The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
The allosteric transition of glycogen phosphorylase
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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
Application of a Theory of Enzyme Specificity to Protein Synthesis
Koshland, D. E. (1958) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.44.2.98 · Cited by 2,396
PRINCIPLES THAT DETERMINE THE STRUCTURE OF PROTEINS
Chothia, C. (1984) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.53.070184.002541 · Cited by 646
Control of Phosphorylase Activity in a Muscle Glycogen Particle
Meyer, F., Heilmeyer, L. M. G., Haschke, R. H., & Fischer, E. H. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62582-7 · Cited by 356
Fitzgerald, P. M. D. (1988) · Journal of Applied Crystallography · doi:10.1107/s0021889887012299 · Cited by 343
Structural changes in glycogen phosphorylase induced by phosphorylation
Sprang, S. R., Acharya, K. R., Goldsmith, E. J., Stuart, D. I., Varvill, K., Fletterick, R. J., Madsen, N. B., & Johnson, L. N. (1988) · Nature · doi:10.1038/336215a0 · Cited by 299
Self-citationA method of positioning a known molecule in an unknown crystal structure
Crowther, R. A., & Blow, D. M. (1967) · Acta Crystallographica · doi:10.1107/s0365110x67003172 · Cited by 267
Crystallographic refinement by simulated annealing: application to crambin
Brünger, A. T., Karplus, M., & Petsko, G. A. (1989) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767388009195 · Cited by 254
Sussman, J. L., Holbrook, S. R., Church, G. M., & Kim, S.-H. (1977) · Acta Crystallographica Section A · doi:10.1107/s0567739477001958 · Cited by 246
THE ROLE OF ADENYLIC ACID IN THE ACTIVATION OF PHOSPHORYLASE
HELMREICH, E. J. M., & Cori, C. F. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.1.131 · Cited by 235
Cited by
Structural Symmetry and Protein Function
Goodsell, D. S., & Olson, A. J. (2000) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.29.1.105 · Cited by 950
Folding funnels and binding mechanisms
Ma, B., Kumar, S., Tsai, C.-J., & Nussinov, R. (1999) · Protein Engineering, Design and Selection · doi:10.1093/protein/12.9.713 · Cited by 594
Network Analysis of Protein Structures Identifies Functional Residues
Amitai, G., Shemesh, A., Sitbon, E., Shklar, M., Netanely, D., Venger, I., & Pietrokovski, S. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.055 · Cited by 499
Allostery and the Monod-Wyman-Changeux Model After 50 Years
Changeux, J.-P. (2012) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-050511-102222 · Cited by 391
Brain nicotinic receptors: structure and regulation, role in learning and reinforcement
Changeux, J.-P., Bertrand, D., Corringer, P.-J., Dehaene, S., Edelstein, S., Léna, C., Le Novère, N., Marubio, L., Picciotto, M., & Zoli, M. (1998) · Brain Research Reviews · doi:10.1016/s0165-0173(97)00040-4 · Cited by 322
Metadata
- Authors
- Barford, D., & Johnson, L. N.
- Venue
- Nature
- Published
- 1989-08
- Volume
- 340
- Issue
- 6235
- Pages
- 609-616
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2088345550
- Cited by
- 294
- References
- 18
- FWCI
- 26.60
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: The allosteric transition of glycogen phosphorylase. https://app.cochat.ai/papers/10.1038/340609a0
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- Barford, D., & Johnson, L. N. (1989). The allosteric transition of glycogen phosphorylase. Nature. https://doi.org/10.1038/340609a0
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.
