Cited by 179Hemoglobin structure and functionHemoglobinopathies and Related DisordersBlood properties and coagulation

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Structure-Function Relations of Human Hemoglobins

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Marengo-Rowe, Alain J.·2006·Baylor University Medical Center Proceedings

DOI 10.1080/08998280.2006.11928171PMC PMC1484532

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Abstract

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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“…structural biology and has led to great successes in revealing the structural basis of numerous fundamental biological processes, including oxygen transport of hemoglobin (Marengo-Rowe, 2006), protein translation of ribosome machine (Schmeing and Ramakrishnan, 2009), enzymatic catalysis and so on.”
Common and ethnic-specific genetic determinants of hemoglobin concentration between Taiwanese Han Chinese and European Whites: findings from comparative two-stage genome-wide association studies
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“Maintaining adequate levels of Hb within red blood cells can help prevent anemia [55].”
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“These complications include but are not limited to priapism, pulmonary emboli, and osteonecrosis and ultimately damage every organ system, including the spleen, retinae, kidneys and liver [10].”
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“127,128 The latter anaemias are generally transfusion-dependent and aside from the reduced life quality for the patient, present a major burden to health care systems with multimillion investments per patient.”
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“Therefore, oxygen is firmly regulated within the body [2].”
BackgroundInfluential
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Background
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“Carbon dioxide binds to the globin protein as carbaminohemoglobin.[1] It maintains the shape of the RBCs; if the Hb structure is abnormal, it can interfere with the flow and function of RBCs.”
Background
Physicochemical evaluation of interaction behavior of a series of biocompatible gemini surfactants with hemoglobin: Insights from spectroscopic and computational studies
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Ultraviolet light oxidation of fresh hemoglobin eliminates aggregate formation seen in commercially sourced hemoglobin
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Biothermodynamics of Hemoglobin and Red Blood Cells: Analysis of Structure and Evolution of Hemoglobin and Red Blood Cells, Based on Molecular and Empirical Formulas, Biosynthesis Reactions, and Thermodynamic Properties of Formation and Biosynthesis
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“The sub‑ ject of this paper are hemoglobin and red blood cells, which are very important for the metabolism of most vertebrates (Marengo‑Rowe 2006; Tonino et al. 2023).”
Exploring clinical chemistry markers in amyotrophic lateral sclerosis: insights into survival and disease trajectories
Psychogios, I., Hu, Y., Seitz, C., Joyce, E. E., Lovik, A., Ingre, C., & Fang, F. (2024) · Journal of Neurology · doi:10.1007/s00415-024-12774-7 · Cited by 4
“Similarly, as hemoglobin is a transporter of oxygen [50], a higher level of hemoglobin can indicate a higher level of oxidative stress [51].”

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
DOI: 10.1080/08998280.2006.11928171
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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Structure-Function Relations of Human Hemoglobins

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