Evidence map›Paper›PMID 39969055›Full record

ArticleProtein science : a publication of the Protein Society2025

Stabilization of a protein by a single halogen-based aromatic amplifier.

Krystel El Hage, Balamurugan Dhayalan, Yen-Shan Chen, Nelson B Phillips, Jonathan Whittaker, Kelley Carr, Linda Whittaker, Manijeh H Phillips, Faramarz Ismail-Beigi, Markus Meuwly and 1 more

Abstract read
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In one paragraph

Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Stabilization of a protein by a single halogen-based aromatic amplifier.Protein science : a publication of the Protein Society · 2025
    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

11 authors.

Krystel El HageDepartment of Chemistry, University of Basel, Basel, Switzerland.ORCID 0000-0003-4837-3888
Balamurugan DhayalanDepartment of Biochemistry & Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Yen-Shan ChenDepartment of Biochemistry & Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Nelson B PhillipsDepartment of Biochemistry, Case Western Reserve University, Cleveland, Ohio, USA.
Jonathan WhittakerDepartment of Biochemistry, Case Western Reserve University, Cleveland, Ohio, USA.
Kelley CarrDepartment of Biochemistry, Case Western Reserve University, Cleveland, Ohio, USA.
Linda WhittakerDepartment of Biochemistry, Case Western Reserve University, Cleveland, Ohio, USA.
Manijeh H PhillipsDepartment of Biochemistry, Case Western Reserve University, Cleveland, Ohio, USA.
Faramarz Ismail-BeigiDepartment of Biochemistry, Case Western Reserve University, Cleveland, Ohio, USA.
Markus MeuwlyDepartment of Chemistry, University of Basel, Basel, Switzerland.
Michael A WeissDepartment of Biochemistry & Molecular Biology, Indiana University School of Medicine, Indianapolis, Indiana, USA.ORCID 0000-0003-1325-1610

Funding

Non-Standard Protein Design in Molecular Endocrinology: Insulin and GlucagonR01DK040949 · NIDDK · UNIVERSITY OF CHICAGO · PI CHERRINGTON, ALAN D, GEORGIADIS, MILLIE M · 1989 to 2024
$8.4M
IU Distinguished Professor Fund at Indiana UniversityLilly INCITE Funds at Indiana UniversityNational Competence Center for Research Molecular and Ultrafast Science and Technology (NCCR MUST)NIDDK NIH HHS R01 DK040949NIH HHS R01DK040949Swiss National Science Foundation 200021-117810University of Basel
6 · The paper itself

Abstract

The utility of halogenation in protein design is investigated by a combination of quantitative atomistic simulations and experiment. Application to insulin is of complementary basic and translational interest. In a singly halogenated aromatic ring, regiospecific inductive effects were predicted to modulate multiple surrounding electrostatic (weakly polar) interactions, thereby amplifying changes in thermodynamic stability. In accordance with the simulations, we demonstrated stabilization of insulin by single halogen atoms at the ortho position of an invariant phenylalanine (2-F-Phe

Indexed as

HalogensInsulinPhenylalanineAnimalsDiabetes Mellitus, ExperimentalHalogenationHumansMolecular Dynamics SimulationProtein StabilityRatsThermodynamicsHalogensInsulinPhenylalanineentropy‐enthalpy compensationfree‐energy simulationprotein dynamicsprotein stabilityunnatural mutagenesis

Identifiers

PMID39969055
PMCPMC11837044

What OpenQuestion holds

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Registered trials

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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.