Ontology highlight
ABSTRACT:
SUBMITTER: Lee AE
PROVIDER: S-EPMC4909354 | biostudies-literature | 2016 Apr
REPOSITORIES: biostudies-literature
Lee Amanda E AE Geis-Asteggiante Lucia L Dixon Emma K EK Kim Yeji Y Kashyap Tanuja R TR Wang Yan Y Fushman David D Fenselau Catherine C
Journal of mass spectrometry : JMS 20160401 4
The profound effects of ubiquitination on the movement and processing of cellular proteins depend exquisitely on the structures of monoubiquitin and polyubiquitin modifications. Unconjugated polyubiquitins also have a variety of intracellular functions. Structures and functions are not well correlated yet, because the structures of polyubiquitins and polyubiquitin modifications of proteins are difficult to decipher. We are moving towards a robust strategy to provide that structural information. ...[more]