Description of hemoglobin oxygenation under universal solution conditions by a global allostery model with a single adjustable parameter-Reference-Cited by-同舟云学术

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Description of hemoglobin oxygenation under universal solution conditions by a global allostery model with a single adjustable parameter

Published:2002-07 Issue:1-2 Volume:98 Page:79-91
ISSN:0301-4622
Container-title:Biophysical Chemistry
language:en
Short-container-title:Biophysical Chemistry

Author:

Imai Kiyohiro,Tsuneshige Antonio,Yonetani Takashi

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,Biophysics

Reference60 articles.

1. Linked functions and reciprocal effects in hemoglobin: a second look;Wyman;Advan. Protein Chem.,1964

2. Hemoglobin and myoglobin in their reactions with ligands;Antonini,1971

3. Allosteric Effects in Haemoglobin;Imai,1982

4. Mechanisms of cooperativity and allosteric regulation in proteins;Perutz,1990

5. Binding and linkage. Functional chemistry of biological macromolecules;Wyman,1990

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1. Cooperative oxygen binding in beta-semihemoglobins caused by a chemical modification in the alpha1beta1 interface;Journal of Inorganic Biochemistry;2023-09

2. Non-Allosteric Cooperativity in Hemoglobin;Current Protein & Peptide Science;2018-04-11

3. Hemoglobin and Cooperativity: Experiments and Theories;Current Protein & Peptide Science;2010-02-01

4. Interfacial and Distal-Heme Pocket Mutations Exhibit Additive Effects on the Structure and Function of Hemoglobin†;Biochemistry;2008-10-07

5. Ligand reactivity and allosteric regulation of hemoglobin-based oxygen carriers;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2008-10

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