in vitro and in vivo evaluation

Obiamaka Obianyo; Corey P. Causey; Tanesha C. Osborne; Justin E. Jones; Young-Ho Lee; Michael R. Stallcup; Paul R. Thompson

doi:10.1002/cbic.201000209

A chloroacetamidine-based inactivator of protein arginine methyltransferase 1: Design, synthesis, and in vitro and in vivo evaluation

Obiamaka Obianyo
, Corey P. Causey
, Tanesha C. Osborne
, Justin E. Jones
, Young-Ho Lee
, Michael R. Stallcup
, Paul R. Thompson

Biochemistry, Chemistry & Physics

University of South Carolina

Research output: Contribution to journal › Article › peer-review

41 Scopus citations

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Abstract

(Chemical Equation Presented) Protein arginine methyltransferases (PRMTs) catalyze the post-translational methylation of arginine residues. PRMT1 is the predominant mammalian isozyme and is responsible for generating the majority of the asymmetrically dimethylated arginine found in vivo. Herein, we describe the most potent PRMT1 inhibitor, C21, described to date.

Original language	English
Pages (from-to)	1219-1223
Number of pages	5
Journal	ChemBioChem
Volume	11
Issue number	9
DOIs	https://doi.org/10.1002/cbic.201000209
State	Published - Jun 14 2010

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Scopus Subject Areas

Biochemistry
Molecular Medicine
Molecular Biology
Organic Chemistry

Keywords

Cl-amidine
Enzymes
Inhibitors
Protein arginine methyltransferase
Transcription

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10.1002/cbic.201000209

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title = "A chloroacetamidine-based inactivator of protein arginine methyltransferase 1: Design, synthesis, and in vitro and in vivo evaluation",

abstract = "(Chemical Equation Presented) Protein arginine methyltransferases (PRMTs) catalyze the post-translational methylation of arginine residues. PRMT1 is the predominant mammalian isozyme and is responsible for generating the majority of the asymmetrically dimethylated arginine found in vivo. Herein, we describe the most potent PRMT1 inhibitor, C21, described to date.",

keywords = "Cl-amidine, Enzymes, Inhibitors, Protein arginine methyltransferase, Transcription",

author = "Obiamaka Obianyo and Causey, \{Corey P.\} and Osborne, \{Tanesha C.\} and Jones, \{Justin E.\} and Young-Ho Lee and Stallcup, \{Michael R.\} and Thompson, \{Paul R.\}",

note = "Obiamaka Obianyo, Corey P. Causey, Tanesha C. Osborne, Justin E. Jones, Young-Ho Lee, Michael R. Stallcup, and Paul R. Thompson. {"}A Chloroacetamidine-based Inactivator of Protein Arginine Methyltransferase 1: Design, Synthesis, and in Vitro and in Vivo Evaluation{"} ChemBioChem 11.9 (2010): 1219-1223. doi:10.1002/cbic.201000209 source:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3060404/ Available at: http://works.bepress.com/tanesha\_osborne/3",

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doi = "10.1002/cbic.201000209",

language = "English",

volume = "11",

pages = "1219--1223",

journal = "ChemBioChem",

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}

TY - JOUR

T1 - A chloroacetamidine-based inactivator of protein arginine methyltransferase 1

T2 - Design, synthesis, and in vitro and in vivo evaluation

AU - Obianyo, Obiamaka

AU - Causey, Corey P.

AU - Osborne, Tanesha C.

AU - Jones, Justin E.

AU - Lee, Young-Ho

AU - Stallcup, Michael R.

AU - Thompson, Paul R.

N1 - Obiamaka Obianyo, Corey P. Causey, Tanesha C. Osborne, Justin E. Jones, Young-Ho Lee, Michael R. Stallcup, and Paul R. Thompson. "A Chloroacetamidine-based Inactivator of Protein Arginine Methyltransferase 1: Design, Synthesis, and in Vitro and in Vivo Evaluation" ChemBioChem 11.9 (2010): 1219-1223. doi:10.1002/cbic.201000209 source:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3060404/ Available at: http://works.bepress.com/tanesha_osborne/3

PY - 2010/6/14

Y1 - 2010/6/14

N2 - (Chemical Equation Presented) Protein arginine methyltransferases (PRMTs) catalyze the post-translational methylation of arginine residues. PRMT1 is the predominant mammalian isozyme and is responsible for generating the majority of the asymmetrically dimethylated arginine found in vivo. Herein, we describe the most potent PRMT1 inhibitor, C21, described to date.

AB - (Chemical Equation Presented) Protein arginine methyltransferases (PRMTs) catalyze the post-translational methylation of arginine residues. PRMT1 is the predominant mammalian isozyme and is responsible for generating the majority of the asymmetrically dimethylated arginine found in vivo. Herein, we describe the most potent PRMT1 inhibitor, C21, described to date.

KW - Cl-amidine

KW - Enzymes

KW - Inhibitors

KW - Protein arginine methyltransferase

KW - Transcription

UR - https://www.scopus.com/pages/publications/77953372136

U2 - 10.1002/cbic.201000209

DO - 10.1002/cbic.201000209

M3 - Article

SN - 1439-4227

VL - 11

SP - 1219

EP - 1223

JO - ChemBioChem

JF - ChemBioChem

IS - 9

ER -

A chloroacetamidine-based inactivator of protein arginine methyltransferase 1: Design, synthesis, and in vitro and in vivo evaluation

Abstract

UN SDGs

Scopus Subject Areas

Keywords

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