Zobrazeno 1 - 10
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pro vyhledávání: '"Julia A. Thissen"'
Publikováno v:
Journal of Biological Chemistry. 272:30362-30370
We recently identified a prenyl peptide-binding protein in microsomal membranes from bovine brain (Thissen, J. A., and Casey, P. J. (1993)J. Biol. Chem. 268, 13780–13783). Through a variety of approaches, this binding protein has been identified as
Publikováno v:
Journal of Biological Chemistry. 272:15591-15594
Protein farnesyltransferase inhibitors (FTIs) inhibit Ras transformation and Ras-dependent tumor cell growth, but the biological mechanisms underlying these activities is unclear. In previous work, we presented support for the hypothesis that the ant
Autor:
Julia A. Thissen, Patrick J. Casey
Publikováno v:
Journal of Biological Chemistry. 268:13780-13783
Prenylation and subsequent processing of many proteins involved in cellular signaling serves to direct and/or anchor these proteins to specific membranes in the cell. One major class of prenylated proteins contains the so-called CAAX motif; such prot
Autor:
Ching C. Wang, Julia A. Thissen
Publikováno v:
Experimental Parasitology. 72:243-251
The internal pH value (pHi) of the long-slender bloodstream form of Trypanosoma brucei was estimated from the distribution of 14C-labeled 5,5-dimethyl-2,4-oxazolidinedione or 14C-labeled methyl amine between the intracellular space of the cells and t
Autor:
Julia A. Thissen, Patrick J. Casey
Publikováno v:
Analytical biochemistry. 243(1)
Protein farnesyl transferase (FTase) catalyzes the addition of a farnesyl isoprenoid to a conserved cysteine residue in Ras and several other key proteins involved in cell regulation. An assay technique commonly used to measure FTase activity involve
Publisher Summary This chapter discusses the methods used in the identification of specific binding proteins for prenylated peptides, which was initially identified and characterized using biochemical binding analysis. The chemical cross-linking appr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a7526f0945aa4cf06b9e5755cd5fca8e
https://doi.org/10.1016/0076-6879(95)50070-7
https://doi.org/10.1016/0076-6879(95)50070-7
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
Publisher Summary This chapter presents recent studies in the field of protein prenylation, with particular emphasis on the enzymology of these processes and the influence of the modifications on specific G proteins involved in cellular signaling. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::071cefa3f096087c841ea7112a09047e
https://doi.org/10.1016/b978-0-12-571149-4.50015-5
https://doi.org/10.1016/b978-0-12-571149-4.50015-5
The prenylation of several proteins involved in oncogenesis and signal transduction plays an essential role in regulating their biological activities. Two distinct isoprenoids are known to be involved in this modification, the 15-carbon farnesyl and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31a08113bd3b23fbf7ef9371fc9bee6c
https://europepmc.org/articles/PMC52563/
https://europepmc.org/articles/PMC52563/
Publikováno v:
Molecular and cellular biology. 10(9)
Glycosomes are microbody organelles found in kinetoplastida, where they serve to compartmentalize the enzymes of the glycolytic pathway. In order to identify the mechanism by which these enzymes are targeted to the glycosome, we have modified the in