Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mapping bidirectional allosteric communication in Arf GTPases.

Biophysical journal - 17 Mar 2026

Peters Edgar V, Koduru Tejaswi, McCallum Scott A, Yee Estella F, Cherfils Jacqueline, Royer Catherine A

Abstract excerpt

The Arf GTPases are eukaryotic signaling proteins implicated in trafficking, motility, and membrane remodeling. They must undergo a massive conformational transition in the switch between their inactive, GDP-bound form and their GTP-bound form, competent for downstream signaling. The mechanism of their GDP-to-GTP nucleotide switch implicates a functional molten globule (MG) ensemble. Access to this ensemble and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to ADP-Ribosylation Factor 1
Share to Allosteric Regulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanosine Diphosphate

Share to Guanosine Triphosphate

Share to Models, Molecular

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 41689259
DOI: 10.1016/j.bpj.2026.02.009
PMCID: PMC13033283

Genes

HP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping bidirectional allosteric communication in Arf GTPases.PMID 41689259Read ↗

Sequence determinants of allosteric back-to-front control of the Arf nucleotide switchSemantic proximity Read ↗

Conformational states of ADP ribosylation factor 1 complexed with different guanosine triphosphates as studied by 31P NMR spectroscopy.Semantic proximity Read ↗

Biophysical basis of cellular multi-specificity encoded in a model molecular switchSemantic proximity Read ↗

Dynamically encoded reactivity of Ras enzymes: opening new frontiers for drug discovery.Semantic proximity Read ↗

Assessing the Influence of Mutation on GTPase Transition States by Using X-ray Crystallography, 19 F NMR, and DFT Approaches.Semantic proximity Read ↗

Computational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases.Semantic proximity Read ↗

Allosteric Dynamic Control of Binding.Semantic proximity Read ↗

Dual specificity of the interfacial inhibitor brefeldin a for arf proteins and sec7 domains.Semantic proximity Read ↗

Interaction of Fapp1 with Arf1 and PI4P at a membrane surface: an example of coincidence detection.Semantic proximity Read ↗

Conformational states dynamically populated by a kinase determine its function.Semantic proximity Read ↗

The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways.Semantic proximity Read ↗

Allosteric site variants affect GTP hydrolysis on RASSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.