TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 274, No. 17, Issue of April 23, pp. 12036 –12042, 1999 © 1999 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Identification of the Activating and Conjugating Enzymes of the NEDD8 Conjugation Pathway* (Received for publication, June 5, 1998, and in revised form, December 26, 1998) Limin Gong and Edward T. H. Yeh‡ From the Research Center for Cardiovascular Diseases, Institute of Molecular Medicine for the Prevention of Human Diseases, and the Division of Molecular Medicine, Department of Internal Medicine, University of Texas-Houston Health Science Center, Houston, Texas 77030 NEDD8 is a ubiquitin-like molecule that can be co- was required for conjugation of NEDD8 to other proteins. The yeast homologue of NEDD8, Rub1, can also be conjugated to a valently conjugated to a limited number of cellular pro- teins, such as Cdc53/cullin. We have previously reported limited number of cellular proteins, including Cdc53/cullin, a that the C terminus of NEDD8 is efficiently processed to component of the SCF ubiquitin ligase (a complex composed of expose Gly-76, which is required for conjugation to tar- Cdc53, Skp1, and an F-box protein) that plays a critical role in get proteins. A 
TI - Identification of the Activating and Conjugating Enzymes of the NEDD8 Conjugation Pathway
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.274.17.12036
DA - 1999-04-01
UR - https://www.deepdyve.com/lp/unpaywall/identification-of-the-activating-and-conjugating-enzymes-of-the-nedd8-9ivhh3RYgW
DP - DeepDyve
ER -