Evidence map›Paper›PMID 42681346›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2026

Design and Optimization of BRIL Fusion Constructs for Membrane Protein Cryo-EM Studies.

Amrutha H Chidananda, Camilo Perez

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Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Amrutha H ChidanandaDepartment of Biochemistry & Molecular Biology, University of Georgia, Athens, GA, USA.
Camilo PerezDepartment of Biochemistry & Molecular Biology, University of Georgia, Athens, GA, USA. camilo.perez@uga.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural determination of small membrane proteins by cryo-electron microscopy (cryo-EM) remains inherently challenging due to their low molecular weight, conformational heterogeneity, and lack of prominent structural features for reliable particle alignment. In this chapter, we describe how to design and perform biophysical characterization of BRIL fusion constructs that may facilitate structure determination by single-particle cryogenic electron microscopy (cryo-EM) analysis. We present a streamlined approach to select optimal constructs using AlphaFold predictions and characterization by mass photometry and thermal stability assays. We demonstrate the suitability of BRIL fusion strategy as a versatile approach for facilitating structural studies of small membrane proteins by cryo-EM.

Indexed as

Cryoelectron MicroscopyMembrane ProteinsRecombinant Fusion ProteinsProtein ConformationMembrane ProteinsRecombinant Fusion ProteinsBRIL fusion constructsCryo-EMFiducial markerMembrane proteins

Identifiers

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.