Structural insights into protein arginine symmetric dimethylation by PRMT5 - Wikidata - thesis-toulmin - TriplyDB

Structural insights into protein arginine symmetric dimethylation by PRMT5

Structural insights into protein arginine symmetric dimethylation by PRMT5

http://www.wikidata.org/entity/Q27675998

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Structural biology and chemistry of protein arginine methyltransferases Cytoplasmic sequestration of FUS/TLS associated with ALS alters histone marks through loss of nuclear protein arginine methyltransferase 1.Crystal structure of the human PRMT5:MEP50 complex Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate Specificity Crystal Structure of Arginine Methyltransferase 6 from Trypanosoma brucei Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats Structural insight into arginine methylation by the mouse protein arginine methyltransferase 7: a zinc finger freezes the mimic of the dimeric state into a single active site A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models Yeast Hmt1 catalyses asymmetric dimethylation of histone H3 arginine 2 in vitro.The PRMT5 arginine methyltransferase: many roles in development, cancer and beyond Structural basis for snRNA recognition by the double-WD40 repeat domain of Gemin5 Theoretical insights into catalytic mechanism of protein arginine methyltransferase 1 Readers of histone methylarginine marks.Compartmentalized nodes control mitotic entry signaling in fission yeast.Interplay between arginine methylation and ubiquitylation regulates KLF4-mediated genome stability and carcinogenesis.Inhibition of cardiomyocyte hypertrophy by protein arginine methyltransferase 5 Selective inhibition of protein arginine methyltransferase 5 blocks initiation and maintenance of B-cell transformation Chemical biology of protein arginine modifications in epigenetic regulation Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues.Diversity and Divergence of Dinoflagellate Histone Proteins.A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase.Protein Arginine Methylation and Citrullination in Epigenetic Regulation Structural basis for Sfm1 functioning as a protein arginine methyltransferase.Recruitment of the NineTeen Complex to the activated spliceosome requires AtPRMT5.Promoter-enhancer looping at the PPARγ2 locus during adipogenic differentiation requires the Prmt5 methyltransferase.Targeting methyltransferase PRMT5 eliminates leukemia stem cells in chronic myelogenous leukemia.Cloning, expression, purification and preliminary X-ray crystallographic analysis of mouse protein arginine methyltransferase 7.A remodeled protein arginine methyltransferase 1 (PRMT1) generates symmetric dimethylarginine.Protein arginine methyltransferases (PRMTs) as therapeutic targets.Protein and nucleic acid methylating enzymes: mechanisms and regulation The promise and failures of epigenetic therapies for cancer treatment Selective small-chemical inhibitors of protein arginine methyltransferase 5 with anti-lung cancer activity.Discovery of selective protein arginine methyltransferase 5 inhibitors and biological evaluations.The story of protein arginine methylation: characterization, regulation, and function.Protein Arginine Methyltransferase Product Specificity Is Mediated by Distinct Active-site Architectures.Structural basis of arginine asymmetrical dimethylation by PRMT6.Functional interplay between protein arginine methyltransferases in Trypanosoma brucei.Epigenetic control via allosteric regulation of mammalian protein arginine methyltransferases.Structure-guided mutational analysis reveals the functional requirements for product specificity of DOT1 enzymes.Targeting protein arginine methyltransferase 5 in disease.

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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Structural insights into protein arginine symmetric dimethylation by PRMT5

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Proceedings of the National Academy of Sciences of the United States of America

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Structural insights into protein arginine symmetric dimethylation by PRMT5

@en

P2093

Litao Sun

http://www.w3.org/2001/XMLSchema#string

Mingzhu Wang

http://www.w3.org/2001/XMLSchema#string

Na Yang

http://www.w3.org/2001/XMLSchema#string

Rui-Ming Xu

http://www.w3.org/2001/XMLSchema#string

Shilai Bao

http://www.w3.org/2001/XMLSchema#string

Weimin Gong

http://www.w3.org/2001/XMLSchema#string

Yingfang Liu

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

The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins

Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes

Crystal structure of the conserved core of protein arginine methyltransferase PRMT3

PHENIX: a comprehensive Python-based system for macromolecular structure solution

A short history of SHELX

Processing of X-ray diffraction data collected in oscillation mode

Caenorhabditis elegans protein arginine methyltransferase PRMT-5 negatively regulates DNA damage-induced apoptosis

The structure and oligomerization of the yeast arginine methyltransferase, Hmt1

Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides

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