http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
1 online resource (x, 322 pages) : illustrations, 14 pages of plates
This is the first compilation of protein lipidation enzymes. This volume summarizes recent dramatic developments regarding enzymes responsible for protein lipidation, a process critical for a number of physiological functions, including cell proliferation and morphology. Inhibitors of protein lipidation have recently been shown to be useful as anticancer drugs. Enzymatic mechanisms, mutational analysis, and structural studies are presented. Key Features * The enzymatic mechanisms of protein lipidation * Three-dimensional structures of protein farnesytransferase, protein geranylgeranytransferase II, and n-myristoryltransferase.
Preface. -- Mechanism of Catalysis by Protein Farnesyltransferase, R.A. Spence and P.J. Casey. -- Structure of Protein Farnesyltransferase, K.L. Terry, S.B. Long, and L.S. Beese. -- Mutational Analyses of Protein Farnesyltransferase, J. Urano, W. Yang, and F. Tamanoi. -- Farnesyltransferase Inhibitors, J.B. Gibbs. -- Protein Geranylgeranyltransferase Type I, K. Yokoyama and M.H. Geleb. -- Biochemistry of Rab Geranylgeranyltransferase, M.C. Seabra. -- Postisoprenylation Protein Processing: CXXX (CaaX) Endoproteases and Isoprenylcysteine Carboxyl Methyltransferase, S.G. Young, P. Ambroziak, E. Kim, and S. Clarke. -- Reversible Modification of Proteins with Thioester-Linked Fatty Acids, M.E. Linder. -- Biology and Enzymology of Protein N-Myristoylation, R.S. Bhatnagar, K. Ashrafi, K. Futterer, G. Waksman, and J.I. Gordon. -- Chapter References. -- Author Index. -- Subject Index.
edited by Fuyuhiko Tamanoi and David S. Sigman.
Master and use copy. Digital master created according to Benchmark for Faithful Digital Reproductions of Monographs and Serials, Version 1. Digital Library Federation, December 2002. http://purl.oclc.org/DLF/benchrepro0212 MiAaHDL
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Includes bibliographical references and index.
82520:82520 Elsevier Science & Technology