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Substrate Specificity And Kinetic Studies Of Pads 1, 3, And 4 Identify Potent And Selective Inhibitors Of Protein Arginine Deiminase 3, Bryan Knuckley, Corey P. Causey, Justin E. Jones, Monica Bhatia, Christina J. Dreyton, Tanesha C. Osborne, Hidenari Takahara, Paul R. Thompson
Substrate Specificity And Kinetic Studies Of Pads 1, 3, And 4 Identify Potent And Selective Inhibitors Of Protein Arginine Deiminase 3, Bryan Knuckley, Corey P. Causey, Justin E. Jones, Monica Bhatia, Christina J. Dreyton, Tanesha C. Osborne, Hidenari Takahara, Paul R. Thompson
Tanesha C. Osborne
Protein citrullination has been shown to regulate numerous physiological pathways (e.g., the innate immune response and gene transcription) and is, when dysregulated, known to be associated with numerous human diseases, including cancer, rheumatoid arthritis, and multiple sclerosis. This modification, also termed deimination, is catalyzed by a group of enzymes called the protein arginine deiminases (PADs). In mammals, there are five PAD family members (i.e., PADs 1, 2, 3, 4, and 6) that exhibit tissue-specific expression patterns and vary in their subcellular localization. The kinetic characterization of PAD4 was recently reported, and these efforts guided the development of the two most …
A Chloroacetamidine-Based Inactivator Of Protein Arginine Methyltransferase 1: Design, Synthesis, And In Vitro And In Vivo Evaluation, Obiamaka Obianyo, Corey P. Causey, Tanesha C. Osborne, Justin E. Jones, Young-Ho Lee, Michael R. Stallcup, Paul R. Thompson
A Chloroacetamidine-Based Inactivator Of Protein Arginine Methyltransferase 1: Design, Synthesis, And In Vitro And In Vivo Evaluation, Obiamaka Obianyo, Corey P. Causey, Tanesha C. Osborne, Justin E. Jones, Young-Ho Lee, Michael R. Stallcup, Paul R. Thompson
Tanesha C. Osborne
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 in vivo. The dysregulation of this enzyme has been implicated in heart disease and cancer; thus, its inhibition would be useful in the treatment of these diseases. Herein, we describe the most potent PRMT1 inhibitor described to date. This compound, denoted C21, is a chloroacetamidine-containing peptide that is able to irreversibly bind and inactivate the enzyme selectively. We have also shown that the coactivator activity of PRMT1 is selectively inhibited …
Kinetic Mechanism Of Protein Arginine Methyltransferase 1, Obiamaka Obianyo, Tanesha C. Osborne, Paul R. Thompson
Kinetic Mechanism Of Protein Arginine Methyltransferase 1, Obiamaka Obianyo, Tanesha C. Osborne, Paul R. Thompson
Tanesha C. Osborne
Protein arginine methyltransferases (PRMTs) are SAM-dependent enzymes that catalyze the mono- and dimethylation of peptidyl arginine residues. Although all PRMTs produce monomethyl arginine (MMA), type 1 PRMTs go on to form asymmetrically dimethylated arginine (ADMA), while type 2 enzymes form symmetrically dimethylated arginine (SDMA). PRMT1 is the major type 1 PRMT in vivo, thus it is the primary producer of the competitive NOS inhibitor, ADMA. Hence, potent inhibitors, which are highly selective for this particular isozyme, could serve as excellent therapeutics for heart disease. However, the design of such inhibitors is impeded by a lack of information regarding this enzyme's …
Alien Crustacean Decapods From The Aegean Coast Of Turkey, M. Baki Yokes, S. Ünsal Karhan, Erdogan Okus, Ahsen Yüksek, Asli Aslan, I. Noyan Yilmaz, Nazli Demirel, Volkan Demir, Bella S. Galil
Alien Crustacean Decapods From The Aegean Coast Of Turkey, M. Baki Yokes, S. Ünsal Karhan, Erdogan Okus, Ahsen Yüksek, Asli Aslan, I. Noyan Yilmaz, Nazli Demirel, Volkan Demir, Bella S. Galil
Asli Aslan
Thirty of the 33 alien decapod crustacean species that have been reported off the Turkish Mediterranean coast are believed to have invaded the region via the Suez Canal, but only three of the species have been recorded along the Turkish Aegean coast. The marine biota of Gökova Bay, Datça Peninsula and Gulf of Fethiye, on the southern Aegean coast of Turkey, was studied by diving between 2002 and 2006. Of the eight Erythrean alien decapod species collected there, five constitute new records for the Aegean Sea and three are newly recorded from the Turkish coast of the Aegean Sea.
Protein Arginine Methyltransferase 1: Positively Charged Residues In Substrate Peptides Distal To The Site Of Methylation Are Important For Substrate Binding And Catalysis, Tanesha C. Osborne, Obiamaka Obianyo, Xing Zhang, Xiadong Cheng, Paul R. Thompson
Protein Arginine Methyltransferase 1: Positively Charged Residues In Substrate Peptides Distal To The Site Of Methylation Are Important For Substrate Binding And Catalysis, Tanesha C. Osborne, Obiamaka Obianyo, Xing Zhang, Xiadong Cheng, Paul R. Thompson
Tanesha C. Osborne
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, including cell growth, RNA splicing, differentiation, and transcriptional regulation. Dysregulation of these enzymes has been linked to heart disease and cancer, suggesting this enzyme family as a novel therapeutic target. To aid the development of PRMT inhibitors, we characterized the substrate specificity of both the rat and human PRMT1 orthologues using histone based peptide substrates. N- and C-terminal truncations to identify a minimal …