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pro vyhledávání: '"Michael T. Wilson"'
Autor:
Michael T. Wilson, Brandon J. Reeder
Publikováno v:
Molecular Aspects of Medicine. 84:101045
Under those pathological conditions in which Myoglobin and Hemoglobin escape their cellular environments and are thus separated from cellular reductive/protective systems, the inherent peroxidase activities of these proteins can be expressed. This ac
Publikováno v:
Free Radical Biology & Medicine
Covalent hemoglobin binding to membranes leads to band 3 (AE1) clustering and the removal of erythrocytes from the circulation; it is also implicated in blood storage lesions. Damaged hemoglobin, with the heme being in a redox and oxygen-binding inac
Autor:
Rebecca S. Silkstone, Gary Silkstone, Kristian Kallberg, Leif Bülow, Khuanpiroon Ratanasopa, Michael T. Wilson, Brandon J. Reeder, Chris E. Cooper, Michelle Simons, Andrea Mozzarelli, Luca Ronda
Publikováno v:
Biochemical Journal
Hemoglobin (Hb)-based oxygen carriers (HBOC) have been engineered to replace or augment the oxygen-carrying capacity of erythrocytes. However, clinical results have generally been disappointing due to adverse side effects linked to intrinsic heme-med
Autor:
John S. Olson, Abdu I. Alayash, Wayne Hicks, Tigist Kassa, Michael Brad Strader, Eileen W. Singleton, Michael T. Wilson, Todd L. Mollan, Mitchell J. Weiss, Jayashree Soman
Publikováno v:
Journal of Biological Chemistry. 289:22342-22357
A pathogenic V67M mutation occurs at the E11 helical position within the heme pockets of variant human fetal and adult hemoglobins (Hb). Subsequent post-translational modification of Met to Asp was reported in γ subunits of human fetal Hb Toms River
Autor:
Michael T. Wilson, Robert C. Hider, Francesca Cutruzzolà, Brandon J. Reeder, Maria Giulia Bigotti
Publikováno v:
Free Radical Biology and Medicine. 44:274-283
A wide range of organic reductants, including many iron chelators, reduce ferryl myoglobin to its ferric states in exponential time courses whose rate constants display double hyperbolic dependencies on the reductant concentration. This concentration
Autor:
Yiping Jia, Fantao Meng, Sirsendu Jana, Tigist Kassa, Michael Brad Strader, Abdu I. Alayash, Michael T. Wilson
Publikováno v:
The Journal of biological chemistry. 290(46)
Polymerization of intraerythrocytic deoxyhemoglobin S (HbS) is the primary molecular event that leads to hemolytic anemia in sickle cell disease (SCD). We reasoned that HbS may contribute to the complex pathophysiology of SCD in part due to its pseud
Publikováno v:
Antioxidants & Redox Signaling. 6:954-966
Recent research has shown that myoglobin and hemoglobin play important roles in the pathology of certain disease states, such as renal dysfunction following rhabdomyolysis and vasospasm following subarachnoid hemorrhages. These pathologies are linked
Publikováno v:
Free radical biologymedicine. 44(3)
Iron chelators such as desferrioxamine have been shown to ameliorate oxidative damage in vivo. The mechanism of this therapeutic action under non-iron-overload conditions is, however, complex, as desferrioxamine has properties that can impact on oxid
Publikováno v:
Journal of magnetic resonance (San Diego, Calif. : 1997). 142(2)
A new method of EPR spectral analysis is developed to quantitate overlapping signals. The method requires double integration of a number of spectra containing the signals in different proportions and the subsequent solution of a system of linear equa
Publikováno v:
Nitric Oxide. 27:S24
The production of nitric oxide by the nitrite reductase activity of deoxyhemoglobin has been proposed to play a major role in hypoxic vasodilation. A feature of this mechanism is that deoxyhemoglobin sites in the R state of tetrameric hemoglobin favo