ArticleNature communications2015
Locking GTPases covalently in their functional states.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- Glutamic acid-lysine (EK) rich motif of RabD2 self-associates and regulates adhesion through multivesicular bodies in Entamoeba histolytica.BMC biology · 2025Article
- Ultrafast and selective labeling of endogenous proteins using affinity-based benzotriazole chemistry.Chemical science · 2022Article
- Review
- GLOBAL AND TARGETED PROFILING OF GTP-BINDING PROTEINS IN BIOLOGICAL SAMPLES BY MASS SPECTROMETRY.Mass spectrometry reviews · 2021Review
- Article
- Rab GTPases take centre stage in understandingSmall GTPases · 2020Review
- Arf6 Can Trigger Wave Regulatory Complex-Dependent Actin Assembly Independent of Arno.International journal of molecular sciences · 2020Article
- Off the wall: The rhyme and reason ofCell surface (Amsterdam, Netherlands) · 2019Review
- USP32 regulates late endosomal transport and recycling through deubiquitylation of Rab7.Nature communications · 2019Article
- The recycling endosome protein RAB-10 promotes autophagic flux and localization of the transmembrane protein ATG-9.Autophagy · 2017Article
- Nucleotide based covalent inhibitors of KRas can only be efficient in vivo if they bind reversibly with GTP-like affinity.Scientific reports · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GTPases act as key regulators of many cellular processes by switching between active (GTP-bound) and inactive (GDP-bound) states. In many cases, understanding their mode of action has been aided by artificially stabilizing one of these states either by designing mutant proteins or by complexation with non-hydrolysable GTP analogues. Because of inherent disadvantages in these approaches, we have developed acryl-bearing GTP and GDP derivatives that can be covalently linked with strategically placed cysteines within the GTPase of interest. Binding studies with GTPase-interacting proteins and X-ray crystallography analysis demonstrate that the molecular properties of the covalent GTPase-acryl-nucleotide adducts are a faithful reflection of those of the corresponding native states and are advantageously permanently locked in a defined nucleotide (that is active or inactive) state. In a first application, in vivo experiments using covalently locked Rab5 variants provide new insights into the mechanism of correct intracellular localization of Rab proteins.
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What OpenQuestion holds
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.