Evidence map›Paper›PMID 35781716›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2022

The Importance of Mg

Gyula Pálfy, Dóra K Menyhárd, Hanna Ákontz-Kiss, István Vida, Gyula Batta, Orsolya Tőke, András Perczel

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
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  10. The Importance of MgChemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  11. 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

7 authors.

Gyula PálfyLaboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, 1/a Pázmány Péter stny., Budapest, 1117, Hungary.
Dóra K MenyhárdMTA-ELTE Protein Modeling Research Group, Eötvös Loránd Research Network (ELKH), 1/a Pázmány Péter stny., Budapest, 1117, Hungary.
Hanna Ákontz-KissLaboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, 1/a Pázmány Péter stny., Budapest, 1117, Hungary.
István VidaLaboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, 1/a Pázmány Péter stny., Budapest, 1117, Hungary.
Gyula BattaStructural Biology Research Group, Department of Organic Chemistry, University of Debrecen, 1 Egyetem tér, Debrecen, 4032, Hungary.
Orsolya TőkeLaboratory for NMR Spectroscopy, Research Centre for Natural Sciences (RCNS), 2 Magyar tudósok körútja, Budapest, 1117, Hungary.
András PerczelLaboratory of Structural Chemistry and Biology, Institute of Chemistry, Eötvös Loránd University, 1/a Pázmány Péter stny., Budapest, 1117, Hungary.ORCID http://orcid.org/0000-0003-1252-6416

Funding

European Union and the State of Hungary GINOP-2.3.3-15-2016-00004European Union and the State of Hungary VEKOP-2.3.2-16-2017-00014European Union and the State of Hungary VEKOP-2.3.3-15-2017-00018HORIZON EUROPE Framework Programme 653706Hungarian Scientific Research Fund (NKFIH-OTKA) K116305Ministry for Innovation and Technology from the Hungarian NRDI Fund 2020-1.1.6-JÖVŐ-2021-00010Nemzeti Kutatási, Fejlesztési és Innovaciós Alap 2018-1.2.1-NKP-2018-00005Thematic Excellence Program 2019 by the National Research, Development and Innovation Office Synth+
6 · The paper itself

Abstract

For efficient targeting of oncogenic K-Ras interaction sites, a mechanistic picture of the Ras-cycle is necessary. Herein, we used NMR relaxation techniques and molecular dynamics simulations to decipher the role of slow dynamics in wild-type and three oncogenic P-loop mutants of K-Ras. Our measurements reveal a dominant two-state conformational exchange on the ms timescale in both GDP- and GTP-bound K-Ras. The identified low-populated higher energy state in GDP-loaded K-Ras has a conformation reminiscent of a nucleotide-bound/Mg

Indexed as

Molecular Dynamics SimulationNucleotidesGuanosine TriphosphateMutationGuanosine TriphosphateNucleotidesK-Rasmolecular dynamicsNMR spectroscopyras cycleslow dynamics

Identifiers

PMID35781716
PMCPMC9804424

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.