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Multicenter Stroke Preclinical Assessment Network Analysis of Cardiovascular Risk Factor Subgroups Treated With the Poly(ADP-Ribose) Polymerase Inhibitor Veliparib. [PDF]

J Am Heart Assoc
Koehler RC, Bedirian K, Chen MH, Shi Y, Cao S, Avery BD, Karuppagounder SS, Akhter K, Bibic A, Dawson VL, Dawson TM, Diniz MA, Lamb J, Nagarkatti KA, Chauhan A, Aronowski J, McCullough LD, de Morais AL, Jin X, Ayata C, Kumskova M, Patel RB, Chauhan AK, Leira EC, Kamat PK, Khan MB, Dhandapani KM, Hess DC, Boisserand LSB, Sanganahalli BG, Sansing LH, Lyden PD, SPAN investigators [Link].   +32 more
europepmc   +1 more source

Versatile Modular Antibodies for Sensitive and Specific Detection of Poly-ADP-Ribose

Dauben H, Matić I.
europepmc   +1 more source

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Importance of Poly(ADP-Ribose) Glycohydrolase in the Control of Poly(ADP-Ribose) Metabolism

Experimental Cell Research, 2001
Poly(ADP-ribosyl)ation is a posttranslational modification that alters the functions of the acceptor proteins and is catalyzed by the poly(ADP-ribose) polymerase (PARP) family of enzymes. Following DNA damage, activated poly(ADP-ribose) polymerase-1 (PARP-1) catalyzes the elongation and branching of poly(ADP-ribose) (pADPr) covalently attached to ...
Laetitia Davidović, Momchil D Vodenicharov, Guy G Poirier   +2 more
exaly   +3 more sources

Poly(ADP-ribose): PARadigms and PARadoxes [PDF]

Molecular Aspects of Medicine, 2013
Poly(ADP-ribosyl)ation (PARylation) is a posttranslational protein modification (PTM) catalyzed by members of the poly(ADP-ribose) polymerase (PARP) enzyme family. PARPs use NAD(+) as substrate and upon cleaving off nicotinamide they transfer the ADP-ribosyl moiety covalently to suitable acceptor proteins and elongate the chain by adding further ADP ...
Alexander Bürkle, László Virág
exaly   +4 more sources

Poly(etheno ADP-ribose) blocks poly(ADP-ribose) glycohydrolase activity

Biochemical and Biophysical Research Communications, 2007
Poly(ADP-ribose) is a biopolymer synthesized by poly(ADP-ribose) polymerases. Recent findings suggest the possibility for modulation of cellular functions including cell death and mitosis by poly(ADP-ribose). Derivatization of poly(ADP-ribose) may be useful for investigating the effects of poly(ADP-ribose) on various cellular processes.
Masatoshi Watanabe, Mitsuko Masutani
exaly   +3 more sources

Poly(ADP‐ribose) and carcinogenesis

Genes, Chromosomes and Cancer, 2003
AbstractPoly(ADP‐ribose) and poly(ADP‐ribose) polymerase (PARP) were discovered about 40 years ago, but their significance was not well elucidated until recently. In the early stage of the history of PARP, the presence of antibodies in the sera of human patients with lupus erythematosus indicated its natural occurrence.
Mitsuko, Masutani, Hitoshi, Nakagama, Takashi, Sugimura   +2 more
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Catching mono- and poly-ADP-ribose readers with synthetic ADP-ribose baits

Molecular Cell, 2021
ADP-ribosylation is an essential post-translational modification that comes in two varieties: mono-ADP-ribosylation (MAR) and poly-ADP-ribosylation (PAR). Modular interaction domains that read MAR and PAR modifications are critical for interpreting the language of ADP-ribosylation. Kliza et al.
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Glycation of proteins by ADP-ribose

Molecular and Cellular Biochemistry, 1994
Numerous metabolic pathways generate free ADP-ribose at many locations within cells. The metabolic fates of this nucleotide are poorly understood and measurement of it in situ is technically difficult at present. Yet considerable evidence has accumulated implicating that protein glycation by ADP-ribose can occur.
E L, Jacobson, D, Cervantes-Laurean, M K, Jacobson   +2 more
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Cyclic ADP-ribose

Cellular Signalling, 1999
The Ca2+-mobilizing natural compound cyclic ADP-ribose was discovered in sea urchin egg homogenates. Recently the involvement of cyclic ADP-ribose in Ca2+ signaling has been demonstrated in diverse biological systems spanning protozoa, plants, and cells from invertebrate, mammalian, and human sources.
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New aspects of the physiological significance of NAD, poly ADP-ribose and cyclic ADP-ribose

Biochimie, 1995
Cyclic ADP-ribose is generated from NAD+ in glucose-stimulated beta-cells by CD38. Cyclic ADP-ribose mobilizes Ca2+ from the endoplasmic reticulum to secrete insulin. The amino acid residues of Cys-119 and Cys-201 in CD38 are essential for the synthesis and hydrolysis of cyclic ADP-ribose.
H, Okamoto, S, Takasawa, A, Tohgo
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