Evidence mapPaperPMID 41823641Full record

ArticleProtein science : a publication of the Protein Society2026

At the core of the interaction: Probing charged side chains in flexible protein regions with simultaneous nuclear magnetic resonance experiments.

Maria Anna Rodella, Marco Schiavina, Maksim Mayzel, Carlotta Cappanni, Rainer Kümmerle, Roberta Pierattelli, Isabella C Felli

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 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

7 authors.

Maria Anna RodellaDepartment of Chemistry "Ugo Schiff" and Magnetic Resonance Center (CERM), University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0003-0053-0864
Marco SchiavinaDepartment of Chemistry "Ugo Schiff" and Magnetic Resonance Center (CERM), University of Florence, Florence, Italy.
Maksim MayzelBruker BioSpin AG, Fällanden, Switzerland.
Carlotta CappanniDepartment of Chemistry "Ugo Schiff" and Magnetic Resonance Center (CERM), University of Florence, Florence, Italy.
Rainer KümmerleBruker BioSpin AG, Fällanden, Switzerland.
Roberta PierattelliDepartment of Chemistry "Ugo Schiff" and Magnetic Resonance Center (CERM), University of Florence, Florence, Italy.ORCID https://orcid.org/0000-0001-7755-0885
Isabella C FelliDepartment of Chemistry "Ugo Schiff" and Magnetic Resonance Center (CERM), University of Florence, Florence, Italy.

Funding

Bruker BioSpinEuropean Cooperation in Science and Technology CA21160Ministero della Salute PAN-HUB 2021-T4-AN-07Ministero dell'Università e della Ricerca IR0000009Ministero dell'Università e della Ricerca MUR DM352/2022
6 · The paper itself

Abstract

Charged amino acid side chains are crucial mediators of biomolecular recognition, but their characterization by nuclear magnetic resonance (NMR) is often hindered by conformational and solvent exchange, particularly for arginine guanidinium groups. We present two complementary

Indexed as

Nuclear Magnetic Resonance, BiomolecularSARS-CoV-2ArginineProtein BindingArginine13C detectionarginineIDRsnuclear magnetic resonanceprotein‐ligand interactionSARS‐CoV‐2

Identifiers

PMID41823641
PMCPMC13140521

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.