The DOI matches its Crossref record; 90 of the 90 references it cites were found in a registry or an index.
Protein oligomerization: How and why
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Citations
Cites
On the nature of allosteric transitions: A plausible model
Monod, J., Wyman, J., & Changeux, J.-P. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80285-6 · Cited by 8,825
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
Hartl, F. U., & Hayer-Hartl, M. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,347
Principles of protein-protein interactions
Jones, S., & Thornton, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.13 · Cited by 2,684
Anatomy of hot spots in protein interfaces
Bogan, A. A., & Thorn, K. S. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1843 · Cited by 1,988
A Hot Spot of Binding Energy in a Hormone-Receptor Interface
Clackson, T., & Wells, J. A. (1995) · Science · doi:10.1126/science.7529940 · Cited by 1,983
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490
Shape Complementarity at Protein/Protein Interfaces
Lawrence, M. C., & Colman, P. M. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1648 · Cited by 1,215
Shape complementarity at protein–protein interfaces
Norel, R., Lin, S. L., Wolfson, H. J., & Nussinov, R. (1994) · Biopolymers · doi:10.1002/bip.360340711 · Cited by 1,208
Principles of protein–protein recognition
Chothia, C., & Janin, J. (1975) · Nature · doi:10.1038/256705a0 · Cited by 1,039
Cited by
Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436
Nanoclustering as a dominant feature of plasma membrane organization
Garcia-Parajo, M. F., Cambi, A., Torreno-Pina, J. A., Thompson, N., & Jacobson, K. (2014) · Journal of Cell Science · doi:10.1242/jcs.146340 · Cited by 284
Jeckelmann, J.-M., & Erni, B. (2019) · Subcellular Biochemistry · doi:10.1007/978-3-030-18768-2_8 · Cited by 55
Protein quaternary structures in solution are a mixture of multiple forms
Marciano, S., Dey, D., Listov, D., Fleishman, S. J., Sonn-Segev, A., Mertens, H., Busch, F., Kim, Y., Harvey, S. R., Wysocki, V. H., et al. (2022) · Chemical Science · doi:10.1039/d2sc02794a · Cited by 41
Thomasen, F. E., Cuneo, M. J., Mittag, T., & Lindorff-Larsen, K. (2023) · eLife · doi:10.7554/elife.84147 · Cited by 9
Metadata
- Authors
- Ali, M. H., & Imperiali, B.
- Venue
- Bioorganic & Medicinal Chemistry
- Publisher
- Elsevier BV
- Published
- 2005-09
- Volume
- 13
- Issue
- 17
- Pages
- 5013-5020
- ISSN
- 0968-0896 (ISSN-L)
- OpenAlex
- W1997566863
- Cited by
- 356
- References
- 90
- FWCI
- 1.96
- Type
- journal article
- Language
- en
- Open access
- closed
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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.
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- CoChat. (2026). Citation check: Protein oligomerization: How and why. https://app.cochat.ai/papers/10.1016/j.bmc.2005.05.037
- The paper
- Ali, M. H., & Imperiali, B. (2005). Protein oligomerization: How and why. Bioorganic & Medicinal Chemistry. https://doi.org/10.1016/j.bmc.2005.05.037
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.
