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Peptidylarginine deiminases

Figure 2.9 Overall structure of Peptidylarginine deiminase 4 (PAD4). Figure 2.9 Overall structure of Peptidylarginine deiminase 4 (PAD4).
Structural basis for histone N-terminal recognition by human peptidylarginine deiminase 4. Proceedings of the National Academy of Sciences of the United States of America, 103 (14), 5291-5296. [Pg.55]

Tarcsa, E., Marekov, L. N., Mei, G., Melino, G., Lee, S. C., and Steinert, P. M. (1996). Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin./. Biol. Chem. 271, 30709-30716. [Pg.200]

Stone EM, Schaller TH, Bianchi H et al (2005) Inactivation of two diverse enzymes in the amidinotransferase superfamily by 2-chloroacetamidine dimethylargininase and peptidylarginine deiminase. Biochemistry 44 13744—13752... [Pg.40]

Raijmakers R, et al. Methylation of arginine residues interferes with citrullination by peptidylarginine deiminases in vitro. J. Mol. [Pg.1578]

Figure 17 Peptidylarginine deiminase catalyzes the posttranslational modification of peptidylarginine to peptidylcitrulline (26). The filled circles represent labeling. Figure 17 Peptidylarginine deiminase catalyzes the posttranslational modification of peptidylarginine to peptidylcitrulline (26). The filled circles represent labeling.
Choi M, Lee OH, Jeon S, Park M, Lee DR, Ko JJ, Yoon TK, Rajkovic A, Choi Y. 2010. The oocyte-specific transcription factor. Nobox, regulates the expression of Pad6, a peptidylarginine deiminase in the oocyte. FEES Lett 584(16) 3629-3634. [Pg.530]

Esposito G, Vitale AM, Leijten FP, Strik AM, Koonen-Reemst AM, Yurttas P, Robben TJ, Coonrod S, Gossen JA. 2007. Peptidylarginine deiminase (PAD) 6 is essential for oocyte cytoskeletal sheet formation and female fertility. Mol Cell Endocrinol 273(1-2) 25-31. [Pg.532]

Wright PW, Bolling LC, Calvert ME, Sarmento OF, Berkeley EV, Shea MC, Hao Z, Jayes FC, Bush LA, Shetty J, Shore AN, Reddi PP, Tung KS, Sarny E, Allietta MM, Sherman NE, Herr JC, Coonrod SA 2003. ePAD, an oocyte and early embryo-abundant peptidylarginine deiminase-like protein that localizes to egg cytoplasmic sheets. Dev Biol 256(l) 73-88. [Pg.553]

Citrullination Also known as deimination, citrullination is the term used for the posttranslational modification of the amino acid arginine in a protein into the amino acid citrulline. This reaction, shown below, is performed by enzymes called peptidylarginine deiminases (PADs). [Pg.760]


See other pages where Peptidylarginine deiminases is mentioned: [Pg.221]    [Pg.17]    [Pg.40]    [Pg.314]    [Pg.357]    [Pg.125]    [Pg.128]    [Pg.139]    [Pg.564]    [Pg.513]    [Pg.514]    [Pg.526]    [Pg.760]    [Pg.361]    [Pg.363]   


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Peptidylarginine deiminases PADs)

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