The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism
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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
PERUTZ, M. F. (1970) · Nature · doi:10.1038/228726a0 · Cited by 2,926
X-ray Diffraction Study of Binding of 2,3-Diphosphoglycerate to Human Deoxyhaemoglobin
ARNONE, A. (1972) · Nature · doi:10.1038/237146a0 · Cited by 739
Structure of myoglobin refined at 2·0 Å resolution
Takano, T. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80111-3 · Cited by 676
Fermi, G. (1975) · Journal of Molecular Biology · doi:10.1016/s0022-2836(75)80037-4 · Cited by 434
Structure of myoglobin refined at 2·0 Å resolution
Takano, T. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80112-5 · Cited by 367
Nature of Haem–Haem Interaction
Perutz, M. F. (1972) · Nature · doi:10.1038/237495a0 · Cited by 367
On the nature of allosteric transitions: Implications of non-exclusive ligand binding
Rubin, M. M., & Changeux, J.-P. (1966) · Journal of Molecular Biology · doi:10.1016/0022-2836(66)90097-0 · Cited by 339
STRUCTURE AND MECHANISM OF HAEMOGLOBIN
PERUTZ, M. F. (1976) · British Medical Bulletin · doi:10.1093/oxfordjournals.bmb.a071363 · Cited by 329
Structure and function of haemoglobin
Bolton, W., Cox, J. M., & Perutz, M. F. (1968) · Journal of Molecular Biology · doi:10.1016/0022-2836(68)90294-5 · Cited by 302
Cited by
The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution
Fermi, G., Perutz, M. F., Shaanan, B., & Fourme, R. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90472-8 · Cited by 771
Sickle Cell Hemoglobin Polymerization
Eaton, W. A., & Hofrichter, J. (1990) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60287-9 · Cited by 623
Protein–protein interaction and quaternary structure
Janin, J., Bahadur, R. P., & Chakrabarti, P. (2008) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583508004708 · Cited by 398
Kinetic and Mechanistic Studies of the NO•-Mediated Oxidation of Oxymyoglobin and Oxyhemoglobin
Herold, S., Exner, M., & Nauser, T. (2001) · Biochemistry · doi:10.1021/bi002407m · Cited by 324
Histidine Metabolism and Function
Brosnan, M. E., & Brosnan, J. T. (2020) · The Journal of Nutrition · doi:10.1093/jn/nxaa079 · Cited by 326
Metadata
- Authors
- Baldwin, J., & Chothia, C.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1979-04
- Volume
- 129
- Issue
- 2
- Pages
- 175-220
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2004194157
- Cited by
- 871
- References
- 21
- FWCI
- 15.67
- 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: Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism. https://app.cochat.ai/papers/10.1016/0022-2836(79)90277-8
- The paper
- Baldwin, J., & Chothia, C. (1979). Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism. Journal of Molecular Biology. https://doi.org/10.1016/0022-2836(79)90277-8
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.
