The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Transmembrane glycine zippers: Physiological and pathological roles in membrane proteins
Open accessAbstract
We have observed a common sequence motif in membrane proteins, which we call a glycine zipper. Glycine zipper motifs are strongly overrepresented and conserved in membrane protein sequences, and mutations in glycine zipper motifs are deleterious to function in many cases. The glycine zipper has a significant structural impact, engendering a strong driving force for right-handed packing against a neighboring helix. Thus, the presence of a glycine zipper motif leads directly to testable structural hypotheses, particularly for a subclass of glycine zipper proteins that form channels. For example, we suggest that the membrane pores formed by the amyloid-β peptide in vitro are constructed by glycine zipper packing and find that mutations in the glycine zipper motif block channel formation. Our findings highlight an important structural motif in a wide variety of normal and pathological processes.
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Cites
Berman, H. M. (2000) · Nucleic Acids Research · doi:10.1093/nar/28.1.235 · Cited by 40,196
The Structure of the Potassium Channel: Molecular Basis of K + Conduction and Selectivity
Doyle, D. A., Cabral, J. M., Pfuetzner, R. A., Kuo, A., Gulbis, J. M., Cohen, S. L., Chait, B. T., & MacKinnon, R. (1998) · Science · doi:10.1126/science.280.5360.69 · Cited by 6,807
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Analysis of membrane and surface protein sequences with the hydrophobic moment plot
Eisenberg, D., Schwarz, E., Komaromy, M., & Wall, R. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90309-7 · Cited by 2,284
Stefani, M., & Dobson, C. M. (2003) · Journal of Molecular Medicine · doi:10.1007/s00109-003-0464-5 · Cited by 1,651
Amyloid pores from pathogenic mutations
Lashuel, H. A., Hartley, D., Petre, B. M., Walz, T., & Lansbury, P. T. (2002) · Nature · doi:10.1038/418291a · Cited by 1,289
Helicobacter pylori Virulence and Genetic Geography
Covacci, A., Telford, J. L., Giudice, G. D., Parsonnet, J., & Rappuoli, R. (1999) · Science · doi:10.1126/science.284.5418.1328 · Cited by 1,049
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Role of BNIP3 and NIX in cell death, autophagy, and mitophagy
Zhang, J., & Ney, P. A. (2009) · Cell Death & Differentiation · doi:10.1038/cdd.2009.16 · Cited by 1,021
The amyloid precursor protein has a flexible transmembrane domain and binds cholesterol
Barrett, P. J., Song, Y., Van Horn, W. D., Hustedt, E. J., Schafer, J. M., Hadziselimovic, A., Beel, A. J., & Sanders, C. R. (2012) · Science · doi:10.1126/science.1219988 · Cited by 467
Mechanisms of Integral Membrane Protein Insertion and Folding
Cymer, F., von Heijne, G., & White, S. H. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.09.014 · Cited by 360
Drugging Membrane Protein Interactions
Yin, H., & Flynn, A. D. (2016) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-092115-025322 · Cited by 339
Computational Design of Peptides That Target Transmembrane Helices
Yin, H., Slusky, J. S., Berger, B. W., Walters, R. S., Vilaire, G., Litvinov, R. I., Lear, J. D., Caputo, G. A., Bennett, J. S., & DeGrado, W. F. (2007) · Science · doi:10.1126/science.1136782 · Cited by 289
Metadata
- Authors
- Kim, S., Jeon, T.-J., Oberai, A., Yang, D., Schmidt, J. J., & Bowie, J. U.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-09-22
- Volume
- 102
- Issue
- 40
- Pages
- 14278-14283
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2051425608
- Cited by
- 278
- References
- 44
- FWCI
- 4.49
- Type
- journal article
- Language
- en
- Open access
- green
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- Kim, S., Jeon, T.-J., Oberai, A., Yang, D., Schmidt, J. J., & Bowie, J. U. (2005). Transmembrane glycine zippers: Physiological and pathological roles in membrane proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0501234102
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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