Evidence map›Paper›PMID 38853146›Full record

ArticleAngewandte Chemie (International ed. in English)2024

Transient Structural Properties of the Rho GDP-Dissociation Inhibitor.

Sara Medina Gomez, Ilaria Visco, Felipe Merino, Peter Bieling, Rasmus Linser

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Sara Medina GomezDepartment of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn-Str. 4a, 44227, Dortmund, Germany.ORCID 0009-0005-9816-8112
Ilaria ViscoDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227, Dortmund, Germany.
Felipe MerinoDepartment of Protein Evolution, Max Planck Institute of Developmental Biology, Max-Planck-Ring 5, 72076, Tübingen, Germany.
Peter BielingDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Str. 11, 44227, Dortmund, Germany.ORCID 0000-0002-7458-4358
Rasmus LinserDepartment of Chemistry and Chemical Biology, TU Dortmund University, Otto-Hahn-Str. 4a, 44227, Dortmund, Germany.ORCID 0000-0001-8983-2935

Funding

Deutsche Forschungsgemeinschaft 24286268Deutsche Forschungsgemeinschaft 27112786Deutsche Forschungsgemeinschaft 325871075Deutsche Forschungsgemeinschaft 390677874Deutsche Forschungsgemeinschaft 399893760European Research Council 101082494HORIZON EUROPE European Research Council 101082494 bypassNMR
6 · The paper itself

Abstract

Rho GTPases, master spatial regulators of a wide range of cellular processes, are orchestrated by complex formation with guanine nucleotide dissociation inhibitors (RhoGDIs). These have been thought to possess an unstructured N-terminus that inhibits nucleotide exchange of their client upon binding/folding. Via NMR analyses, molecular dynamics simulations, and biochemical assays, we reveal instead pertinent structural properties transiently maintained both, in the presence and absence of the client, imposed onto the terminus context-specifically by modulating interactions with the surface of the folded C-terminal domain. These observations revise the long-standing textbook picture of the GTPases' mechanism of membrane extraction. Rather than by a disorder-to-order transition upon binding of an inhibitory peptide, the intricate and highly selective extraction process of RhoGTPases is orchestrated via a dynamic ensemble bearing preformed transient structural properties, suitably modulated by the specific surrounding along the multi-step process.

Indexed as

Molecular Dynamics SimulationHumansProtein Conformationrho-Specific Guanine Nucleotide Dissociation Inhibitorsrho-Specific Guanine Nucleotide Dissociation InhibitorsConformational disorderNMR spectroscopyProtein complexesProtein dynamicsRhoGTPases

Identifiers

PMID38853146
PMCPMC7616425

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 Socratic graph.