ADP-ribosylation of nuclear proteins is a critical feature of various DNA damage repair pathways. Histones, particularly H3 and H2B, are major targets of ADP-ribosylation and are primarily modified on ...

The ANBP structure is a novel ADP- and zinc-binding fold, and, to our knowledge, it also represents the first structure of a protein derived from in vitro evolution. Our structure determination ...

Bacterial ADP-ribosyltransferase toxins (bARTTs) transfer ADP-ribose to a range of eukaryotic proteins to promote bacterial pathogenesis. In this Review, the authors discuss the structural and ...

Poly(ADP-ribose) (PAR) is a large, negatively charged post-translational modification that is produced by polymerization of NAD+ by PAR polymerases (PARPs)1. There are at least 18 PARPs in the ...

The ADP-ribosylating toxins (ADPRTs) produced by pathogenic bacteria modify intracellular protein and affect eukaryotic cell function. Actin-specific ADPRTs (including Clostridium perfringens ι-toxin ...

The structure and function of ADP-ribose transferases have been studied extensively but very little is known about the mechanism of the hydrolases that remove ADP-ribosylations, ... The structure of ...

In addition to Arfs, the Arf subfamily contains another, more heterogenous group of proteins with hitherto unknown function. These Arf‐like (Arl) proteins (Tamkun et al., 1991) are similar in sequence ...

The chaperonin proteins GroEL and GroES are cellular nanomachines driven by the hydrolysis of ATP that facilitate the folding of structurally diverse substrate proteins. In response to ligand binding, ...