Výsledky vyhledávání

Otitis externa: what is the problem with getting it right? A mixed-methods study in primary and secondary care

Autor: H, Mohammed, M W, Mather, J, Lumb, C C, Butler, J A, Wilson

Publikováno v: The Journal of Laryngology & Otology. 136:486-491

ObjectiveOtitis externa accounts for 1.1–1.3 per cent of patient presentations in primary care and 25 per cent of urgent referrals to ENT. This study aimed to explore otitis externa clinical decision-making at the primary-secondary care interface,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40e07abb7b5c2134ed90e7c535599486
https://doi.org/10.1017/s0022215121003649

Zobrazit plný text záznamu

A post-genomic view of the mitochondrion in malaria parasites

Autor: A B, Vaidya, M W, Mather

Publikováno v: Current topics in microbiology and immunology. 295

Mitochondria in Plasmodium parasites have many characteristics that distinguish them from mammalian mitochondria. Selective targeting of malaria parasite mitochondrial physiology has been exploited in successful antimalarial chemotherapy. At present,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5e5fdc4438bcff06449f645b5307fd8f
https://pubmed.ncbi.nlm.nih.gov/16265893

Zobrazit plný text záznamu

A career in academic medicine

Autor: J Gupta, Rory J Piper, M W Mather, R Dbeis

Publikováno v: BMJ. :g3506

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b402b9b24d4fd4193188d1b2094c24bb
https://doi.org/10.1136/sbmj.g3506

Zobrazit plný text záznamu

Cytochrome oxidase genes from Thermus thermophilus. Nucleotide sequence of the fused gene and analysis of the deduced primary structures for subunits I and III of cytochrome caa3

Autor: M W, Mather, P, Springer, S, Hensel, G, Buse, J A, Fee

Publikováno v: The Journal of biological chemistry. 268(8)

Cytochrome caa3, a cytochrome c oxidase from Thermus thermophilus, has been purified and extensively characterized as a two-subunit enzyme containing the metal centers characteristic of cytochrome c oxidases (cytochromes a and a3; copper centers CuA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a10e07b0c1b2ff8418bde721f73dff26
https://pubmed.ncbi.nlm.nih.gov/8383670

Zobrazit plný text záznamu

Cytochrome oxidase genes from Thermus thermophilus. Nucleotide sequence and analysis of the deduced primary structure of subunit IIc of cytochrome caa3

Autor: M W, Mather, P, Springer, J A, Fee

Publikováno v: The Journal of biological chemistry. 266(8)

Cytochrome caa3, a cytochrome c oxidase from Thermus thermophilus, is a two-subunit enzyme containing the four canonical metal centers of cytochrome c oxidases (cytochromes a and a3; copper centers CuA and CuB) and an additional cytochrome c. The sma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::776ce57e6a2fcf443b3cd40972b86faf
https://pubmed.ncbi.nlm.nih.gov/1848234

Zobrazit plný text záznamu

Relationship of Cytochrome caa3 from Thermus thermophilus to Other Heme- and Copper-Containing Terminal Oxidases

Autor: P. Springer, M. W. Mather, James A. Fee

Publikováno v: The Molecular Basis of Bacterial Metabolism ISBN: 9783642759710

Cytochrome oxidases are a key component of the energy metabolism of most aerobic organisms from mammals to bacteria. They are the final enzyme of the membrane-associated respiratory chain responsible for converting the chemical energy of reduced subs

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::17dffdac95d19c3d73b8d8f317f12c14
https://doi.org/10.1007/978-3-642-75969-7_10

Zobrazit plný text záznamu

Base composition-independent hybridization in dried agarose gels: screening and recovery for cloning of genomic DNA fragments

Autor: M W, Mather

Publikováno v: BioTechniques. 6(5)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8440d1b1f9fd77419a22d9cc291ccfa3
https://pubmed.ncbi.nlm.nih.gov/3273405

Zobrazit plný text záznamu

Spectroscopic studies of pyruvate oxidase flavoprotein from Escherichia coli trapped in the lipid-activated form by cross-linking

Autor: M W, Mather, R B, Gennis

Publikováno v: The Journal of biological chemistry. 260(19)

Pyruvate oxidase is a flavoprotein dehydrogenase isolated from Escherichia coli which catalyzes the oxidative decarboxylation of pyruvate to acetate plus CO2. The maximal turnover of the enzyme, measured using a ferricyanide reductase assay, is incre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2e79cd412de6d0b254461a47ed24a737
https://pubmed.ncbi.nlm.nih.gov/3928620

Zobrazit plný text záznamu

Kinetic studies of the lipid-activated pyruvate oxidase flavoprotein of Escherichia coli

Autor: M W, Mather, R B, Gennis

Publikováno v: The Journal of biological chemistry. 260(30)

Pyruvate oxidase is a flavoprotein dehydrogenase isolated from Escherichia coli which catalyzes the oxidative decarboxylation of pyruvate to acetate and CO2. In vivo, the enzyme can bind to the bacterial membrane and reduce ubiquinone-8, feeding elec

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b744d51c7ff9f23e2b316db5663d646a
https://pubmed.ncbi.nlm.nih.gov/3905808

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání