Design, synthesis and biological evaluation of carboxy analogues of arginine methyltransferase inhibitor 1 (AMI-1). (Q43187441)

15 November 2017

Design, synthesis and biological evaluation of carboxy analogues of arginine methyltransferase inhibitor 1 (AMI-1). (English)

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Arginine methyltransferase

15 November 2017

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author

Sabrina Castellano

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Ingo Bauer

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Astrid Spannhoff

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10

object named as

Astrid Spannhoff

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Donghang Cheng

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Mark T Bedford

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Silvia Simeoni

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Gerald Brosch

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PubMed ID

20091730

15 November 2017

language of work or name

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1 March 2010

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398-414

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LDL cholesterol upregulates synthesis of asymmetrical dimethylarginine in human endothelial cells: involvement of S-adenosylmethionine-dependent methyltransferases

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In vivo and in vitro arginine methylation of RNA-binding proteins

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The language of covalent histone modifications

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Chromatin modifications by methylation and ubiquitination: implications in the regulation of gene expression

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Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1. Coactivator-associated arginine methyltransferase

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Arginine methylation an emerging regulator of protein function

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Protein arginine methylation: Cellular functions and methods of analysis

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Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential

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Protein arginine methylation in health and disease

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Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails

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Arginine methylation at a glance

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Protein arginine methyltransferases: from unicellular eukaryotes to humans

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Arginine methylation of scaffold attachment factor A by heterogeneous nuclear ribonucleoprotein particle-associated PRMT1.

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Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities

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Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

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Aberrant expression of CARM1, a transcriptional coactivator of androgen receptor, in the development of prostate carcinoma and androgen-independent status

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Involvement of arginine methyltransferase CARM1 in androgen receptor function and prostate cancer cell viability

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The DDAH/ADMA/NOS pathway

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Cardiovascular biology of the asymmetric dimethylarginine:dimethylarginine dimethylaminohydrolase pathway

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S-nitrosylation of dimethylarginine dimethylaminohydrolase regulates enzyme activity: further interactions between nitric oxide synthase and dimethylarginine dimethylaminohydrolase

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Accumulation of an endogenous inhibitor of nitric oxide synthesis in chronic renal failure

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Disruption of methylarginine metabolism impairs vascular homeostasis

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Expression of nitric oxide related enzymes in coronary heart disease

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The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing.

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PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays

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CARM1 regulates proliferation of PC12 cells by methylating HuD

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Protein arginine methyltransferase 1 coactivates NF-kappaB-dependent gene expression synergistically with CARM1 and PARP1.

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Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains

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Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of Its Binding to Substrate Peptides

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Crystal structure of the conserved core of protein arginine methyltransferase PRMT3

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Kinetic mechanism of protein arginine methyltransferase 1.

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Small molecule regulators of protein arginine methyltransferases

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epigenetic multiple ligands: mixed histone/protein methyltransferase, acetyltransferase, and class III deacetylase (sirtuin) inhibitors.

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Synthesis and biological validation of novel synthetic histone/protein methyltransferase inhibitors

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Pyrazole inhibitors of coactivator associated arginine methyltransferase 1 (CARM1).

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Small molecule inhibitors of histone arginine methyltransferases: homology modeling, molecular docking, binding mode analysis, and biological evaluations

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Target-based approach to inhibitors of histone arginine methyltransferases

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A novel arginine methyltransferase inhibitor with cellular activity

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In situ generation of a bisubstrate analogue for protein arginine methyltransferase 1

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N-Benzyl-1-heteroaryl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamides as inhibitors of co-activator associated arginine methyltransferase 1 (CARM1).

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Virtual screening and biological characterization of novel histone arginine methyltransferase PRMT1 inhibitors

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Benzo[d]imidazole inhibitors of Coactivator Associated Arginine Methyltransferase 1 (CARM1)--Hit to Lead studies.

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Identifiers

DOI

10.1002/CMDC.200900459

1 reference

15 November 2017

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PubMed ID

20091730