The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
The interaction of Ras with GTPase‐activating proteins
Abstract
Ras plays a major role as a molecular switch in many signal transduction pathways which lead to cell growth and differentiation. The GTPase reaction of Ras is of central importance in the function of the switch since it terminates Ras‐effector interactions. GTPase‐activating proteins (GAPs) accelerate the very slow intrinsic hydrolysis reaction of the GTP‐bound Ras by several orders of magnitude and thereby act as presumably negative regulators of Ras action. The GTP hydrolysis of oncogenic mutants of Ras remains unaltered. In this review we discuss recent biochemical and structural findings relating to the mechanism of GAP action, which strengthen the hypothesis that GAP accelerates the actual cleavage step by stabilizing the transition state of the phosphoryl transfer reaction.
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“Activated RAS proteins can interact with many downstream effector proteins, such as RAF kinase, son of sevenless (SOS), phosphatidylinositol 3-kinase (PI3K) and Ral guanine nucleotide dissociation stimulating factors (RalGDS), which regulate cell events such as cell proliferation and apoptosis.323–325”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [324]
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Cites
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
The GTPase superfamily: a conserved switch for diverse cell functions
Bourne, H. R., Sanders, D. A. R., & McCormick, F. P. (1990) · Nature · doi:10.1038/348125a0 · Cited by 2,336
A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic Mutants
Trahey, M., & McCormick, F. (1987) · Science · doi:10.1126/science.2821624 · Cited by 1,211
The neurofibromatosis type 1 gene encodes a protein related to GAP
Xu, G., O'Connell, P., Viskochil, D., Cawthon, R., Robertson, M., Culver, M., Dunn, D., Stevens, J., Gesteland, R., White, R., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90024-9 · Cited by 1,095
Cawthon, R., Weiss, R. B., Xu, G., Viskochil, D. H., Culver, M., Stevens, J., Robertson, M. A., Dunn, D. M., Gesteland, R. F., O'Connell, P., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90253-b · Cited by 1,093
Deletions and a translocation interrupt a cloned gene at the neurofibromatosis type 1 locus
Viskochil, D. H., Buchberg, A. M., Xu, G., Cawthon, R., Stevens, J., Wolff, R. K., Culver, M., Carey, J. C., Copeland, N. G., Jenkins, N. A., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90252-a · Cited by 1,082
Milburn, M. V., Tong, L., deVos, A. M., Brünger, A. T., Yamaizumi, Z., Nishimura, S., & Kim, S. (1990) · Science · doi:10.1126/science.2406906 · Cited by 1,062
The GAP-related domain of the neurofibromatosis type 1 gene product interacts with ras p21
Martin, G. A., Viskoohil, D., Bollag, G. E., McCabe, P. C., Crosier, W. J., Haubruck, H., Conroy, L., Clark, R., O'Connell, P., Cawthon, R., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90150-d · Cited by 983
PAI, E. F., Kabsch, W., Krengel, U., Holmes, K. C., John, J., & Wittinghofer, A. (1989) · Nature · doi:10.1038/341209a0 · Cited by 876
Self-citation
Research works printed but not linked: 4
- Klebe C., 1995, Biochemistry, 34, 1254
- Ahmadian MR Hoffmann U Goody RS Wittinghofer A. Biochemistry 1997 (in press).
- Gawler D.J., 1995, Oncogene, 10, 817
- John J. Thesis Ruprecht-Karls-Universität Heidelberg 1990.
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Self-citationRecent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials
Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396
Metadata
- Authors
- Wittinghofer, A., Scheffzek, K., & Ahmadian, M. R.
- Affiliations
- Max Planck Institute of Molecular Physiology (DE)
- Corresponding author
- Wittinghofer, Alfred
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1997-06-23
- Volume
- 410
- Issue
- 1
- Pages
- 63-67
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2001438210
- Cited by
- 135
- References
- 58
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 3 · 2023: 4 · 2022: 7 · 2021: 5 · 2020: 4 · 2019: 5 · 2017: 2 · 2016: 3 · 2015: 7 · 2014: 2 · 2013: 1 · 2012: 5
- FWCI
- 0.59
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Ras, GTPase-activating protein, GTP hydrolysis, signal transduction, transition state stabilization, phosphoryl transfer
- MeSH terms
- Animals, Humans, Models, Molecular, Protein Conformation, Proteins, ras Proteins, GTPase-Activating Proteins, ras GTPase-Activating Proteins
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