Výsledky vyhledávání - "Tanesha C. Osborne"

A Chloroacetamidine-Based Inactivator of Protein Arginine Methyltransferase 1: Design, Synthesis, and In Vitro and In Vivo Evaluation

Autor: Justin E. Jones, Paul R. Thompson, Obiamaka Obianyo, Youngho Lee, Corey P. Causey, Michael R. Stallcup, Tanesha C. Osborne

Publikováno v: ChemBioChem. 11:1219-1223

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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4874ac1930a968418f87527b8986ca88
https://doi.org/10.1002/cbic.201000209

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Kinetic Mechanism of Protein Arginine Methyltransferase 1

Autor: Paul R. Thompson, Tanesha C. Osborne, Obiamaka Obianyo

Publikováno v: Biochemistry. 47:10420-10427

Protein arginine methyltransferases (PRMTs) are SAM-dependent enzymes that catalyze the mono- and di-methylation of peptidyl arginine residues. Although all PRMTs produce mono-methyl arginine (MMA), type 1 PRMTs go on to form asymmetrically dimethyla

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::453db0e79acbbae6a21dc0122f9515ff
https://doi.org/10.1021/bi800904m

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

Autor: Scott R Rajski, Tanesha C. Osborne, Rachel L. Weller Roska, Paul R. Thompson

Publikováno v: Journal of the American Chemical Society. 130(14)

Protein arginine methyltransferases (PRMTs) are (S)-adenosylmethionine (SAM)-dependent methyltransferases that catalyze the post-translational methylation of Arg residues in a variety of different proteins involved in transcriptional regulation and R

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e07d8d0a29b32eedc90b5d33980dd687
https://pubmed.ncbi.nlm.nih.gov/18338885

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Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis

Autor: Xing Zhang, Xiaodong Cheng, Paul R. Thompson, Obiamaka Obianyo, Tanesha C. Osborne

Publikováno v: Biochemistry. 46(46)

Protein arginine methyltransferases (PRMTs) are a group of eukaryotic enzymes that catalyze the methylation of Arg residues in a variety of proteins (e.g., histones H3 and H4), and their activities influence a wide range of cellular processes, includ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8366d71621dbeda56657799431a9f49d
https://pubmed.ncbi.nlm.nih.gov/17960915

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