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Catching mono- and poly-ADP-ribose readers with synthetic ADP-ribose baits
Molecular Cell, 2021ADP-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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1987
In eukaryotic cells, two different types of enzymes are known to attack poly-(ADP-ribose). The first enzyme, poly(ADP-ribose) glycohydrolase, cleaves ri-bose-ribose bonds of both linear and branched portions of poly(ADP-ribose) polymers by an exoglycosidic hydrolysis mode.
Felix R. Althaus, Christoph Richter
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In eukaryotic cells, two different types of enzymes are known to attack poly-(ADP-ribose). The first enzyme, poly(ADP-ribose) glycohydrolase, cleaves ri-bose-ribose bonds of both linear and branched portions of poly(ADP-ribose) polymers by an exoglycosidic hydrolysis mode.
Felix R. Althaus, Christoph Richter
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European Journal of Biochemistry, 1984
Poly(ADP‐ribose) polymerase and poly(ADP‐ribose) glycohydrolase have been detected in chromatin extracts from the dinoflagellate Crypthecodinium cohnii. Poly(ADP‐ribose) glycohydrolase was detected by the liberation of ADP‐ribose from poly(ADP‐ribose).
E, Werner +5 more
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Poly(ADP‐ribose) polymerase and poly(ADP‐ribose) glycohydrolase have been detected in chromatin extracts from the dinoflagellate Crypthecodinium cohnii. Poly(ADP‐ribose) glycohydrolase was detected by the liberation of ADP‐ribose from poly(ADP‐ribose).
E, Werner +5 more
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Regulation of poly(ADP-ribose) metabolism by poly(ADP-ribose) glycohydrolase: where and when?
Cellular and molecular life sciences : CMLS, 2005Poly(ADP-ribose) glycohydrolase (PARG) is a catabolic enzyme that cleaves ADP-ribose polymers formed by members of the PARP family of enzymes. Despite its discovery and subsequent partial purification in the 1970s and the cloning of its single gene in the late 1990s, little is known about the role of PARG in cell function.
M-E, Bonicalzi +3 more
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1985
Nucleoids are nuclei-like structures produced from cells lysed with nonionic detergents in the presence of high salt concentrations. By this treatment, histones and most of the nonhistone proteins are removed [3]. They contain naked, histone-free DNA, RNA, and a few proteins [1]. DNA is supercoiled and attached to a cage of residual proteins and RNA [5]
Gordana Brkić +2 more
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Nucleoids are nuclei-like structures produced from cells lysed with nonionic detergents in the presence of high salt concentrations. By this treatment, histones and most of the nonhistone proteins are removed [3]. They contain naked, histone-free DNA, RNA, and a few proteins [1]. DNA is supercoiled and attached to a cage of residual proteins and RNA [5]
Gordana Brkić +2 more
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1987
There is overwhelming evidence showing that poly-ADP-ribosylation reactions are ubiquitously distributed among higher eukaryotes (Table 2.1). A notable exception to this are mammalian erythrocytes, which lose the activity during ery-thropoiesis concomitant with the enucleation step.
Felix R. Althaus, Christoph Richter
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There is overwhelming evidence showing that poly-ADP-ribosylation reactions are ubiquitously distributed among higher eukaryotes (Table 2.1). A notable exception to this are mammalian erythrocytes, which lose the activity during ery-thropoiesis concomitant with the enucleation step.
Felix R. Althaus, Christoph Richter
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Poly(ADP-ribose): A Dynamic Trigger for Biomolecular Condensate Formation
Trends in Cell Biology, 2020Anthony K L Leung
exaly
Poly(ADP-Ribose) polymerase (PARP) inhibitors: Exploiting a synthetic lethal strategy in the clinic
Ca-A Cancer Journal for Clinicians, 2011Timothy A Yap +2 more
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Role of poly(ADP-ribose) synthetase in inflammation and ischaemia–reperfusion
Trends in Pharmacological Sciences, 1998Csaba SZABÓ +2 more
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