The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Bilayer Thickness and Membrane Protein Function: An Energetic Perspective
Abstract
The lipid bilayer component of biological membranes is important for the distribution, organization, and function of bilayer-spanning proteins. This regulation is due to both specific lipid-protein interactions and general bilayer-protein interactions, which modulate the energetics and kinetics of protein conformational transitions, as well as the protein distribution between different membrane compartments. The bilayer regulation of membrane protein function arises from the hydrophobic coupling between the protein's hydrophobic domains and the bilayer hydrophobic core, which causes protein conformational changes that involve the protein/bilayer boundary to perturb the adjacent bilayer. Such bilayer perturbations, or deformations, incur an energetic cost, which for a given conformational change varies as a function of the bilayer material properties (bilayer thickness, intrinsic lipid curvature, and the elastic compression and bending moduli). Protein function therefore is regulated by changes in bilayer material properties, which determine the free-energy changes caused by the protein-induced bilayer deformation. The lipid bilayer thus becomes an allosteric regulator of membrane function.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Lipid–protein interactions in biological membranes: A structural perspective
Lee, A. G. (2003) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(03)00056-7 · Cited by 886 · cited 2×
“In fact, when lipid molecules can be discerned and identified in membrane protein structures, they usually are resolved only in part (59, 60)—even at cryogenic temperatures— suggesting limited chemical specificity, significant disorder/mobility, or both.”
BackgroundPermeability of small nonelectrolytes through lipid bilayer membranes
Walter, A., & Gutknecht, J. (1986) · The Journal of Membrane Biology · doi:10.1007/bf01870127 · Cited by 502
Cited by
Membrane lipids: where they are and how they behave
van Meer, G., Voelker, D. R., & Feigenson, G. W. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2330 · Cited by 7,157
Emerging Diversity in Lipid–Protein Interactions
Corradi, V., Sejdiu, B. I., Mesa-Galloso, H., Abdizadeh, H., Noskov, S. Y., Marrink, S. J., & Tieleman, D. P. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00451 · Cited by 459
Optically monitoring voltage in neurons by photo-induced electron transfer through molecular wires
Miller, E. W., Lin, J. Y., Frady, E. P., Steinbach, P. A., Kristan, W. B., & Tsien, R. Y. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120694109 · Cited by 323
Coon, B. G., Baeyens, N., Han, J., Budatha, M., Ross, T. D., Fang, J. S., Yun, S., Thomas, J.-L., & Schwartz, M. A. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201408103 · Cited by 299
Torres, M. J., Kew, K. A., Ryan, T. E., Pennington, E. R., Lin, C.-T., Buddo, K. A., Fix, A. M., Smith, C. A., Gilliam, L. A., Karvinen, S., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2017.10.003 · Cited by 170
Metadata
- Authors
- Andersen, O. S., & Koeppe, R. E.
- Venue
- Annual Review of Biophysics and Biomolecular Structure
- Publisher
- Annual Reviews
- Published
- 2007-06-01
- Volume
- 36
- Issue
- 1
- Pages
- 107-130
- ISSN
- 1056-8700 (ISSN-L)
- 1545-4266
- OpenAlex
- W2101934167
- Cited by
- 866
- References
- 2
- FWCI
- 12.69
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Bilayer Thickness and Membrane Protein Function: An Energetic Perspective. https://app.cochat.ai/papers/10.1146/annurev.biophys.36.040306.132643
- The paper
- Andersen, O. S., & Koeppe, R. E. (2007). Bilayer Thickness and Membrane Protein Function: An Energetic Perspective. Annual Review of Biophysics and Biomolecular Structure. https://doi.org/10.1146/annurev.biophys.36.040306.132643
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.