Discovery - University of Dundee - Online Publications

Library & Learning Centre

Specificity and disease in the ubiquitin system

Specificity and disease in the ubiquitin system

Research output: Contribution to journalArticle

View graph of relations

Authors

  • Viduth K. Chaugule
  • Helen Walden (Lead / Corresponding author)

Research units

Info

Original languageEnglish
Pages (from-to)212-227
Number of pages16
JournalBiochemical Society Transactions
Volume44
Issue number1
Early online date9 Feb 2016
DOIs
StatePublished - 15 Feb 2016

Abstract

Post-translational modification (PTM) of proteins by ubiquitination is an essential cellular regulatory process. Such regulation drives the cell cycle and cell division, signalling and secretory pathways, DNA replication and repair processes and protein quality control and degradation pathways. A huge range of ubiquitin signals can be generated depending on the specificity and catalytic activity of the enzymes required for attachment of ubiquitin to a given target. As a consequence of its importance to eukaryotic life, dysfunction in the ubiquitin system leads to many disease states, including cancers and neurodegeneration. This review takes a retrospective look at our progress in understanding the molecular mechanisms that govern the specificity of ubiquitin conjugation.

Download statistics

No data available

Documents

Open Access permissions

Open

Documents

  • Final Published Version

    Final published version, 953 KB, PDF-document

    Copyright 2016 Authors. This is an open access article published by Portland Press Limited and distributed under the Creative Commons Attribution Licence 3.0.

DOI

Library & Learning Centre

Contact | Accessibility | Policy