Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Michael T. Wilson"'
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:
Amanda K. Chaplin, Jonathan A. R. Worrall, Erik Vijgenboom, Vassiliy N. Bavro, Michael T. Wilson, Jordi Paps, Michael A. Hough, Megan L. Straw
Publikováno v:
Metallomics, 10(1), 180-193. OXFORD UNIV PRESS
Metallomics
Metallomics
Streptomyces lividans has a distinct dependence on the bioavailability of copper for its morphological development. A cytosolic copper resistance system is operative in S. lividans that serves to preclude deleterious copper levels. This system compri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::681a7d249fbab6f8edf28b9258389ed7
http://hdl.handle.net/1887/3217486
http://hdl.handle.net/1887/3217486
Autor:
Michael A. Hough, Amanda K. Chaplin, Jonathan A. R. Worrall, Dimitri A. Svistunenko, Erik Vijgenboom, Michael T. Wilson
Publikováno v:
Biochemical Journal, 474(5), 809-825
Biochemical Journal
Biochemical Journal
GlxA from Streptomyces lividans is a mononuclear copper-radical oxidase and a member of the auxiliary activity family 5 (AA5). Its domain organisation and low sequence homology make it a distinct member of the AA5 family in which the fungal galactose
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b9a274b4a058c3adb0e223bbf8efea6
https://doi.org/10.1042/bcj20160968
https://doi.org/10.1042/bcj20160968
Autor:
Gary Silkstone, Badri S. Rajagopal, Michael T. Wilson, Peter Nicholls, Jonathan A. R. Worrall
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1817:780-791
Mitochondrial cytochrome c associates with the phosphoplipid cardiolipin (CL) through a combination of electrostatic and hydrophobic interactions. The latter occurs by insertion into cytochrome c of an acyl chain, resulting in the dissociation of the
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
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:
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:
Jonathan A. R. Worrall, Dimitri A. Svistunenko, Katie L. I. M. Blundell, Michael T. Wilson, Erik Vijgenboom
Publikováno v:
Open Biology, 3(1)
Open Biology
Open Biology, Vol 3, Iss 1 (2013)
Open Biology
Open Biology, Vol 3, Iss 1 (2013)
Copper has an important role in the life cycle of many streptomycetes, stimulating the developmental switch between vegetative mycelium and aerial hyphae concomitant with the production of antibiotics. In streptomycetes, a gene encoding for a putativ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f796179857707ab3d32f74504b46792
http://hdl.handle.net/1887/3209877
http://hdl.handle.net/1887/3209877
Publikováno v:
Biochemistry. 51(34)
Cardiolipin, a phospholipid specific to the mitochondrion, interacts with the small electron transfer heme protein cytochrome c through both electrostatic and hydrophobic interactions. Once in a complex with cardiolipin, cytochrome c has been shown t
Publikováno v:
The Biochemical journal. 434(3)
Cytoglobin is a recently discovered hexa-co-ordinate haemoglobin that does not appear to function as a classical oxygen-binding protein. Its function is unknown and studies on the effects of changes in its expression have not decisively determined it