Evidence map›Paper›PMID 29382720›Full record

ArticleThe Journal of biological chemistry2018

The protonation states of GTP and GppNHp in Ras proteins.

Daniel Mann, Jörn Güldenhaupt, Jonas Schartner, Klaus Gerwert, Carsten Kötting

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 38% of its field
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

8 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Assessing the mechanism of fast-cycling cancer-associated mutations of Rac1 small Rho GTPase.Protein science : a publication of the Protein Society · 2024
    Article
  3. Article
  4. Mechanism-Based Redesign of GAP to Activate Oncogenic Ras.Journal of the American Chemical Society · 2023
    Article
  5. Article
  6. Article
  7. Article
  8. Review
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 at 1 institution in 2 countries.

Daniel MannFrom the Department of Biophysics, Ruhr University Bochum, 44780 Bochum, Germany and.
Jörn GüldenhauptFrom the Department of Biophysics, Ruhr University Bochum, 44780 Bochum, Germany and.
Jonas SchartnerFrom the Department of Biophysics, Ruhr University Bochum, 44780 Bochum, Germany and.
Klaus GerwertFrom the Department of Biophysics, Ruhr University Bochum, 44780 Bochum, Germany and gerwert@bph.rub.de.
Carsten KöttingFrom the Department of Biophysics, Ruhr University Bochum, 44780 Bochum, Germany and carsten.koetting@rub.de.
Ruhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small GTPase Ras transmits signals in a variety of cellular signaling pathways, most prominently in cell proliferation. GTP hydrolysis in the active center of Ras acts as a prototype for many GTPases and is the key to the understanding of several diseases, including cancer. Therefore, Ras has been the focus of intense research over the last decades. A recent neutron diffraction crystal structure of Ras indicated a protonated γ-guanylyl imidodiphosphate (γ-GppNHp) group, which has put the protonation state of GTP in question. A possible protonation of GTP was not considered in previously published mechanistic studies. To determine the detailed prehydrolysis state of Ras, we calculated infrared and NMR spectra from quantum mechanics/molecular mechanics (QM/MM) simulations and compared them with those from previous studies. Furthermore, we measured infrared spectra of GTP and several GTP analogs bound to lipidated Ras on a membrane system under near-native conditions. Our findings unify results from previous studies and indicate a structural model confirming the hypothesis that γ-GTP is fully deprotonated in the prehydrolysis state of Ras.

Indexed as

ProtonsCrystallography, X-RayGuanosine TriphosphateGuanylyl ImidodiphosphateHumansHydrogenationHydrolysisMolecular Dynamics Simulationras ProteinsGuanosine TriphosphateGuanylyl ImidodiphosphateProtonsras ProteinsFourier transform IR, FTIRGTPaseGTP hydrolysismolecular dynamicsNMRnuclear magnetic resonanceQM/MM simulationquantum chemistryRas protein

Identifiers

PMID29382720
PMCPMC5857994
OpenAlexW2786480913

What OpenQuestion holds

Textmetadata
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 OpenQuestion graph.