Evidence map›Paper›PMID 19826804›Full record

ReviewEuropean biophysics journal : EBJ2010

Crystal structures of all-alpha type membrane proteins.

Karen McLuskey, Aleksander W Roszak, Yanshi Zhu, Neil W Isaacs

Abstract readReview
PubMed Publisher
In one paragraph

Review in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Utilization ofBiochimica et biophysica acta. Biomembranes · 2018
    Article
  2. Article
  3. Article
  4. Structural Symmetry in Membrane Proteins.Annual review of biophysics · 2015
    Review
  5. Life at the border: adaptation of proteins to anisotropic membrane environment.Protein science : a publication of the Protein Society · 2014
    Review
  6. Helical membrane protein conformations and their environment.European biophysics journal : EBJ · 2013
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
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

4 authors.

Karen McLuskeyWestchem, Department of Chemistry, Glasgow Biomedical Research Centre, University of Glasgow, 120 University Place, Glasgow, G12 8TA, UK. k.mcluskey@chem.gla.ac.uk
Aleksander W Roszak
Yanshi Zhu
Neil W Isaacs

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

Integral membrane proteins are involved in a wide range of essential biological functions and the determination of their three-dimensional structures plays a central role in understanding their function. This review focuses on the structures of one class of integral membrane proteins: the functionally diverse all-alpha type membrane proteins. It gives an overview of all the structures determined by X-ray crystallography, describing each system and structure in turn. It shows that the structures of all-alpha type membrane proteins have made valuable contributions to understanding structure-function relationships in membrane proteins. These range from the first insights into the function of exciting individual proteins to an in-depth knowledge of protein function from entire biological systems.

Indexed as

Crystallography, X-RayMembrane ProteinsProtein ConformationMembrane Proteins

Identifiers

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.