The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.
Conformation, co-operativity and ligand binding in human hemoglobin
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“both ferrous deoxy and oxyheme react relatively rapidly (rate constants ~107 M-1s-1) with NO to produce nitrosyl heme (Scheme 1) or nitrate respectively [29, 30].”
From Current perspectives and challenges in understanding the role of nitrite as an integral player in nitric oxide biology and therapy (2011) · cites this paper as [29]
Citations
Cites
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.
Monod, J., Wyman, J., & Changeux, J. (1965) · Journal of Molecular Biology · doi:10.1016/s0022-2836(65)80285-6 · Cited by 7,681
Perutz, M. F. (1970) · Nature · doi:10.1038/228726a0 · Cited by 2,914
The kinetics and equilibria of the reactions of nitric oxide with sheep haemoglobin
Gibson, Q. H., & Roughton, F. J. W. (1957) · The Journal of Physiology · doi:10.1113/jphysiol.1957.sp005777 · Cited by 396
Preparation and Properties of α- and β-Chains from Human Hemoglobin
GERACI, G., Parkhurst, L. J., & Gibson, Q. H. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)93675-6 · Cited by 365
The Binding of Hemoglobin to Haptoglobin and Its Relation to Subunit Dissociation of Hemoglobin
Nagel, R. L., & Gibson, Q. H. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62533-5 · Cited by 204
Gibson, Q. H. (1970) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62992-8 · Cited by 174
An allosteric model of hemoglobin: I, kinetics
Hopfield, J. J., Shulman, R. G., & Ogawa, S. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90391-3 · Cited by 160
Banerjee, R., Alpert, Y., Leterrier, F., & Williams, R. J. P. (1969) · Biochemistry · doi:10.1021/bi00835a025 · Cited by 111
Observation of allosteric transition in hemoglobin
Ogawa, S., & Shulman, R. G. (1971) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(71)90354-8 · Cited by 105
Ligand Binding and Release of an Analogue of 2,3-Diphosphoglycerate from Human Hemoglobin
MacQuarrie, R. A., & Gibson, Q. H. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44814-x · Cited by 87
Research works printed but not linked: 6
- Benesch, 1968, 59, 526
- Benesch, 1968, 61, 1102
- Cassoly, 1974, C.R. Acad. Sci, 278, 1417
- Gibson, 1957, 146, 206
- Gibson, 1957, 147, 44
- Gibson, 1965, 163, 197
Cited by
Sorted by citations
Cell-free hemoglobin limits nitric oxide bioavailability in sickle-cell disease
Reiter, C. D., Wang, X., Tanus-Santos, J. E., Hogg, N., Cannon, R. O., Schechter, A. N., & Gladwin, M. T. (2002) · Nature Medicine · doi:10.1038/nm1202-799 · Cited by 1,330
Reactive nitrogen species in the chemical biology of inflammation
Dedon, P. C., & Tannenbaum, S. R. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.12.017 · Cited by 681
Oxidation of nitrogen-oxides by bound dioxygen in hemoproteins
Doyle, M. P., & Hoekstra, J. W. (1981) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)80291-3 · Cited by 643
Reactions between nitric oxide and haemoglobin under physiological conditions
Gow, A. J., & Stamler, J. S. (1998) · Nature · doi:10.1038/34402 · Cited by 562
Nitric oxide and iron proteins
Cooper, C. E. (1999) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(99)00021-3 · Cited by 510
Metadata
- Authors
- Cassoly, R., & Gibson, Q. H.
- Affiliations
- Institut de Biologie Physico-Chimique (FR)
- Cornell University (US)
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1975-01
- Volume
- 91
- Issue
- 3
- Pages
- 301-313
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2007942188
- Cited by
- 259
- References
- 18
- Citations by year
- 2024: 2 · 2023: 1 · 2022: 3 · 2021: 4 · 2019: 3 · 2018: 3 · 2017: 5 · 2016: 5 · 2015: 5 · 2014: 10 · 2013: 8 · 2012: 8
- FWCI
- 2.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
- Keywords
- human hemoglobin, nitric oxide binding, carbon monoxide binding, ligand binding kinetics, ligand competition, conformational change
- MeSH terms
- Arylsulfonates, Carbon Monoxide, Chemistry, Hemoglobins, Humans, Kinetics, Ligands, Nitric Oxide, Protein Binding, Protein Conformation, Pyrenes, Chemical Phenomena
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
