Semihemoglobins, High Oxygen Affinity Dimeric Forms of Human Hemoglobin Respond Efficiently to Allosteric Effectors without Forming Tetramers-Reference-Cited by-同舟云学术

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Semihemoglobins, High Oxygen Affinity Dimeric Forms of Human Hemoglobin Respond Efficiently to Allosteric Effectors without Forming Tetramers

Published:2004-11 Issue:47 Volume:279 Page:48959-48967
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Tsuneshige Antonio,Kanaori Kenji,Samuni Uri,Danstker David,Friedman Joel M.,Neya Saburo,Giangiacomo Laura,Yonetani Takashi

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference52 articles.

1. On the nature of allosteric transitions: A plausible model

2. Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery

3. Heterotropic effectors control the hemoglobin function by interacting with its T and R states—a new view on the principle of allostery

4. Global Allostery Model of Hemoglobin

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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. Hemoglobin allostery and pharmacology;Molecular Aspects of Medicine;2022-04

3. Roles of Fe-His Bonds in stability of Hemoglobin: Recognition of Protein Flexibility by Q Sepharose;Biophysical Journal;2021-06

4. Interaction of human hemoglobin and semi-hemoglobins with the Staphylococcus aureus hemophore IsdB: a kinetic and mechanistic insight;Scientific Reports;2019-12

5. Structure and function of haemoglobins;Blood Cells, Molecules, and Diseases;2018-05

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