The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Structure of erythrocruorin in different ligand states refined at 1·4 Å resolution
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Citations
Cites
The interpretation of protein structures: Estimation of static accessibility
Lee, B., & Richards, F. M. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90324-x · Cited by 5,850
PERUTZ, M. F. (1970) · Nature · doi:10.1038/228726a0 · Cited by 2,926
Porphyrins and metalloporphyrins
Gray, C. H. (1976) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(76)90037-2 · Cited by 1,941
Traitement statistique des erreurs dans la determination des structures cristallines
Luzzati, V. (1952) · Acta Crystallographica · doi:10.1107/s0365110x52002161 · Cited by 1,251
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
Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor
Huber, R., Kukla, D., Bode, W., Schwager, P., Bartels, K., Deisenhofer, J., & Steigemann, W. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90163-6 · Cited by 549
Self-citationDeisenhofer, J., & Steigemann, W. (1975) · Acta Crystallographica Section B Structural Crystallography and Crystal Chemistry · doi:10.1107/s0567740875002415 · Cited by 546
Self-citationReal-space refinement of the structure of hen egg-white lysozyme
Diamond, R. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90598-1 · Cited by 536
The refined crystal structure of bovine β-trypsin at 1·8 Å resolution
Bode, W., & Schwager, P. (1975) · Journal of Molecular Biology · doi:10.1016/s0022-2836(75)80005-2 · Cited by 464
Fermi, G. (1975) · Journal of Molecular Biology · doi:10.1016/s0022-2836(75)80037-4 · Cited by 434
Cited by
The relation between the divergence of sequence and structure in proteins.
Chothia, C., & Lesk, A. M. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04288.x · Cited by 2,458
A revised set of potentials for β‐turn formation in proteins
Hutchinson, E. G., & Thornton, J. M. (1994) · Protein Science · doi:10.1002/pro.5560031206 · Cited by 937
Improvements in protein secondary structure prediction by an enhanced neural network
Kneller, D. G., Cohen, F. E., & Langridge, R. (1990) · Journal of Molecular Biology · doi:10.1016/0022-2836(90)90154-e · Cited by 698
Evaluation and improvement of multiple sequence methods for protein secondary structure prediction
Cuff, J. A., & Barton, G. J. (1999) · Proteins: Structure, Function, and Genetics · doi:10.1002/(sici)1097-0134(19990301)34:4<508::aid-prot10>3.0.co;2-4 · Cited by 667
Accurate modeling of protein conformation by automatic segment matching
Levitt, M. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90964-l · Cited by 558
Metadata
- Authors
- Steigemann, W., & Weber, E.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1979-01
- Volume
- 127
- Issue
- 3
- Pages
- 309-338
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1998460935
- Cited by
- 302
- References
- 27
- FWCI
- 8.19
- 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: Structure of erythrocruorin in different ligand states refined at 1·4 Å resolution. https://app.cochat.ai/papers/10.1016/0022-2836(79)90332-2
- The paper
- Steigemann, W., & Weber, E. (1979). Structure of erythrocruorin in different ligand states refined at 1·4 Å resolution. Journal of Molecular Biology. https://doi.org/10.1016/0022-2836(79)90332-2
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.
