The DOI matches its Crossref record; 54 of the 54 references it cites were found in a registry or an index.
Structure-Function Relations of Human Hemoglobins
Open accessAbstract
In 1949 Pauling and his associates showed that sickle cell hemoglobin (HbS) belonged to an abnormal molecular species. In 1958 Ingram, who used a two-dimensional system of electrophoresis and chromatography to break down the hemoglobin molecule into a mixture of smaller peptides, defined the molecular defect in HbS by showing that it differed from normal adult hemoglobin by only a single peptide. Since then, more than 200 variant and abnormal hemoglobins have been described. Furthermore, the construction of an atomic model of the hemoglobin molecule based on a high-resolution x-ray analysis by Dr. Max Perutz at Cambridge has permitted the study of the stereochemical part played by the amino acid residues, which were replaced, deleted, or added to in each of the hemoglobin variants. Some of the variants have been associated with clinical conditions. The demonstration of a molecular basis for a disease was a significant turning point in medicine. A new engineered hemoglobin derived from crocodile blood, with markedly reduced oxygen affinity and increased oxygen delivery to the tissues, points the way for future advances in medicine.
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“The haem group contains iron as a co-factor at its core and the iron reversibly binds oxygen only when it is in the ferrous form (Fe2+) (Marengo-Rowe, 2006).”
From Iron at the Centre of Candida albicans Interactions (2018) · cites this paper as Marengo-Rowe, 2006
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Mortality in sickle cell disease. Life expectancy and risk factors for early death
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“Leukocytosis itself is a risk factor for increased mortality (24).”
BackgroundPerutz, M. F. (1970) · Nature · doi:10.1038/228726a0 · Cited by 2,914
Sickle Cell Anemia, a Molecular Disease
Pauling, L., Itano, H. A., Singer, S. J., & Wells, I. C. (1949) · Science · doi:10.1126/science.110.2865.543 · Cited by 2,319
Perutz, M. F., Rossmann, M. G., Cullis, A. F., Muirhead, H., Will, G., & North, A. C. T. (1960) · Nature · doi:10.1038/185416a0 · Cited by 1,351
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“In the deoxygenated form of HbS, the beta-6 valine becomes buried in a hydrophobic pocket on an adjacent beta-globin chain, joining the molecules together to form insoluble polymers (9).”
BackgroundINGRAM, V. M. (1957) · Nature · doi:10.1038/180326a0 · Cited by 978
Effect of Hydroxyurea on Mortality and Morbidity in Adult Sickle Cell Anemia
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PECULIAR ELONGATED AND SICKLE-SHAPED RED BLOOD CORPUSCLES IN A CASE OF SEVERE ANEMIA
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Candida albicans iron acquisition within the host
Almeida, R. S., Wilson, D., & Hube, B. (2009) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2009.00570.x · Cited by 199
Under the spotlight: mechanisms of photobiomodulation concentrating on blue and green light
Serrage, H. J., Heiskanen, V., Palin, W. M., Cooper, P. R., Milward, M. R., Hadis, M. A., & Hamblin, M. R. (2019) · Photochemical & Photobiological Sciences · doi:10.1039/c9pp00089e · Cited by 168
Paper Microfluidics for Point-of-Care Blood-Based Analysis and Diagnostics
Li, H., & Steckl, A. J. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.8b03636 · Cited by 158
Protein Nanoparticles: Uniting the Power of Proteins with Engineering Design Approaches
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Metadata
- Authors
- Marengo-Rowe, A. J.
- Affiliations
- Baylor University Medical Center (US)
- Corresponding author
- Marengo-Rowe, Alain J.
- Venue
- Baylor University Medical Center Proceedings
- Publisher
- Informa UK Limited
- Published
- 2006-07
- Volume
- 19
- Issue
- 3
- Pages
- 239-245
- ISSN
- 0899-8280 (ISSN-L)
- 1525-3252
- PMC
- PMC1484532
- OpenAlex
- W1589718460
- Cited by
- 179
- References
- 54
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 27 · 2023: 26 · 2022: 32 · 2021: 21 · 2020: 15 · 2019: 9 · 2018: 9 · 2017: 2 · 2016: 7 · 2015: 2 · 2014: 2 · 2013: 3 · 2012: 2
- FWCI
- 0.28
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Baylor University Medical Center Proceedings (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Health Sciences › Medicine › Genetics (clinical) › Hemoglobinopathies and Related Disorders
- Health Sciences › Medicine › Hematology › Blood properties and coagulation
- Keywords
- hemoglobin variants, hemoglobin S, structure-function relationship, amino acid substitutions, hemoglobinopathies, oxygen affinity, oxygen delivery
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