ArticleProtein science : a publication of the Protein Society2026
Induced opening of conformational switch I in GTP-bound Ran GTPase.
Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
1 citing paper in PubMed.
- Induced opening of conformational switch I in GTP-bound Ran GTPase.Protein science : a publication of the Protein Society · 2026Article
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
Ran is a small GTPase that regulates nucleocytoplasmic transport by cycling between an inactive GDP-bound and active GTP-bound state. Structurally, Ran consists of a globular G-domain and a C-terminal region that includes a C-terminal helix. The switch I and II regions of the G-domain undergo major conformational changes upon GTP hydrolysis, with switch I shifting from a closed to an open conformation, regulating cargo loading/unloading. In this study, we describe an induced conformational change in RanGTP that drives switch I from its closed, active state (state 2) to a fully open, inactive state, resembling the RanGDP conformation. This transition is consistently triggered by disruption of two key interactions: Thr42-Mg
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.