Zobrazeno 1 - 10
of 12
pro vyhledávání: '"John F. Moomaw"'
Publikováno v:
Science. 275:1800-1805
Protein farnesyltransferase (FTase) catalyzes the carboxyl-terminal lipidation of Ras and several other cellular signal transduction proteins. The essential nature of this modification for proper function of these proteins has led to the emergence of
Publikováno v:
Journal of Biological Chemistry. 271:28541-28548
Protein farnesyltransferase (FTase) is a zinc metalloenzyme that performs a post-translational modification on many proteins that is critical for their function. The importance of cysteine residues in FTase activity was investigated using cysteine-sp
Publikováno v:
Journal of Biological Chemistry. 269:23465-23470
Protein geranylgeranyltransferase type I (GGTase I) catalyzes the prenylation of a number of proteins that play important roles in cellular signaling. The recent cDNA cloning of this enzyme (Zhang, F. L., Diehl, R. E., Kohl, N. E., Gibbs, J. B., Giro
Autor:
Patrick J. Casey, John F. Moomaw
Publikováno v:
Journal of Biological Chemistry. 267:17438-17443
An enzyme capable of specifically modifying, with a geranylgeranyl isoprenoid, candidate proteins containing a consensus prenylation sequence ending in leucine has been purified from bovine brain. This protein geranylgeranyltransferase (PGGT), isolat
Autor:
Alexander Dietrich, Ole N. Jensen, John F. Moomaw, Michael Meister, Daria Illenberger, Derek P. Brazil, Marion Schrader, Matthias Mann, Peter Gierschik
Publikováno v:
Biochemistry. 35(48)
We have previously shown that isoprenylation and/or additional post-translational processing of the G protein gamma 1 subunit carboxyl terminus is required for beta 1 gamma 1 subunit stimulation of phospholipase C-beta 2 (PLC beta 2) [Dietrich, A., M
Publisher Summary This chapter discusses the methodologies used for the isolation and expression of the prenyltransferases acting on CaaX-containing proteins—namely, protein farnesyltransferase (FTase) and protein geranylgeranyltransferase type I (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::759e37ecc614e78419b384351397770a
https://doi.org/10.1016/0076-6879(95)50058-8
https://doi.org/10.1016/0076-6879(95)50058-8
Autor:
C. Wayne Bardin, Eugene A. Berkowitz, David M. Berman, Susan Bonner-Weir, David L. Brautigan, Sondi Brown, Michael J. Brownstein, James T. Bryant, Dennis R. Burholt, E.R. Burns, Kristine M. Cala, Patrick J. Casey, William W. Chu, Donald S. Coffey, S.B. Conway, Daphne L. Davis, Jakob Dupont, Marilyn I. Evans, Stanley Friedman, Masato Fujisawa, Susan Gamble, Susan Garfinkel, D.W. Gietzen, Danling Gu, Joyce B. Higgins, Lyann R. Hodgskin, Beth J. Hoffman, W.G. Hope, Xiaoguo Hu, Anthony Jackson, Gary L. Johnson, L.-M. Kow, Narender Kumar, Charles P. Landrum, Carol A. Lange-Carter, A.H. Lauber, Xingquan Liu, P. Kay Lund, Thomas Maciag, Paul Mak, M.M. McCarthy, Arlene Mercado, John F. Moomaw, Patricia L. Morris, F. Murad, Maria I. New, Ishwar S. Parhar, Alan W. Partin, J.N. Pasley, Tony Pawson, D.W. Pfaff, Chris Pleiman, Sandra L. Polizotto, James S. Prihoda, Igor Prudovsky, P.L. Rayford, David W. Russell, Madhabananda Sar, Nora Sarvetnick, M. Schwanzel-Fukuda, William A. Segraves, Jianping Shi, Richard I. Silver, Phyllis W. Speiser, Elizabeth Stoner, Kalyan Sundaram, Francesca Tarantini, Anice E. Thigpen, Julia A. Thissen, M.A. Thompson-Reece, Donald J. Tindall, Fred W. Turek, Anthony N. Wakim, Jörg Wessendorf, Perrin C. White, W. Christian Wigley, Elizabeth M. Wilson, Choi-iok Wong, D.E. Woolley, Charles Y.-F. Young, Xi Zhan, Fang L. Zhang, Zhong-xun Zhou, Deguang Zhu, Ann Zimrin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::abcc00d91f1705d83f31c98a5b0fb114
https://doi.org/10.1016/b978-0-12-571149-4.50003-9
https://doi.org/10.1016/b978-0-12-571149-4.50003-9