The DOI matches its Crossref record; 149 of the 149 references it cites were found in a registry or an index.
The GTPase superfamily: conserved structure and molecular mechanism
Abstract
GTPases are conserved molecular switches, built according to a common structural design. Rapidly accruing knowledge of individual GTPases--crystal structures, biochemical properties, or results of molecular genetic experiments--support and generate hypotheses relating structure to function in other members of the diverse family of GTPases.
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“Rather, due to the intrinsically low GTPase activity of G-proteins, regulatory proteins are required for spatiotemporal control of the transition between active and inactive states (Fig. 1B).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [8]
In the citing paper
“The affinity of the interaction between GTPases and either guanine nucleotides is extremely high (Kd 10−7–10−11) ensuring that these are committed states that do not spontaneously interchange; they do not respond to changes in cellular nucleotide concentrations (8).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [8]
In the citing paper
“KRAS proteins primarily bind to guanosine diphosphate (GDP) and are in an inactive conformation maintained by intrinsic guanosine triphosphate (GTP) hydrolytic activity.”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [8]
Citations
Cites
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Cited by
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Items 1,001–1,010 of 1,010
YeiR: a metal-binding GTPase from Escherichia coli involved in metal homeostasis
Blaby-Haas, C. E., Flood, J. A., Crécy-Lagard, V. D., & Zamble, D. B. (2012) · Metallomics · doi:10.1039/c2mt20012k · Cited by 54
Structure-Function Analysis of the Yeast Mitochondrial Rho GTPase, Gem1p
Koshiba, T., Holman, H. A., Kubara, K., Yasukawa, K., Kawabata, S.-I., Okamoto, K., Macfarlane, J., & Shaw, J. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.180034 · Cited by 50
Jafry, M., & Sidbury, R. (2020) · Clinics in Dermatology · doi:10.1016/j.clindermatol.2020.03.010 · Cited by 40
Intrinsic GTPase activity of K-RAS monitored by native mass spectrometry
Moghadamchargari, Z., Huddleston, J., Shirzadeh, M., Zheng, X., Clemmer, D. E., M. Raushel, F., Russell, D. H., & Laganowsky, A. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00532 · Cited by 38
Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation
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Heterotrimeric G Proteins: Insights into the Neurobiology of Mood Disorders
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Thompson, A. P., Bitsina, C., Gray, J. L., von Delft, F., & Brennan, P. E. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100521 · Cited by 21
“The affinity of the interaction between GTPases and either guanine nucleotides is extremely high (Kd 10 –10) ensuring that these are committed states that do not spontaneously interchange; they do not respond to changes in cellular nucleotide concentrations (8).”
BackgroundTet(O), a protein that mediates ribosomal protection to tetracycline, binds, and hydrolyses GTP
Taylor, D. E., Jerome, L. J., Grewal, J., & Chang, N. (1995) · Canadian Journal of Microbiology · doi:10.1139/m95-134 · Cited by 17
CoCoNuTs: A diverse subclass of Type IV restriction systems predicted to target RNA
Bell, R. T., Sahakyan, H., Makarova, K. S., Wolf, Y. I., & Koonin, E. V. (2023) · doi:10.1101/2023.07.31.551357 · Cited by 1
Metadata
- Authors
- Bourne, H. R., Sanders, D. A., & McCormick, F.
- Affiliations
- University of California, San Francisco (US)
- Whitehead Institute for Biomedical Research (US)
- Venue
- Nature
- Published
- 1991-01-10
- Volume
- 349
- Issue
- 6305
- Pages
- 117-127
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1977598234
- Cited by
- 3,392
- References
- 149
- Citations by year
- 2026: 24 · 2025: 44 · 2024: 51 · 2023: 52 · 2022: 37 · 2021: 55 · 2020: 62 · 2019: 50 · 2018: 48 · 2017: 44 · 2016: 58 · 2015: 56 · 2014: 63 · 2013: 61 · 2012: 69
- FWCI
- 30.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- 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 › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- GTPase, GTPase superfamily, molecular switches, structure-function relationship, molecular mechanisms, crystal structure, molecular genetics
- MeSH terms
- Amino Acid Sequence, Animals, Guanosine Diphosphate, Guanosine Triphosphate, Humans, Molecular Sequence Data, Peptide Elongation Factors, Peptide Initiation Factors, Protein Conformation, Protein Processing, Post-Translational, Signal Transduction, Proto-Oncogene Proteins p21(ras), GTP-Binding Proteins, GTP Phosphohydrolase-Linked Elongation Factors
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