scholarly journals Protein Farnesyltransferase Subunit Beta

2020 ◽  
Author(s):  
Keyword(s):  
Protein Farnesyltransferase

scholarly journals Protein farnesyltransferase fromTrypanosoma brucei. A heterodimer of 61- and 65-kDa subunits as a new target for antiparasite therapeutics.

2001 ◽  
Vol 276 (25) ◽  
pp. 23212
Author(s):  
Kohei Yokoyama ◽  
Patty Trobridge ◽  
Frederick S. Buckner ◽  
Wesley C. Van Voorhis ◽  
Kenneth D. Stuart ◽  
...  
Keyword(s):  
Protein Farnesyltransferase

Anti-Inflammatory Activity in Vitro and in Vivo of the Protein Farnesyltransferase Inhibitor Tipifarnib

2005 ◽  
Vol 317 (1) ◽  
pp. 53-60 ◽  
Author(s):  
Xiaohua Xue ◽  
Kuei-Tai A. Lai ◽  
Jing-Feng Huang ◽  
Yin Gu ◽  
Lars Karlsson ◽  
...  
Keyword(s):  
Inflammatory Activity ◽  
Farnesyltransferase Inhibitor ◽  
Protein Farnesyltransferase ◽  
Anti Inflammatory

scholarly journals Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila

2010 ◽  
Vol 207 (8) ◽  
pp. 1713-1726 ◽  
Author(s):  
Christopher T.D. Price ◽  
Tasneem Al-Quadan ◽  
Marina Santic ◽  
Snake C. Jones ◽  
Yousef Abu Kwaik
Keyword(s):  
Legionella Pneumophila ◽  
Biological Function ◽  
Host Cells ◽  
Dependent Manner ◽  
Protein Farnesyltransferase ◽  
Type Iv ◽  
Eukaryotic Proteins ◽  
Bacterial Effectors

Farnesylation involves covalent linkage of eukaryotic proteins to a lipid moiety to anchor them into membranes, which is essential for the biological function of Ras and other proteins. A large cadre of bacterial effectors is injected into host cells by intravacuolar pathogens through elaborate type III–VII translocation machineries, and many of these effectors are incorporated into the pathogen-containing vacuolar membrane by unknown mechanisms. The Dot/Icm type IV secretion system of Legionella pneumophila injects into host cells the F-box effector Ankyrin B (AnkB), which functions as platforms for the docking of polyubiquitinated proteins to the Legionella-containing vacuole (LCV) to enable intravacuolar proliferation in macrophages and amoeba. We show that farnesylation of AnkB is indispensable for its anchoring to the cytosolic face of the LCV membrane, for its biological function within macrophages and Dictyostelium discoideum, and for intrapulmonary proliferation in mice. Remarkably, the protein farnesyltransferase, RCE-1 (Ras-converting enzyme-1), and isoprenyl cysteine carboxyl methyltransferase host farnesylation enzymes are recruited to the LCV in a Dot/Icm-dependent manner and are essential for the biological function of AnkB. In conclusion, this study shows novel localized recruitment of the host farnesylation machinery and its anchoring of an F-box effector to the LCV membrane, and this is essential for biological function in vitro and in vivo.

Protein Farnesyltransferase Inhibitors

2004 ◽  
Vol 1 (1) ◽  
pp. 97-128
Author(s):  
Semiramis Ayral-Kaloustian ◽  
Edward J. Salaski
Keyword(s):  
Farnesyltransferase Inhibitors ◽  
Protein Farnesyltransferase

Protein Farnesyltransferase

2018 ◽  
pp. 4211-4216
Author(s):  
Lai N. Chan ◽  
Fuyuhiko Tamanoi
Keyword(s):  
Protein Farnesyltransferase

Highly improved antiparasitic activity after introduction of an N-benzylimidazole moiety on protein farnesyltransferase inhibitors

2016 ◽  
Vol 109 ◽  
pp. 173-186 ◽  
Author(s):  
Damien Bosc ◽  
Elisabeth Mouray ◽  
Sandrine Cojean ◽  
Caio Haddad Franco ◽  
Philippe M. Loiseau ◽  
...  
Keyword(s):  
Farnesyltransferase Inhibitors ◽  
Antiparasitic Activity ◽  
Protein Farnesyltransferase
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