@inbook{98fd0c1de3a7454f8c365907bc1d8a9e,
title = "Chapter 13 Ubiquitination Mediated by Inhibitor of Apoptosis Proteins",
abstract = "Inhibitor of apoptosis (IAP) proteins are a family of evolutionarily conserved proteins that regulate apoptosis as well as other cellular processes. The functions of many IAPs are defined by their RING domains, which possess E3 ubiquitin ligase activity and promote proteasomal degradation of an increasing number of target proteins. In this chapter, we describe the methods used in our laboratories to study the IAP's E3 activity.",
author = "Park, {Sun Mi} and Shimin Hu and Lee, {Tae H.} and Xiaolu Yang",
note = "Funding Information: This work was supported by NIH grants CA88868 and CA108872 and a Leukemia & Lymphoma Society Scholar award to X. Y., and the Korea Research Foundation Grant (KRF‐2006‐005‐J04502) and Brain Korea 21 project to T.H.L. The authors are grateful for critical reading of the manuscript by the members of the Yang laboratory.",
year = "2008",
doi = "10.1016/S0076-6879(08)01613-3",
language = "English (US)",
isbn = "9780123744647",
series = "Methods in Enzymology",
pages = "225--235",
editor = "Roya Khosravi-Far and Zahra Zakeri and Richard Lockshin and Mauro Piacentini",
booktitle = "Programmed Cell Death, The Biology and Therapeutic Implications of Cell Death, Part B",
}