The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
The influence of bound GDP on the kinetics of guanine nucleotide binding to G proteins.
Open accessAbstract
Purified guanine nucleotide-binding regulatory proteins, as either the oligomers or the isolated nucleotide-binding alpha subunits, display anomalous kinetics of nucleotide binding. This is due to the presence of tightly bound GDP in these preparations. The dissociation of bound GDP is the rate-limiting step for nucleotide binding. GDP can be removed by chromatography in the presence of 1 M (NH4)2SO4 and 20% glycerol, which yields preparations of G proteins that contain less than 0.1 mol of GDP/mol of guanosine 5'-(gamma-thio)triphosphate (GTP gamma S)-binding site. When the GDP is removed, the binding of GTP gamma S displays kinetics consistent with a bimolecular reaction.
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Citations
Cites
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G proteins and dual control of adenylate cyclase
Gilman, A. G. (1984) · Cell · doi:10.1016/0092-8674(84)90336-2 · Cited by 1,802
Self-citationIsolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain.
Sternweis, P. C., & Robishaw, J. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89817-9 · Cited by 1,301
The Glucagon-sensitive Adenyl Cyclase System in Plasma Membranes of Rat Liver
Rodbell, M., Birnbaumer, L., Pohl, S. L., & Krans, H. M. J. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62390-7 · Cited by 812
Cassel, D., & Selinger, Z. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.8.3307 · Cited by 719
Catecholamine-stimulated GTPase activity in turkey erythrocyte membranes
Cassel, D., & Selinger, Z. (1976) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(76)90206-0 · Cited by 619
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Identification of the predominant substrate for ADP-ribosylation by islet activating protein.
Bokoch, G. M., Katada, T., Northup, J. K., Hewlett, E. L., & Gilman, A. G. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32881-3 · Cited by 583
Self-citationNorthup, J. K., Smigel, M. D., & Gilman, A. G. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33775-x · Cited by 547
Self-citationThe regulatory component of adenylate cyclase. Purification and properties.
Sternweis, P. C., Northup, J. K., Smigel, M. D., & Gilman, A. G. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68431-0 · Cited by 508
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Cited by
Nichols, D. E., & Nichols, C. D. (2008) · Chemical Reviews · doi:10.1021/cr078224o · Cited by 895
Lipid modifications of G protein subunits.
Linder, M. E., Pang, I. H., Duronio, R. J., Gordon, J. I., Sternweis, P. C., & Gilman, A. G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64372-1 · Cited by 278
Self-citationRegulation of Phospholipase C-β1 by Gq and m1 Muscarinic Cholinergic Receptor
Biddlecome, G. H., Berstein, G., & Ross, E. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.14.7999 · Cited by 224
(1997) · American Journal of Psychiatry · doi:10.1176/ajp.154.2.211 · Cited by 58
Metadata
- Authors
- Ferguson, K. M., Higashijima, T., Smigel, M. D., & Gilman, A. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1986-06
- Volume
- 261
- Issue
- 16
- Pages
- 7393-7399
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1544256708
- Cited by
- 259
- References
- 21
- FWCI
- 7.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Ferguson, K. M., Higashijima, T., Smigel, M. D., & Gilman, A. G. (1986). The influence of bound GDP on the kinetics of guanine nucleotide binding to G proteins. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)38404-1
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
