Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Michael T. Wilson"'
Autor:
Michael T. Wilson, Asma Munir, Steven W. Hardwick, Dimitri Y. Chirgadze, Amanda K. Chaplin, Jonathan A. R. Worrall, Tom L. Blundell
Publikováno v:
Structure(London, England:1993)
Summary Resolution advances in cryoelectron microscopy (cryo-EM) now offer the possibility to visualize structural effects of naturally occurring resistance mutations in proteins and also of understanding the binding mechanisms of small drug molecule
Autor:
Michael T. Wilson, Geoffrey R. Moore, Jonathan A. R. Worrall, Oliver M. Deacon, Dimitri A. Svistunenko
Publikováno v:
Biochemistry. 57(29)
Naturally occurring mutations found in one of the two Ω-loop substructures in human cytochrome c are associated with low blood platelet count (thrombocytopenia). Both Ω-loops participate in the formation of conformers associated with cytochrome c p
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
Autor:
Brandon J. Reeder, Michael T. Wilson
Publikováno v:
Chemical Research in Toxicology. 18:1004-1011
The heme group of myoglobin can form a covalent bond to the protein when met (ferric) myoglobin is reacted with peroxides under acidic conditions. This heme to protein cross-linked species is highly pro-oxidant and found in the urine of patients with
Publikováno v:
Biophysical Chemistry. 98:65-77
The iron ligand, Met80, of yeast iso-1-cytochrome c has been mutated to residues that are unable to bind to the iron. The resultant proteins, Met80Ala, Ser, Asp, Glu, have been expressed and purified. All mutant proteins exhibit well defined pH depen
Autor:
Brandon J. Reeder, Michael T. Wilson
Publikováno v:
Free Radical Biology and Medicine. 30:1311-1318
Myoglobin catalyses the breakdown of lipid hydroperoxides (e.g., HPODE) during which the absorption band of the lipid conjugated diene (234 nm) is partially bleached. The constant for this process is strongly pH-dependent (k = 9.5 × 10 −3 s −1 ,
Autor:
Michael T. Wilson, Alexander J. Howie, John A. Oates, Taneem Amin, Clare K. Carney, D. S. Harry, David W. Wright, Kevin P. Moore, Olivier Boutaud, Shuhe Wang, Brandon J. Reeder, Tina S. Masterson, L. Jackson Roberts
Hemoproteins, hemoglobin and myoglobin, once released from cells can cause severe oxidative damage as a consequence of heme redox cycling between ferric and ferryl states that generates radical species that induce lipid peroxidation. We demonstrate i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3abb2a8c35a362d794c65f89ef2d2583
https://europepmc.org/articles/PMC2823910/
https://europepmc.org/articles/PMC2823910/
Autor:
Béatrice Faivre, Michael T. Wilson, Abdu I. Alayash, Jacqueline Dunne, Radu Silaghi-Dumitrescu, Alexis Caron, Chris E. Cooper, Patrick Menu, Paul W. Buehler
Publikováno v:
The Biochemical journal. 399(3)
Haemoglobin initiates free radical chemistry. In particular, the interactions of peroxides with the ferric (met) species of haemoglobin generate two strong oxidants: ferryl iron and a protein-bound free radical. We have studied the endogenous defence
Publikováno v:
Journal of the American Chemical Society. 127(1)
The ferric forms of Met80X mutants of yeast iso-1-cytochrome c (X = Ala, Ser, Asp, and Glu) display EPR and optical spectra that are strongly pH dependent. At low pH values (pH approximately 5) the sixth coordination sites are filled by H(2)O that, o