Family-wide analysis of poly(ADP-ribose) polymerase activity

• Published in: Nature communications Vol. 5; no. 1; p. 4426
• Main Authors: Vyas, Sejal, Matic, Ivan, Uchima, Lilen, Rood, Jenny, Zaja, Roko, Hay, Ronald T., Ahel, Ivan, Chang, Paul
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 21.07.2014; Nature Publishing Group
• Subjects: 38; 38/109; 631/45/173; 631/80/458/2389; 82; 82/16; 82/29; 82/80; 82/83; Adenosine Diphosphate Ribose - metabolism; Amino Acid Motifs; Cells, Cultured; Cysteine - metabolism; Humanities and Social Sciences; Humans; Lysine - metabolism; multidisciplinary; Poly Adenosine Diphosphate Ribose - metabolism; Poly(ADP-ribose) Polymerases - chemistry; Poly(ADP-ribose) Polymerases - genetics; Poly(ADP-ribose) Polymerases - metabolism; Science; Science (multidisciplinary)

The poly(adenosine diphosphate (ADP)-ribose) polymerase (PARP) protein family generates ADP-ribose (ADPr) modifications onto target proteins using NAD + as substrate. Based on the composition of three NAD + coordinating amino acids, the H-Y-E motif, each PARP is predicted to generate either poly(ADP...