Evidence map›Paper›PMID 36151492›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Exploring the Topology of Cytoplasmic Membrane Proteins Involved in Lipopolysaccharide Biosynthesis by in Silico and Biochemical Analyses.

Julia Monjarás Feria, Miguel A Valvano

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. 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 73% 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.

Julia Monjarás FeriaWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.
Miguel A ValvanoWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK. m.valvano@qub.ac.uk.
Queen's University Belfast · GB

Funding

Biotechnology and Biological Sciences Research Council BB/S006281/1Biotechnology and Biological Sciences Research Council BB/T005807/1Medical Research Council MR/P022480/1
6 · The paper itself

Abstract

In the absence of a tri-dimensional structure, revealing the topology of a membrane protein provides relevant information to identify the number and orientation of transmembrane helices and the localization of critical amino acid residues, contributing to a better understanding of function and intermolecular associations. Topology can be predicted in silico by bioinformatic analysis or solved by biochemical methods. In this chapter, we describe a pipeline employing bioinformatic approaches for the prediction of membrane protein topology, followed by experimental validation through the substituted-cysteine accessibility method and the analysis of the protein's oligomerization state.

Indexed as

CysteineLipopolysaccharidesAmino AcidsCell MembraneMembrane ProteinsAmino AcidsCysteineLipopolysaccharidesMembrane ProteinsLipopolysaccharideMembrane proteinProtein oligomerizationProtein topologySubstituted cysteine accessibility mutagenesisSulfhydryl labeling

Identifiers

PMID36151492
OpenAlexW4296869462

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.