Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.

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The story of protein arginine methylation: characterization, regulation, and function.The Role of Electron Transfer Dissociation in Modern Proteomics.

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P2860

Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.

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http://www.wikidata.org/entity/Q38454812

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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name

Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.

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type

Item

label

Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.

@en

prefLabel

Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.

@en

P1476

Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.

@en

P2093

Hogune Im

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

Marc R Wilkins

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

Melissa A Erce

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

Michael P Snyder

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

P2860

Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications

Gene ontology: tool for the unification of biology

Phospho-tyrosine dependent protein-protein interaction network

Arginine methylation of RNA helicase a determines its subcellular localization

The arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1.

IsoBase: a database of functionally related proteins across PPI networks

Global analysis of protein localization in budding yeast.

A novel methyltransferase (Hmt1p) modifies poly(A)+-RNA-binding proteins.

A conditional two-hybrid (C2H) system for the detection of protein-protein interactions that are mediated by post-translational modification.

Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists

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465-476

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scholarly article

P356

10.1002/PMIC.201400564

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

P478

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

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Gene Hart-Smith

Jason K K Low

P577

2015-11-17T00:00:00Z

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P698

26572822

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Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.

about

P2860

P2860

Protein substrates of the arginine methyltransferase Hmt1 identified by proteome arrays.

description

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type

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P1433

P1476

P2093

P2860

P304

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P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

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P31

P356

P433

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P50

P577

P698