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Crystallographic Evidence for a New Ensemble of Ligand-Induced Allosteric Transitions in Hemoglobin: The T-to-THigh Quaternary Transitions,
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Allosteric free energy changes at the α1β2 interface of human hemoglobin probed by proton exchange of Trpβ37
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The mutation β99 Asp‐Tyr stabilizes Y—A new, composite quaternary state of human hemoglobin
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Structure and Oxygen Affinity of Crystalline of DesArg141α Human Hemoglobin A in the T State
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Crystal Structure of T State Haemoglobin with Oxygen Bound At All Four Haems
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Conformation-invariant structures of the α 1 β 1 human hemoglobin dimer 1 1Edited by P. E. Wright
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Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of gower II (α 2 ϵ 2 ) haemoglobin at 2.9 å resolution 1 1Edited by K. Nagai
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Design of a diffractometer and flow cell system for X-ray analysis of crystalline proteins with applications to the crystal chemistry of ribonuclease-S
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Haemoglobin: The structural changes related to ligand binding and its allosteric mechanism
inferredcites →https://doi.org/10.1016/0022-2836(84)90472-8openalex-snapshot
The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution
inferredcites →https://doi.org/10.1016/0022-2836(91)90387-lopenalex-snapshot
Analysis of protein loop closure
inferredcites →https://doi.org/10.1016/s0021-9258(18)41919-9openalex-snapshot
A third quaternary structure of human hemoglobin A at 1.7-A resolution.
inferredcites →https://doi.org/10.1016/s0022-2836(65)80285-6openalex-snapshot
On the nature of allosteric transitions: A plausible model
inferredcites →https://doi.org/10.1016/s0022-2836(83)80313-1openalex-snapshot
Structure of human oxyhaemoglobin at 2·1resolution
inferredcites →https://doi.org/10.1017/s0033583500003826openalex-snapshot
Mechanisms of cooperativity and allosteric regulation in proteins
inferredcites →https://doi.org/10.1021/ja00489a046openalex-snapshot
Structural changes upon oxygenation of an iron(II)(porphyrinato)(imidazole) complex
inferredcites →https://doi.org/10.1038/249034a0openalex-snapshot
Structure of inositol hexaphosphate–human deoxyhaemoglobin complex
inferredcites →https://doi.org/10.1038/249036a0openalex-snapshot
β-2-Microglobulin is part of the HL-A molecule in the lymphocyte membrane
inferredcites →https://doi.org/10.1107/s0108768190000313openalex-snapshot
Refinement of a partially oxygenated T state human haemoglobin at 1.5 Å resolution
inferredcites →https://doi.org/10.1146/annurev.bi.48.070179.001551openalex-snapshot
Regulation of Oxygen Affinity of Hemoglobin: Influence of Structure of the Globin on the Heme Iron
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THE STEREOCHEMICAL MECHANISM OF THE COOPERATIVE EFFECTS IN HEMOGLOBIN REVISITED
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