Evidence map›Paper›PMID 33877621›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Biochemical Characterization of GPCR-G Protein Complex Formation.

Filip Pamula, Ching-Ju Tsai

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. 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
–field-weighted citation impact, top 93% of its field
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, 0 citations in OpenAlex.

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 at 1 institution in 1 country.

Filip PamulaLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Ching-Ju TsaiLaboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland. ching-ju.tsai@psi.ch.
Paul Scherrer Institute · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The complex of G protein-coupled receptors (GPCR) and G proteins is the core assembly in GPCR signaling in eukaryotes. With the recent development of cryo-electron microscopy, there has been a rapid growth in structures of GPCR-G protein complexes solved to near-atomic resolution, giving important insights into this signaling complex. Here we describe the biochemical protocol to study the interaction between GPCRs and G proteins before preparation of GPCR-G protein complexes for structural studies. We use gel filtration to analyze the binding properties between GPCR and G protein with the presence of agonist or antagonist, as well as the complex dissociation in the presence of GTP analogue. Methods used in the protocol are affinity purification and gel filtration, which are also commonly used in protein sample preparation for structural work. Therefore, the protocol can be easily adapted for large-scale sample preparation.

Indexed as

Cell MembraneChromatography, GelGTP-Binding ProteinsGuanosine TriphosphateHEK293 CellsHumansProtein BindingReceptors, G-Protein-CoupledSignal TransductionGTP-Binding ProteinsGuanosine TriphosphateReceptors, G-Protein-CoupledAffinity purificationComplex formationDetergentGel filtrationGPCRG proteinLigand

Identifiers

PMID33877621
OpenAlexW3155720078

What OpenQuestion holds

Textmetadata
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.