Evidence map›Paper›PMID 21848311›Full record

ReviewBiochemistry2011

Tolerance to changes in membrane lipid composition as a selected trait of membrane proteins.

Charles R Sanders, Kathleen F Mittendorf

Abstract readReview
In one paragraph

Review in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing 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

54 citing papers in PubMed.

  1. Article
  2. The Evolution of Lipids from Solvents to Substrates.Annual review of biophysics · 2026
    Review
  3. Endogenous Aquaporin-0 Lipid Binding in Ocular Lens Tissue via Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Physical properties of the bacterial outer membrane.Nature reviews. Microbiology · 2022
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Structural cavities are critical to balancing stability and activity of a membrane-integral enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Article
  20. De novo resonance assignment of the transmembrane domain of LR11/SorLA in E. coli membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020
    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

2 authors.

Charles R SandersDepartment of Biochemistry and Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-8725, USA. chuck.sanders@vanderbilt.edu
Kathleen F Mittendorf

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
Protein Structure and Dynamics from EPR Spectroscopy and MD SimulationsP01GM080513 · NIGMS · VANDERBILT UNIVERSITY · PI LYBRAND, TERRY P · 2008 to 2012
$5.6M
Structural Basis for KCNE Modulation of the KCNQ1 ChannelR01DC007416 · NIDCD · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R, VANOYE, CARLOS G. · 2006 to 2014
$3.0M
Structure, Folding, and Misfolding of PMP22R01NS058815 · NINDS · VANDERBILT UNIVERSITY · PI CARTER, BRUCE D, SANDERS, CHARLES R · 2010 to 2012
$921k
NIDCD NIH HHS R01 DC007416NIGMS NIH HHS P01 GM080513NIGMS NIH HHS T32 GM008320NINDS NIH HHS NS058815NINDS NIH HHS R01 NS058815
6 · The paper itself

Abstract

Membrane lipid composition can vary dramatically across the three domains of life and even within single organisms. Here we review evidence that the lipid-exposed surfaces of membrane proteins have generally evolved to maintain correct structure and function in the face of major changes in lipid composition. Such tolerance has allowed evolution to extensively remodel membrane lipid compositions during the emergence of new species without having to extensively remodel the associated membrane proteins. The tolerance of membrane proteins also permits single-cell organisms to vary their membrane lipid composition in response to their changing environments and allows dynamic and organelle-specific variations in the lipid compositions of eukaryotic cells. Membrane protein structural biology has greatly benefited from this seemingly intrinsic property of membrane proteins: the majority of structures determined to date have been characterized under model membrane conditions that little resemble those of native membranes. Nevertheless, with a few notable exceptions, most experimentally determined membrane protein structures appear, to a good approximation, to faithfully report on native structure.

Indexed as

Amino Acid SequenceAnimalsCrystallography, X-RayEvolution, MolecularHumansLipid BilayersMembrane LipidsMembrane ProteinsMolecular Sequence DataProtein Structure, SecondaryProtein Structure, TertiaryLipid BilayersMembrane LipidsMembrane Proteins

Identifiers

PMID21848311
PMCPMC3172382

What OpenQuestion holds

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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.