Evidence map›Paper›PMID 41418323›Full record

ReviewBiological chemistry2026

Mechanistic insights into Ras-catalyzed GTP hydrolysis: conformational dynamics, catalytic mechanisms, and emerging therapeutic strategies.

Carsten Kötting, Till Rudack, Klaus Gerwert

Abstract readReview
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In one paragraph

Review in Biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

3 authors.

Carsten KöttingCenter for Protein Diagnostics (PRODI), Biospectroscopy, Ruhr University Bochum, Bochum, Germany.ORCID 0000-0002-3599-9657
Till RudackStructural Bioinformatics Group, Regensburg Center for Biochemistry, University of Regensburg, Regensburg, Germany.ORCID 0000-0003-2693-9561
Klaus GerwertCenter for Protein Diagnostics (PRODI), Biospectroscopy, Ruhr University Bochum, Bochum, Germany.ORCID 0000-0001-8759-5964

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ras is a key regulator of signal transduction in cells. Ras malfunction is associated with a huge variety of oncological diseases. It is turned off by hydrolysis of bound GTP, which is accelerated by GTPase-activating proteins (GAPs). This minireview discusses the mechanism of Ras-catalyzed GTP hydrolysis, focusing on conformational dynamics and catalytic mechanisms. We discuss structural changes and the role of key residues such as Thr35, Gly60, Tyr32, Gln61, Gly12, and Gly13. Biophysical techniques such as X-ray crystallography, time-resolved FTIR spectroscopy, and hybrid quantum mechanics/molecular mechanics calculations have revealed the detailed reaction mechanisms, including the entry of the arginine finger and the rate-limiting step of inorganic phosphate release. Recent studies on the hydrolysis mechanism favor a solvent-assisted pathway. In addition, we summarize recent advances in Ras-targeting drugs.

Indexed as

Guanosine Triphosphateras ProteinsAnimalsBiocatalysisHumansHydrolysisProtein ConformationGuanosine Triphosphateras ProteinsFTIR-spectroscopyGTPaseQM/MM calculationsRasX-ray crystallography

Identifiers

PMID41418323

What OpenQuestion holds

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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 OpenQuestion graph.