Title |
GTPase activating proteins: structural and functional insights 18 years after discovery
|
---|---|
Published in |
Cellular and Molecular Life Sciences, November 2005
|
DOI | 10.1007/s00018-005-5136-x |
Pubmed ID | |
Authors |
K. Scheffzek, M. R. Ahmadian |
Abstract |
The conversion of guanosine triphosphate (GTP) to guanosine diphosphate (GDP) and inorganic phosphate (P(i)) by guanine nucleotide binding proteins (GNBPs) is a fundamental process in living cells and represents an important timer in intracellular signalling and transport processes. While the rate of GNBP-mediated GTP hydrolysis is intrinsically slow, direct interaction with GTPase activating proteins (GAPs) accelerates the reaction by up to five orders of magnitude in vitro. Eighteen years after the discovery of the first GAP, biochemical and structural research has been accumulating evidence that GAPs employ a much wider spectrum of chemical mechanisms than had originally been assumed, in order to regulate the chemical players on the catalytic protein-protein interaction stage. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Germany | 2 | 1% |
Belgium | 2 | 1% |
Hungary | 1 | <1% |
Brazil | 1 | <1% |
Portugal | 1 | <1% |
Spain | 1 | <1% |
Japan | 1 | <1% |
Unknown | 147 | 94% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 41 | 26% |
Researcher | 36 | 23% |
Student > Master | 19 | 12% |
Student > Bachelor | 14 | 9% |
Other | 7 | 4% |
Other | 16 | 10% |
Unknown | 23 | 15% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 68 | 44% |
Biochemistry, Genetics and Molecular Biology | 30 | 19% |
Chemistry | 12 | 8% |
Medicine and Dentistry | 8 | 5% |
Pharmacology, Toxicology and Pharmaceutical Science | 5 | 3% |
Other | 8 | 5% |
Unknown | 25 | 16% |