Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Bennett J. Giardina"'
Publikováno v:
Journal of Extracellular Vesicles, Vol 3, Iss 0, Pp 1-11 (2014)
Background: Protein secretion is a fundamental process in all living cells. Gluconeogenic enzymes are secreted when Saccharomyces cerevisiae are grown in media containing low glucose. However, when cells are transferred to media containing high gluco
Externí odkaz:
https://doaj.org/article/e365ba42eace4a4082cee32c7cf66bd4
Publikováno v:
Journal of Biological Chemistry. 291:20503-20515
Pseudomonas aeruginosa acquires extracellular heme via the Phu (Pseudomonas heme uptake) and Has (heme assimilation system) systems. We have previously shown the catalytic actions of heme oxygenase (HemO) along with the cytoplasmic heme transport pro
Autor:
Wenbo Yu, Geoffrey Heinzl, Bennett J. Giardina, Angela Wilks, Fengtian Xue, Yue Zhou, Weiliang Huang, Alexander D. MacKerell
Publikováno v:
Journal of Medicinal Chemistry. 59:6929-6942
New therapeutic targets are required to combat multidrug resistant infections, such as the iron-regulated heme oxygenase (HemO) of Pseudomonas aeruginosa, due to links between iron and virulence and dependence on heme as an iron source during infecti
Publikováno v:
Journal of Extracellular Vesicles, Vol 3, Iss 0, Pp 1-11 (2014)
Journal of Extracellular Vesicles
Journal of Extracellular Vesicles; Vol 3 (2014) incl supplements
Journal of Extracellular Vesicles
Journal of Extracellular Vesicles; Vol 3 (2014) incl supplements
Background : Protein secretion is a fundamental process in all living cells. Gluconeogenic enzymes are secreted when Saccharomyces cerevisiae are grown in media containing low glucose. However, when cells are transferred to media containing high gluc
Publikováno v:
Arch Biochem Biophys
Acinetobacter baumannii is an opportunistic pathogen that causes serious infections in critically ill and immune compromised patients. The ability to acquire iron from the hosts iron and heme containing proteins is critical to their survival and viru
Publikováno v:
Journal of Biological Chemistry. 288:11636-11648
Gluconeogenic enzymes are induced when Saccharomyces cerevisiae are starved of glucose. However, when glucose is added to prolonged starved cells, these enzymes are degraded in the vacuole via the vacuole import and degradation (Vid) pathway. The Vid
Publikováno v:
Journal of Biological Chemistry. 287:33080-33093
When Saccharomyces cerevisiae are starved of glucose for a prolonged period of time, gluconeogenic enzymes such as fructose-1,6-bisphosphatase (FBPase), malate dehydrogenase, isocitrate lyase, and phosphoenolpyruvate carboxykinase are induced. Howeve
Publikováno v:
Proteome Science
Background Protein secretion is a fundamental process in all living cells. Proteins can either be secreted via the classical or non-classical pathways. In Saccharomyces cerevisiae, gluconeogenic enzymes are in the extracellular fraction/periplasm whe
Publikováno v:
Clinical & Experimental Pharmacology.
Protein secretion is a fundamental process in all living cells. Proteins that contain the ER signal are secreted by the classical pathway, whereas proteins without the ER sequence are secreted via the non-classical pathway. Recent evidence indicates
Autor:
Bennett J. Giardina, Hui Ling Chiang
Publikováno v:
Plant Signaling & Behavior
In Saccharomyces cerevisia, the key gluconeogenic enzyme fructose-1,6-bisphosphatase is secreted into the periplasm during prolonged glucose starvation and is internalized into Vid/endosomes following glucose re-feeding. Fructose-1,6-bisphosphatase d