Evidence map›Paper›PMID 41562307›Full record

ReviewProtein science : a publication of the Protein Society2026

Deceptive beauty of non-natural structures.

Vsevolod V Gurevich, Eugenia V Gurevich

Abstract readReview
In one paragraph

Review 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. Deceptive beauty of non-natural structures.Protein science : a publication of the Protein Society · 2026
    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

2 authors.

Vsevolod V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, Tennessee, USA.ORCID https://orcid.org/0000-0002-3950-5351
Eugenia V GurevichDepartment of Pharmacology, Vanderbilt University, Nashville, Tennessee, USA.ORCID https://orcid.org/0000-0002-0563-8295

Funding

STRUCTURE/FUNCTION STUDIES OF VISUAL ARRESTINR01EY011500 · NEI · VANDERBILT UNIVERSITY · PI T M Iverson · 1997 to 2026
$12.3M
NEI NIH HHS R01 EY011500NIH HHS EY011500
6 · The paper itself

Abstract

Structures of proteins and multiprotein complexes are considered landmark achievements. However, in many cases, mutant proteins are used for structural work. Even when wild type proteins are used, crystallization or complex formation for cryoEM is performed in highly nonphysiological conditions. This explains why the structures can be inconsistent with the functional data. The structures are always true, but solved structures faithfully reveal the mode of interactions of the proteins used in the conditions employed. The structures are static, whereas proteins are dynamic. Even when a series of structures are solved, the dynamics are only implied or deduced via molecular dynamics simulations. The mechanisms of protein function in the natural environment can be revealed by the combination of structural, biochemical, biophysical, and in vivo studies, supplemented by molecular modeling.

Indexed as

ProteinsAnimalsHumansModels, MolecularMolecular Dynamics SimulationProtein ConformationProteinsarrestinGPCRprotein–protein interactionsprotein structure

Identifiers

PMID41562307
PMCPMC12820791

What OpenQuestion 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 OpenQuestion graph.