ArticleBiophysical journal2008
Cofactor dependent conformational switching of GTPases.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 36 citations in OpenAlex.
- D81 Mutants Reveal Hidden EF-Tu Diversity while Natural Sequences Preserve Aspartate.Computational and structural biotechnology journal · 2026Article
- The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11.FEBS letters · 2023Review
- Structural basis for assembly of TRAPPII complex and specific activation of GTPase Ypt31/32.Science advances · 2022Article
- Structural basis of elongation factor 2 switching.Current research in structural biology · 2020Article
- E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form.Nucleic acids research · 2018Article
- Mechanistic insight into eukaryotic 60S ribosomal subunit biogenesis by cryo-electron microscopy.RNA (New York, N.Y.) · 2016Review
- Mechanism of eIF6 release from the nascent 60S ribosomal subunit.Nature structural & molecular biology · 2015Article
- EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways.Nucleic acids research · 2015Article
- Structural and Functional Analysis of BipA, a Regulator of Virulence in Enteropathogenic Escherichia coli.The Journal of biological chemistry · 2015Article
- Binding affinities controlled by shifting conformational equilibria: opportunities and limitations.Biophysical journal · 2015Article
- Identification of a second GTP-bound magnesium ion in archaeal initiation factor 2.Nucleic acids research · 2015Article
- A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNA(Cys.).Journal of structural and functional genomics · 2015Article
- A monovalent cation acts as structural and catalytic cofactor in translational GTPases.The EMBO journal · 2014Article
- eIF5B employs a novel domain release mechanism to catalyze ribosomal subunit joining.The EMBO journal · 2014Article
- Relationship between Ni(II) and Zn(II) coordination and nucleotide binding by the Helicobacter pylori [NiFe]-hydrogenase and urease maturation factor HypB.The Journal of biological chemistry · 2014Article
- Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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- GTPases IF2 and EF-G bind GDP and the SRL RNA in a mutually exclusive manner.Scientific reports · 2012Article
- Activation of initiation factor 2 by ligands and mutations for rapid docking of ribosomal subunits.The EMBO journal · 2011Article
- Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 3 countries.
Funding
Abstract
This theoretical work covers structural and biochemical aspects of nucleotide binding and GDP/GTP exchange of GTP hydrolases belonging to the family of small GTPases. Current models of GDP/GTP exchange regulation are often based on two specific assumptions. The first is that the conformation of a GTPase is switched by the exchange of the bound nucleotide from GDP to GTP or vice versa. The second is that GDP/GTP exchange is regulated by a guanine nucleotide exchange factor, which stabilizes a GTPase conformation with low nucleotide affinity. Since, however, recent biochemical and structural data seem to contradict this view, we present a generalized scheme for GTPase action. This novel ansatz accounts for those important cases when conformational switching in addition to guanine nucleotide exchange requires the presence of cofactors, and gives a more nuanced picture of how the nucleotide exchange is regulated. The scheme is also used to discuss some problems of interpretation that may arise when guanine nucleotide exchange mechanisms are inferred from experiments with analogs of GTP, like GDPNP, GDPCP, and GDP gamma S.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.