(Q27670511)

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Investigation of the Molecular Origins of Protein-arginine Methyltransferase I (PRMT1) Product Specificity Reveals a Role for Two Conserved Methionine Residues

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Investigation of the Molecular Origins of Protein-arginine Methyltransferase I (PRMT1) Product Specificity Reveals a Role for Two Conserved Methionine Residues (English)

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5

object named as

Sean J Johnson

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object named as

Joan M Hevel

6

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author name string

Shanying Gui

1

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Whitney L Wooderchak

2

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Michael P Daly

3

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Paula J Porter

4

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language of work or name

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publication date

19 August 2011

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Journal of Biological Chemistry

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286

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33

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29118-26

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MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

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In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases

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Structural Basis for Substrate Recognition in the Salicylic Acid Carboxyl Methyltransferase Family

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

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Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1

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The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity

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29 September 2017

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Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain

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Asymmetric arginine dimethylation of heterogeneous nuclear ribonucleoprotein K by protein-arginine methyltransferase 1 inhibits its interaction with c-Src

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10.1074/JBC.M111.224097

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