Evidence map›Paper›PMID 39769139›Full record

ArticleInternational journal of molecular sciences2024

Molecular Dynamics Simulations Suggest That Side-Chain Motions of Charged Amino Acids Determine Long-Range Effects in Proteins: An Egg of Coulomb.

Neri Niccolai, Edoardo Morandi, Andrea Bernini

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2024. 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.

Neri NiccolaiDepartment of Biotechnology, Chemistry and Pharmacy, University of Siena, 53100 Siena, Italy.
Edoardo MorandiDepartment of Biotechnology, Chemistry and Pharmacy, University of Siena, 53100 Siena, Italy.ORCID 0000-0003-0086-7168
Andrea BerniniDepartment of Biotechnology, Chemistry and Pharmacy, University of Siena, 53100 Siena, Italy.ORCID 0000-0002-7528-2749

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Living systems cannot rely on random intermolecular approaches toward cell crowding, and hidden mechanisms must be present to favor only those molecular interactions required explicitly by the biological function. Electromagnetic messaging among proteins is proposed from the observation that charged amino acids located on the protein surface are mostly in adjacent sequence positions and/or in spatial proximity. Molecular dynamics (MD) simulations have been used to predict electric charge proximities arising from concerted motions of charged amino acid side chains in two protein model systems, human ubiquitin and the chitinolytic enzyme from

Indexed as

Amino AcidsMolecular Dynamics SimulationUbiquitinAnimalsHumansProtein ConformationProteinsStatic ElectricityAmino AcidsProteinsUbiquitinprotein–ligand interactionsprotein long-range communicationsprotein surface electrodynamics

Identifiers

PMID39769139
PMCPMC12381767

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.