ArticleBiochemistry2009
Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The trial behind it
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
14 citing papers in PubMed.
- Article
- GTP hydrolysis by Synechocystis IM30 does not decisively affect its membrane remodeling activity.Scientific reports · 2020Article
- Signal Recognition Particle RNA Contributes to Oxidative Stress Response inFrontiers in microbiology · 2020Article
- Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting.The Journal of cell biology · 2014Article
- Biochemical and functional characterization of Plasmodium falciparum GTP cyclohydrolase I.Malaria journal · 2014Article
- Speed controls in translating secretory proteins in eukaryotes--an evolutionary perspective.PLoS computational biology · 2014Article
- The tRNA-modifying function of MnmE is controlled by post-hydrolysis steps of its GTPase cycle.Nucleic acids research · 2013Article
- Precise timing of ATPase activation drives targeting of tail-anchored proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- SecYEG activates GTPases to drive the completion of cotranslational protein targeting.The Journal of cell biology · 2013Article
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- Signal sequence-independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle.Molecular biology of the cell · 2011Article
- Molecular mechanism of co-translational protein targeting by the signal recognition particle.Traffic (Copenhagen, Denmark) · 2011Review
- The activation mechanism of Irga6, an interferon-inducible GTPase contributing to mouse resistance against Toxoplasma gondii.BMC biology · 2011Article
- Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.The Journal of cell biology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The GTP-binding proteins or GTPases comprise a superfamily of proteins that provide molecular switches in numerous cellular processes. The "GTPase switch" paradigm, in which a GTPase acts as a bimodal switch that is turned "on" and "off" by external regulatory factors, has been used to interpret the regulatory mechanism of many GTPases for more than two decades. Nevertheless, recent work has unveiled an emerging class of "multistate" regulatory GTPases that do not adhere to this classical paradigm. Instead of relying on external nucleotide exchange factors or GTPase activating proteins to switch between the on and off states, these GTPases have the intrinsic ability to exchange nucleotides and to sense and respond to upstream and downstream factors. In contrast to the bimodal nature of the GTPase switch, these GTPases undergo multiple conformational rearrangements, allowing multiple regulatory points to be built into a complex biological process to ensure the efficiency and fidelity of the pathway. We suggest that these multistate regulatory GTPases are uniquely suited to provide spatial and temporal control of complex cellular pathways that require multiple molecular events to occur in a highly coordinated fashion.
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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.