作者: Sjoerd J. L. van Wijk , Magda Bienko , Ivan Dikic
DOI: 10.1007/978-1-61779-474-2_11
关键词: Computational biology 、 Ubiquitin 、 Chemistry 、 Function (biology) 、 Multiple forms 、 DNA-binding protein
摘要: The versatile function of ubiquitin (Ub) is powerfully illustrated by its appearance in multiple forms and shapes, like polymeric chains. These chains, when recognized specific ubiquitin-binding domains (UBDs), give rise to extraordinary complex signaling networks that regulate virtually every cellular function. At the heart our understanding this complexity evolution adaptation technologies methods analyze biochemistry, e.g., covalent Ub-substrate conjugates as well transient Ub-UBD interactions. Here, we describe seminal developments those methodologies have paved way diversity Ub signals their recognition interpretation UBD-containing proteins.