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Poly ation

Researchers found that NAD serves as a substrate in poly(ADP-ribose) synthesis, a reaction important for DNA repair processes. In addition, it takes part in mono (ADP-ribosyl)ation reactions that are involved in endogenous regulation of many aspects of signal transduction and membrane trafficking in eukaryotic cells. [Pg.851]

McLaren J, Boulikas T, Vamvakas S. 1994. Induction of poly(ADP-ribosyl)ation in the kidney after in vivo application of renal carcinogens. T oxicology 88 101-112. [Pg.278]

Our objective In this paper is to illustrate the methods for functionalizing poly(arylene ether sulfone). Particular attention will be paid to bromination, nitration, aminatlon, chloromethyl-ation, and aminomethylatlon of 1 and its corresponding model compound. [Pg.8]

Philippova and Starodubtzev have also extensively studied the complex-ation behavior of polyacids and PEG, especially, the system of crosslinked of poly(methacrylic acid) and linear poly(ethylene glycol) (Philippova and Starodubtzev, 1995 Philippova et al., 1994). They observed that decreasing the molecular weight of PEG from 6000 to 1500 resulted in its slower diffusion into the swollen network of PMAA, and a drastic decrease in both the stability and equilibrium composition of the intermacromolecular complex. Analysis of dried polymer networks of PMAA with absorbed PEG chains by FT-IR spectroscopy revealed the presence of two types of hydrogen bonded structures (1) dimers of methacrylic acid at absorption frequency of 1700 cm-1 and (2) interpolymer complexes of PMAA and PEG at 1733 cm-1. In addition, they also suggested as a result of their studies, that the hydrogen bonded dimer of PMAA forms preferentially to the intermacromolecular complex between the PMAA network and PEG chains. [Pg.94]

BRCT BRCAl C-terminus-like DBD DNA-binding domain dPARP Drosophila PARP MPTP l-methyl-4-phenyl-l,2,3,6-tetrahydropyridine NAD+ Nicotinamide adenine dinucleotide NAm Nicotinamide NLS Nuclear locahzation signal OAADPR O-acetyl-ADP-ribose PAR Poly(ADP-ribose) PARG Poly(ADP-ribose) glycohydrolase PARP Poly(ADP-ribose) polymerase PARylation poly(ADP-ribosyl)ation... [Pg.45]

Beneke S, Diefenbach J, Burkle A (2004) Poly(ADP-ribosyl)ation inhibitors promising drug candidates for a wide variety of pathophysiologic conditions. Int J Cancer 111 813-818... [Pg.64]

Burkle A (2001) Physiology and pathophysiology of poly(ADP-ribosyl)ation. Bioessays 23 795-806... [Pg.64]

Curtin NJ (2006) PARP inhibitors and cancer therapy. In Biirlde A (ed) Poly(ADP-Ribosyl)ation. Landes Bioscience, Georgetown, pp218—233... [Pg.65]

Thus, the poly(ADP-ribosyl)ation process is involved in determining and/or maintaining the methylation patterns on DNA. Considering the importance for cells to preserve these patterns, further research will be performed to find additional proof to convalidate one or another mechanism or to identify other possibilities. [Pg.333]

Poly(ADP-ribosyl)ation induces decondensation of chromatin structure which remains significantly decondensed even in the presence of Mg ions ... [Pg.374]

Figure 7.4 Activation of PARP-1 by DNA breaks. PARP-1 is composed of three domains, DNA binding, automodification and catalytic (NAD+ binding) domains (1). In cells, PARP-1 localizes to nucleoli and actively transcribed regions of chromatin by interacting with RNA. When PARP-1 binds to DNA breaks, PARP-1 initiates the poly(ADP-ribosyl)ation reaction by using NAD+ as its substrate (2). PARP-1 itself is the main target of the poly(ADP-ribosyl)ation reaction. ADP-ribose polymers are formed on the automodification domain of PARP-1 (automodification). As a consequence of automodification, PARP-1 dissociates from DNA breaks (3). When cells are committed to apoptosis, PARP-1 is specifically cleaved by an apoptosisspecilic protease, caspase-3, resulting in the formation of a 24kDa N-terminal and 89 kDa C-terminal fragments (4). (see Color Plate 7)... Figure 7.4 Activation of PARP-1 by DNA breaks. PARP-1 is composed of three domains, DNA binding, automodification and catalytic (NAD+ binding) domains (1). In cells, PARP-1 localizes to nucleoli and actively transcribed regions of chromatin by interacting with RNA. When PARP-1 binds to DNA breaks, PARP-1 initiates the poly(ADP-ribosyl)ation reaction by using NAD+ as its substrate (2). PARP-1 itself is the main target of the poly(ADP-ribosyl)ation reaction. ADP-ribose polymers are formed on the automodification domain of PARP-1 (automodification). As a consequence of automodification, PARP-1 dissociates from DNA breaks (3). When cells are committed to apoptosis, PARP-1 is specifically cleaved by an apoptosisspecilic protease, caspase-3, resulting in the formation of a 24kDa N-terminal and 89 kDa C-terminal fragments (4). (see Color Plate 7)...
Poirer, G.G., de Murcia, G., Jongstra-Bilen, J., Niedergang, C. and Mandel, P. (1982) Poly(ADP-ribosyl)ation of polynucleosomes causes relaxation of chromatin structure. Proc. Natl. Acad. Sci. USA, 79, 3423-3427. [Pg.121]

Vispe, S., Yung, T.M.C., Ritchot, J., Serizawa, H. and Satoh, M.S. (2000) New cellular defense pathway regulating transcription through poly(ADP-ribosyl)ation in response to DNA damage. Proc. Natl. Acad. Sci. USA, 97, 9886-9891. [Pg.121]

Wang, Z.Q., Auer, B., Stingl, L., Berghammer, H., Haidacher, D., Schweiger, M. et al. (1995) Mice lacking ADPRT and poly(ADP-ribosyl)ation develop normally but are susceptible to skin disease. Genes Dev., 9, 509-520. [Pg.122]

Mineral Site Point sym- metry Metal-oxygen distances (pm) Mean Poly- Quadratic M-O hedral elong-(pm) volume0 ation ... [Pg.471]

See other pages where Poly ation is mentioned: [Pg.138]    [Pg.237]    [Pg.46]    [Pg.65]    [Pg.66]    [Pg.66]    [Pg.66]    [Pg.67]    [Pg.67]    [Pg.68]    [Pg.70]    [Pg.70]    [Pg.309]    [Pg.315]    [Pg.332]    [Pg.332]    [Pg.333]    [Pg.335]    [Pg.380]    [Pg.1383]    [Pg.1384]    [Pg.908]    [Pg.280]    [Pg.229]    [Pg.110]    [Pg.111]    [Pg.115]    [Pg.115]    [Pg.116]   
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See also in sourсe #XX -- [ Pg.169 ]



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Ation

Cellular Function, Including Centrosome Duplication, by Poly(ADP-Ribosyl)ation

Functional Regulation of p53 by Covalent Poly(ADP-Ribosyl)ation

Histones poly ation

Poly(ADP-Ribosyl)ation Activity and NF-KB-Dependent Gene Expression

Protein-poly ation

The poly(ADP-ribosyl)ation link

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