Evidence map›Paper›PMID 18539023›Full record

ReviewCurrent opinion in structural biology2008

Association energetics of membrane spanning alpha-helices.

Kevin R MacKenzie, Karen G Fleming

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

53 citing papers in PubMed, 87 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Spiers Memorial Lecture: Analysis andFaraday discussions · 2021
    Article
  6. Folding and misfolding of potassium channel monomers during assembly and tetramerization.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. Quarterly reviews of biophysics · 2020
    Review
  11. Review
  12. Article
  13. Design of self-assembling transmembrane helical bundles to elucidate principles required for membrane protein folding and ion transport.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Biologically active LIL proteins built with minimal chemical diversity.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

2 authors at 2 institutions in 1 country.

Kevin R MacKenzieDepartment of Biochemistry & Cell Biology, Rice University, Houston, TX 77251-1892, USA.
Karen G Fleming
Johns Hopkins University · USRice University · US

Funding

Structural analysis of BNIP3 transmembrane interactionsR01GM067850 · NIGMS · RICE UNIVERSITY · PI MACKENZIE, KEVIN R · 2004 to 2008
$1.2M
NIGMS NIH HHS R01 GM 067850NIGMS NIH HHS R01 GM067850
6 · The paper itself

Abstract

Since Popot and Engelman proposed the 'two-stage' thermodynamic framework for dissecting the energetics of helical membrane protein folding, scientists have endeavored to measure the free energies of helix-helix associations to better understand how interactions between helices stabilize and specify native membrane protein folds. Chief among the biophysical tools used to probe these energies are sedimentation equilibrium analytical ultracentrifugation, fluorescence resonance energy transfer, and thiol disulfide interchange experiments. Direct and indirect comparisons of thermodynamic results suggest that differences in helix-helix stabilities between micelles and bilayers may not be as large as previously anticipated. Genetic approaches continue to become more quantitative, and the propensities for helices to interact in bacterial membranes generally correlate well with in vitro measurements.

Indexed as

Biophysical PhenomenaBiophysicsLipid BilayersMembrane ProteinsMicellesThermodynamicsLipid BilayersMembrane ProteinsMicelles

Identifiers

PMID18539023
PMCPMC7127525
OpenAlexW2019666571

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.