ArticleNature structural & molecular biology2010
Dynamic structure of membrane-anchored Arf*GTP.
Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 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
79 citing papers in PubMed, 140 citations in OpenAlex.
- The Activation of ARF1 Is Dynamically Regulated by its Palmitoylation.Molecular & cellular proteomics : MCP · 2026Article
- Phosphatidylinositol 4,5-bisphosphate mediates Arl4D self-interaction to promote Pak1 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- ARF GTPases Function at the Golgi.Sub-cellular biochemistry · 2026Review
- Putting a lid on it: The N-terminal helix of Arf1 inhibits switching via uniform stabilization.Biophysical journal · 2025Article
- Sequence Determinants of Allosteric Back-to-front Control of the Arf Nucleotide Switch.Journal of molecular biology · 2025Article
- ARF: the most misunderstood GTPase I ever knew - why study ARF GAPs.Frontiers in molecular biosciences · 2025Review
- Surface tension-driven sorting of human perilipins on lipid droplets.The Journal of cell biology · 2024Article
- A molten globule ensemble primes Arf1-GDP for the nucleotide switch.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Myr-Arf1 conformational flexibility at the membrane surface sheds light on the interactions with ArfGAP ASAP1.Nature communications · 2023Article
- Targeting small GTPases: emerging grasps on previously untamable targets, pioneered by KRAS.Signal transduction and targeted therapy · 2023Review
- A plant virus hijacks phosphatidylinositol-3,5-bisphosphate to escape autophagic degradation in its insect vector.Autophagy · 2023Article
- Interactions between TULP3 tubby domain and ARL13B amphipathic helix promote lipidated protein transport to cilia.Molecular biology of the cell · 2023Article
- Myristic acid as a checkpoint to regulate STING-dependent autophagy and interferon responses by promoting N-myristoylation.Nature communications · 2023Article
- ARL3 mediates BBSome ciliary turnover by promoting its outward movement across the transition zone.The Journal of cell biology · 2022Article
- Structural basis for activation of Arf1 at the Golgi complex.Cell reports · 2022Article
- Transient lipid-bound states of spike protein heptad repeats provide insights into SARS-CoV-2 membrane fusion.Science advances · 2021Article
- Fusion Peptide of SARS-CoV-2 Spike Rearranges into a Wedge Inserted in Bilayered Micelles.Journal of the American Chemical Society · 2021Article
- Revealing the activation mechanism of autoinhibited RalF by integrated simulation and experimental approaches.Scientific reports · 2021Article
- Roles for ELMOD2 and Rootletin in ciliogenesis.Molecular biology of the cell · 2021Article
19 more citing papers are in PubMed but not listed here.
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 at 2 institutions in 1 country.
Funding
Abstract
ADP ribosylation factors (Arfs) are N-myristoylated GTP/GDP switch proteins that have key regulatory roles in vesicle transport in eukaryotic cells. ARFs execute their roles by anchoring to membrane surfaces, where they interact with other proteins to initiate budding and maturation of transport vesicles. However, existing structures of Arf*GTP are limited to nonmyristoylated and truncated forms with impaired membrane binding. We report a high-resolution NMR structure for full-length myristoylated yeast (Saccharomyces cerevisiae) Arf1 in complex with a membrane mimic. The two-domain structure, in which the myristoylated N-terminal helix is separated from the C-terminal domain by a flexible linker, suggests a level of adaptability in binding modes for the myriad of proteins with which Arf interacts and allows predictions of specific lipid binding sites on some of these proteins.
Indexed as
Identifiers
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.