ADP-ribosylation—the transfer of ADP-ribose (ADPr) from NAD⁺ onto target molecules—is catalyzed by members of the ADP-ribosyltransferase (ART) superfamily of proteins, found in all kingdoms of life. Modification of amino acids in protein targets by ADPr regulates critical cellular pathways in eukaryotes and underlies the pathogenicity of certain bacteria. Several members of the ART superfamily are highly relevant for disease; these include the poly(ADP-ribose) polymerases (PARPs), recently shown to be important cancer targets, and the bacterial toxins diphtheria toxin and cholera toxin, long known to be responsible for the symptoms of diphtheria and cholera that result in morbidity. In this Review, we discuss the functions of amino acid ADPr modifications and the ART proteins that make them, the nature of the chemical linkage between ADPr and its targets and how this impacts function and stability, and the way that ARTs select specific amino acids in targets to modify.

ADP-核糖基化-从NAD ⁺转移ADP-核糖（ADPr）在所有生命王国中发现的蛋白质的ADP-核糖基转移酶（ART）超家族成员催化到目标分子上。ADPr修饰蛋白质靶标中的氨基酸可调节真核生物中的关键细胞途径，并成为某些细菌的致病力的基础。ART超家族的几个成员与疾病高度相关。这些包括最近被证明是重要的癌症靶点的聚（ADP-核糖）聚合酶（PARP），以及细菌毒素白喉毒素和霍乱毒素，人们早已知道它们会导致白喉和霍乱的症状，从而导致发病。在这篇综述中，我们讨论了氨基酸ADPr修饰的功能以及使它们发生修饰的ART蛋白，ADPr及其靶标之间化学键的性质以及其如何影响功能和稳定性，