2022
DOI: 10.1016/j.mam.2021.101037
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Hemoglobin allostery and pharmacology

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Cited by 15 publications
(11 citation statements)
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“…Hb contains four different ligand binding sites: heme, exposed cysteine residues, DPG binding sites and Bohr residues [ 59 ]. Changes in any binding site can induce corresponding structural alterations in Hb, affecting the balance between the “T” (tense) and “R” (relaxed) states, subsequently resulting in altered oxygen affinity, called “allosteric effects” [ 57 ].…”
Section: Oxygen-releasing Biomaterialsmentioning
confidence: 99%
“…Hb contains four different ligand binding sites: heme, exposed cysteine residues, DPG binding sites and Bohr residues [ 59 ]. Changes in any binding site can induce corresponding structural alterations in Hb, affecting the balance between the “T” (tense) and “R” (relaxed) states, subsequently resulting in altered oxygen affinity, called “allosteric effects” [ 57 ].…”
Section: Oxygen-releasing Biomaterialsmentioning
confidence: 99%
“…O 2 binds to heme Fe(II) atoms, transforming the quaternary structure of Hb from a deoxygenated (T) state to a relaxed ligand-bound (R) state, 8 The R-to-T state transition is the reversible electrostatic binding of allosteric effectors such as hydrogen ions, carbon dioxide, and 2,3-bisphosphoglycerate (DPG) to two β subunits (pockets), and the combined effectors reduce the Hb oxygen affinity and promote oxygen unloading. 9,10 In addition to oxygen transport, Hb also has other important physiological functions, such as blood heat exchange, catabolism of one porphyrin to produce CO to regulate vascular tone 11 and to produce bilirubin to scavenge free radicals simultaneously, scavenging and transporting NO, 12−14 etc.…”
Section: Hb-based Oxygen Carriersmentioning
confidence: 99%
“…Human hemoglobin has a molecular weight of 64 500 Da and is composed of two α and two β subunits, each containing a heme group that can transport an oxygen molecule (Figure ). O 2 binds to heme Fe­(II) atoms, transforming the quaternary structure of Hb from a deoxygenated (T) state to a relaxed ligand-bound (R) state, The R-to-T state transition is the reversible electrostatic binding of allosteric effectors such as hydrogen ions, carbon dioxide, and 2,3-bisphosphoglycerate (DPG) to two β subunits (pockets), and the combined effectors reduce the Hb oxygen affinity and promote oxygen unloading. , …”
Section: Hb-based Oxygen Carriersmentioning
confidence: 99%
“…Patients often suffer from blood abnormalities, platelet dysfunction, and other diseases, such as abnormal liver function and anemia, that change the number and state of their platelets ( Newsome et al, 2018 ; Bellelli and Tame, 2022 ). An insufficient number of platelets or dysfunction in them might lead to thrombosis-related disorders ( Zhou et al, 2021 ).…”
Section: Biomaterials-mediated Therapy Through Activation Of Platelet...mentioning
confidence: 99%