Zobrazeno 21 - 30
of 66
pro vyhledávání: '"Michael T. Wilson"'
Autor:
Winston A. Anderson, Jonathan K. Stiles, Shailesh Singh, Vincent C. Bond, Andrew A. Adjei, Methode Bacanamwo, Ben Gyan, Carmen Dickinson-Copeland, Nana O. Wilson, Adel Driss, Mingli Liu, Felix Botchway, Hassana Salifu, Michael T. Wilson, Daniel Oduro, Kingsley Badu
Publikováno v:
PLoS ONE, Vol 10, Iss 11, p e0142328 (2015)
PLoS ONE
PLoS ONE
Plasmodium falciparum infection can cause microvascular dysfunction, cerebral encephalopathy and death if untreated. We have previously shown that high concentrations of free heme, and C-X-C motif chemokine 10 (CXCL10) in sera of malaria patients ind
Autor:
Andreea Manole, Demet Kekilli, Michael T. Wilson, Paul S. Dobbin, Michael A. Hough, Dimitri A. Svistunenko
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 20(4)
The cytochromes c′ (CYTcp) are found in denitrifying, methanotrophic and photosynthetic bacteria. These proteins are able to form stable adducts with CO and NO but not with O2. The binding of NO to CYTcp currently provides the best structural model
Autor:
Ursula Liebl, Michael T. Wilson, Latifa Bouzhir-Sima, Marten H. Vos, Taku Yamashita, Laura Lobato
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (38), pp.26514-24. ⟨10.1074/jbc.M114.571398⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2014, 289 (38), pp.26514-24. ⟨10.1074/jbc.M114.571398⟩
International audience; DNR (dissimilative nitrate respiration regulator) is a heme-binding transcription factor that is involved in the regulation of denitrification in Pseudomonas aeruginosa. In the ferrous deoxy state, the heme is 6-coordinate; ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::950f1d704309843293227820feb66809
https://hal-polytechnique.archives-ouvertes.fr/hal-01079002
https://hal-polytechnique.archives-ouvertes.fr/hal-01079002
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:
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:
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:
Michael Brad, Strader, Wayne A, Hicks, Tigist, Kassa, Eileen, Singleton, Jayashree, Soman, John S, Olson, Mitchell J, Weiss, Todd L, Mollan, Michael T, Wilson, Abdu I, Alayash
Publikováno v:
The Journal of biological chemistry. 289(32)
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:
Nathan Davies, Martyn A. Sharpe, Chris E. Cooper, Dimitri A. Svistunenko, Jacqueline Dunne, Christine Blenkinsop, Peter Nicholls, Michael T. Wilson
Publikováno v:
Biochemical Journal. 351:595-605
The paramagnetic species in human metHb and horse metmyoglobin (metMb) have been studied at low temperature using EPR spectroscopy. The high-spin (HS) haem signal in aquometMb has a greater rhombic distortion than the HS metHb signal. Nevertheless, t
Autor:
Chris E. Cooper, Dominik J. Schaer, Paul W. Buehler, Michael T. Wilson, Brandon J. Reeder, Gary Silkstone, Dimitri A. Svistunenko, Leif Bulow, Abdu I. Alayash
Aim: Hemoglobin (Hb) becomes toxic when released from the erythrocyte. The acute phase protein haptoglobin (Hp) binds avidly to Hb and decreases oxidative damage to Hb itself and to the surrounding proteins and lipids. However, the molecular mechanis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a3f006fb7b8a0c8e0f14d01fe1f6a6a
https://doi.org/10.5167/uzh-71620
https://doi.org/10.5167/uzh-71620
Autor:
Magda Gioia, Brandon J. Reeder, Alessandra Pesce, Fabio Polticelli, Michael T. Wilson, Massimo Coletta, Paolo Ascenzi, Marco Nardini, Maria Marino, Martino Bolognesi, Stefano Marini
Publikováno v:
Biochimica et biophysica acta. 1834(9)
Multimeric globins (e.g., hemoglobin) are considered to be the prototypes of allosteric enzymes, whereas monomeric globins (e.g., myoglobin; Mb) usually are assumed to be non-allosteric. However, the modulation of the functional properties of monomer