@inbook{97b45fa27be6469da6165b1e63bf6c26,
title = "Using C. elegans to identify the protease targets of serpins in vivo",
abstract = "Most serpins inhibit serine and/or cysteine proteases, and their inhibitory activities are usually defined in vitro. However, the physiological protease targets of most serpins are unknown despite many years of research. This may be due to the rapid degradation of the inactive serpin:protease complexes and/or the conditions under which the serpin inhibits the protease. The model organism Caenorhabditis elegans is an ideal system for identifying protease targets due to powerful forward and reverse genetics, as well as the ease of creating transgenic animals. Using combinatorial approaches of genetics and biochemistry in C. elegans, the true in vivo protease targets of the endogenous serpins can be elucidated.",
keywords = "Caenorhabditis elegans, Mass spectrometry, RNAi, Serpin, Tandem affinity purification",
author = "Bhatia, {Sangeeta R.} and Miedel, {Mark T.} and Chotoo, {Cavita K.} and Graf, {Nathan J.} and Hood, {Brian L.} and Conrads, {Thomas P.} and Silverman, {Gary A.} and Luke, {Cliff J.}",
note = "Copyright: Copyright 2019 Elsevier B.V., All rights reserved.",
year = "2011",
doi = "10.1016/B978-0-12-386471-0.00014-6",
language = "English",
series = "Methods in Enzymology",
publisher = "Academic Press Inc.",
pages = "283--299",
booktitle = "Methods in Enzymology",
}