Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Kathleen R. Terry"'
Publikováno v:
Cureus
Cardiovascular disease still remains the leading cause of deaths worldwide. Atherosclerosis, the most common type of cardiovascular disease, has continued to progress due to many factors, genetics, and lifestyles. All cells require adequate adenosine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e0dac8a706e1506b0efe798800eda5f
https://doi.org/10.7759/cureus.2291
https://doi.org/10.7759/cureus.2291
Publikováno v:
Recent Patents on Cardiovascular Drug Discovery. 5:138-142
Cardiovascular diseases account for more deaths worldwide than any other illness. Myocardial ischemia, a common finding in cardiovascular diseases, lowers cellular energy levels, which affects a cell's integrity and function. Pre-clinical animal stud
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea3c1498ba66195d645daf6feca5e8d9
https://doi.org/10.2174/157489010791515241
https://doi.org/10.2174/157489010791515241
Autor:
Kathleen R. Terry
Publikováno v:
Industry and Higher Education. 13:198-202
As collaboration between companies and research institutions increases, joint ownership of patents resulting from collaboration also increases. The agreement to own patents jointly is often entered into casually by parties who are unaware of the impl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13c6335a03b8d51fd4e1fc58f35c3ea7
https://doi.org/10.5367/000000099101294537
https://doi.org/10.5367/000000099101294537
Publikováno v:
Global Journal of Medical and Clinical Case Reports. :001-002
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc723fae17b9fc4e20ac390a6c87e263
https://doi.org/10.17352/2455-5282.000015
https://doi.org/10.17352/2455-5282.000015
Autor:
Alan B. Hooper, Kathleen R. Terry
Publikováno v:
Biochemistry. 16:455-459
Incubation of hydroxylamine oxidoreductase of Nitrosomonas with hydrogen peroxide resulted in the rapid and irreversible loss of the ability to catalyze the dehydrogenation of hydroxylamine in the presence of electron acceptors, such as phenazine met
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af84ee329ff5b11f1ac118bce855e3fe
https://doi.org/10.1021/bi00622a018
https://doi.org/10.1021/bi00622a018
Autor:
Alan B. Hooper, Kathleen R. Terry
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Enzymology. 571:12-20
As shown previously, higly purified hydroxylamine oxidoreductase (hydroxylamine:oxygen oxidoreductase, EC 1.7.3.4) from Nitrosomonas catalyzes the aerobic oxidation of NH2OH to a mixture of NO2− and NO3− in the presence of phenazine methosulfate.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dfd5ba0db3feeb7fa4060eccdb56abef
https://doi.org/10.1016/0005-2744(79)90220-1
https://doi.org/10.1016/0005-2744(79)90220-1
Publikováno v:
Biochemistry. 17:2984-2989
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7675784902adddb20d41d093c4a0cdbc
https://doi.org/10.1021/bi00608a007
https://doi.org/10.1021/bi00608a007
Publikováno v:
Journal of Bacteriology. 110:430-438
Freezing and thawing of Nitrosomonas , followed by centrifugation of the homogenate at 3,000 × g , resulted in a fraction which appeared to consist of an intact membrane-envelope complex and contained approximately 50% of the cell protein and more t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dede1b395f5208addbb7f7a1111add31
https://doi.org/10.1128/jb.110.1.430-438.1972
https://doi.org/10.1128/jb.110.1.430-438.1972
Publikováno v:
Biochimica et biophysica acta. 462(1)
Although nitrate was not produced in the oxidation of ammonia or hydroxylamine as catalyzed by intact cells, hydroxylamine oxidoreductase from Nitrosomonas europaea catalyzed the aerobic oxidation of hydroxylamine to nitrite and nitrate. The reaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dfbd89fac5c316afbeb0cda222a5093
https://pubmed.ncbi.nlm.nih.gov/199251
https://pubmed.ncbi.nlm.nih.gov/199251
Publikováno v:
Biochimica et biophysica acta. 358(1)
Glutamate dehydrogenase [ l -glutamate: NAD(P) oxidoreductase (deaminating), EC 1.4.1.3] located in the mitochondria and able to utilize NAD, NADP, NADH or NADPH as substrate, has been purified 67-fold from Tetrahymena pyriformis . The activity with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28be264775da3f1fe2ba56192ef10dd7
https://pubmed.ncbi.nlm.nih.gov/4152893
https://pubmed.ncbi.nlm.nih.gov/4152893