TY - JOUR
T1 - GTPases in protozoan parasites
T2 - Tools for cell biology and chemotherapy
AU - Field, M. C.
AU - Ali, B. R.S.
AU - Field, H.
N1 - Funding Information:
We thank all those who generously provided unpublished data for inclusion. These include Frederic Bringaud (Bordeaux, France), Al Ivens (London, UK), Darren Nesbeth (London, UK), Keith Joiner and Tim Stedman (New Haven, USA) and also Keith Gull (Manchester, UK) for invaluable assistance with establishing microscopy in our laboratory. We also thank Tim Jeffries for noticing the rtb8–TbRab4 identity and for database searching. Research in our laboratory is supported by The Wellcome Trust, the Medical Research Council (MRC) and the Biotechnology and Biological Sciences Research Council (BBSRC).
PY - 1999/9/1
Y1 - 1999/9/1
N2 - Small G proteins belong to a superfamily of GTPases related to the protooncogene ras, and function as master control elements for a range of cellular functions. This ability is related to their low rate of substrate turnover; GTPases catalyse the conversion of GTP to GDP, but with a rate in the order of one substrate per second, orders of magnitude slower than 'good' enzyme catalysis, but placing the reaction into the temporal frame of many cellular processes including signal transduction, cytoskeletal reorganization and vesicle trafficking. In this article, Mark Field, Bassam Ali and Helen Field describe some recent advances in G-protein studies in the parasite field, concentrating on the protozoan parasites. Because of their numerous roles in cell biology, understanding parasite G proteins has great potential for increasing our knowledge of parasite cellular physiology, as well as providing important inroads into vital processes for potential therapeutic exploitation. Copyright (C) 1999 Elsevier Science Ltd.
AB - Small G proteins belong to a superfamily of GTPases related to the protooncogene ras, and function as master control elements for a range of cellular functions. This ability is related to their low rate of substrate turnover; GTPases catalyse the conversion of GTP to GDP, but with a rate in the order of one substrate per second, orders of magnitude slower than 'good' enzyme catalysis, but placing the reaction into the temporal frame of many cellular processes including signal transduction, cytoskeletal reorganization and vesicle trafficking. In this article, Mark Field, Bassam Ali and Helen Field describe some recent advances in G-protein studies in the parasite field, concentrating on the protozoan parasites. Because of their numerous roles in cell biology, understanding parasite G proteins has great potential for increasing our knowledge of parasite cellular physiology, as well as providing important inroads into vital processes for potential therapeutic exploitation. Copyright (C) 1999 Elsevier Science Ltd.
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U2 - 10.1016/S0169-4758(99)01499-4
DO - 10.1016/S0169-4758(99)01499-4
M3 - Review article
C2 - 10461165
AN - SCOPUS:0033198291
SN - 0169-4758
VL - 15
SP - 365
EP - 371
JO - Parasitology Today
JF - Parasitology Today
IS - 9
ER -