Evidence map›Paper›PMID 20101433›Full record

ReviewCellular and molecular life sciences : CMLS2010

Protein folding in membranes.

Sebastian Fiedler, Jana Broecker, Sandro Keller

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 86 citations in OpenAlex.

  1. Review
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  9. Membranes as the third genetic code.Molecular biology reports · 2020
    Review
  10. Article
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  12. Article
  13. Article
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  15. Article
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  18. Implications of aromatic-aromatic interactions: From protein structures to peptide models.Protein science : a publication of the Protein Society · 2015
    Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Sebastian FiedlerLeibniz Institute of Molecular Pharmacology (FMP), Robert-Rössle-Str. 10, 13125, Berlin, Germany.
Jana Broecker
Sandro Keller
Leibniz Association · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Separation of cells and organelles by bilayer membranes is a fundamental principle of life. Cellular membranes contain a baffling variety of proteins, which fulfil vital functions as receptors and signal transducers, channels and transporters, motors and anchors. The vast majority of membrane-bound proteins contain bundles of alpha-helical transmembrane domains. Understanding how these proteins adopt their native, biologically active structures in the complex milieu of a membrane is therefore a major challenge in today's life sciences. Here, we review recent progress in the folding, unfolding and refolding of alpha-helical membrane proteins and compare the molecular interactions that stabilise proteins in lipid bilayers. We also provide a critical discussion of a detergent denaturation assay that is increasingly used to determine membrane-protein stability but is not devoid of conceptual difficulties.

Indexed as

Protein FoldingHydrogen BondingHydrophobic and Hydrophilic InteractionsLipid BilayersMembrane ProteinsModels, MolecularProtein DenaturationProtein MultimerizationProtein StabilityProtein Structure, SecondaryLipid BilayersMembrane Proteins

Identifiers

PMID20101433
PMCPMC11115603
OpenAlexW2060463651

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.