The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Geminate recombination of carbon monoxide to myoglobin
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Citations
Cites
Singular value decomposition and least squares solutions
Golub, G. H., & Reinsch, C. (1970) · Numerische Mathematik · doi:10.1007/bf02163027 · Cited by 2,929
Dynamics of ligand binding to myoglobin
Austin, R. H., Beeson, K. W., Eisenstein, L., Frauenfelder, H., & Gunsalus, I. C. (1975) · Biochemistry · doi:10.1021/bi00695a021 · Cited by 1,624
Solvent viscosity and protein dynamics
Beece, D., Eisenstein, L., Frauenfelder, H., Good, D., Marden, M. C., Reinisch, L., Reynolds, A. H., Sorensen, L. B., & Yue, K. T. (1980) · Biochemistry · doi:10.1021/bi00564a001 · Cited by 669
Dynamics of ligand binding to heme proteins
Case, D. A., & Karplus, M. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90265-1 · Cited by 442
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
Influence of globin structure on the state of the heme. I. Human deoxyhemoglobin
Perutz, M. F., Ladner, J. E., Simon, S. R., & Ho, C. (1974) · Biochemistry · doi:10.1021/bi00707a026 · Cited by 292
Interrelationship Between Structure and Function in Hemoglobin and Myoglobin
Antonini, E. (1965) · Physiological Reviews · doi:10.1152/physrev.1965.45.1.123 · Cited by 238
Shrager, R. I., & Hendler, R. W. (1982) · Analytical Chemistry · doi:10.1021/ac00244a031 · Cited by 167
Real space refinement of neutron diffraction data from sperm whale carbonmonoxymyoglobin
Hanson, J. C., & Schoenborn, B. P. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90530-1 · Cited by 160
Control and pH dependence of ligand binding to heme proteins
Doster, W., Beece, D., Bowne, S. F., DiIorio, E. E., Eisenstein, L., Frauenfelder, H., Reinisch, L., Shyamsunder, E., Winterhalter, K. H., & Yue, K. T. (1982) · Biochemistry · doi:10.1021/bi00263a001 · Cited by 160
Cited by
Aspects of Protein Reaction Dynamics: Deviations from Simple Behavior
Karplus, M. (2000) · The Journal of Physical Chemistry B · doi:10.1021/jp993555t · Cited by 306
Kinetic pathways and barriers for ligand binding to myoglobin
Olson, J. S., & Phillips, G. N. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17593 · Cited by 259
“…intramolecular recombination on nanosecond time scales is usually interpreted in terms of a simple two-step scheme involving either rebinding to form the original liganded complex or ligand escape to the solvent to generate the equilibrium form of Mb (Henry et al., 1983; Carver et al., 1990).”
BackgroundLigand recombination to the alpha and beta subunits of human hemoglobin.
Olson, J. S., Rohlfs, R. J., & Gibson, Q. H. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45147-2 · Cited by 58
Metadata
- Authors
- Henry, E. R., Sommer, J. H., Hofrichter, J., Eaton, W. A., & Gellert, M.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1983-05
- Volume
- 166
- Issue
- 3
- Pages
- 443-451
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1974237118
- Cited by
- 268
- References
- 18
- FWCI
- 3.75
- 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: Geminate recombination of carbon monoxide to myoglobin. https://app.cochat.ai/papers/10.1016/s0022-2836(83)80094-1
- The paper
- Henry, E. R., Sommer, J. H., Hofrichter, J., Eaton, W. A., & Gellert, M. (1983). Geminate recombination of carbon monoxide to myoglobin. Journal of Molecular Biology. https://doi.org/10.1016/s0022-2836(83)80094-1
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.