Results 241 to 250 of about 213,750 (303)
The PFI-index according to Aasen for prognosis and course of polytraumatized patients [PDF]
, 1988 Baumgartner, I. +7 more
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The Hemoprotein Hhy1 Promotes Heme‐Dependent Catalase Activity of Ctt1
Molecular Microbiology, EarlyView.A Schizosaccharomyces pombe strain deficient in heme (hem1Δ) and siderophore (Fc) biosynthesis, as well as high‐affinity iron (Fe) uptake (blue), was used to uncover the hemoprotein Hhy1 that promotes the heme‐dependent activity of the catalase Ctt1. In contrast, hhy1Δ cells exhibit reduced Ctt1 activity and increased sensitivity to oxidative stress ...
Tobias Vahsen +3 more
wiley +1 more source
Bacterial Involvement in Oral Squamous Cell Carcinoma and Potentially Malignant Oral Disorders
Oral Diseases, EarlyView.ABSTRACT Objective To clarify the relationship between oral squamous cell carcinoma (OSCC), potentially malignant oral disease (OPMD), and bacterial flora using metagenomic analysis. Methods This cross‐sectional observational study included 50 patients in the control group and 77 patients with OPMDs, 41 with early OSCCs, and 20 with advanced OSCCs ...
Atsumu Koketsu +16 more
wiley +1 more source
Plant phospholipase D. I. Studies on cottonseed and cabbage phospholipase D.
The Journal of biological chemistry, 2003 H L, TOOKEY, A K, BALLS
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Biochemistry and Cell Biology, 2004
Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals.
Mark, McDermott +2 more
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Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals.
Mark, McDermott +2 more
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Seminars in Cell & Developmental Biology, 1997
Phospholipase D catalyses the hydrolysis of phosphatidylcholine to generate phosphatidate. The regulation of PLD activity is complex involving a number of small GTP binding proteins, but in particular Arf and Rho, phosphatidylinositol 4,5-bisphosphate and protein kinase C.
, Wakelam, , Hodgkin, , Martin, , Saqib
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Phospholipase D catalyses the hydrolysis of phosphatidylcholine to generate phosphatidate. The regulation of PLD activity is complex involving a number of small GTP binding proteins, but in particular Arf and Rho, phosphatidylinositol 4,5-bisphosphate and protein kinase C.
, Wakelam, , Hodgkin, , Martin, , Saqib
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Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1996
Abstract:Phospholipase D is an ubiquitous enzyme that hydrolyzes phosphatidylcholine to phosphatidic acid and choline. Its cellular actions are related to the production of phosphatidic acid and include alterations to cell growth, shape, and secretion.
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Abstract:Phospholipase D is an ubiquitous enzyme that hydrolyzes phosphatidylcholine to phosphatidic acid and choline. Its cellular actions are related to the production of phosphatidic acid and include alterations to cell growth, shape, and secretion.
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Phospholipase D in cellular senescence
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1999Cellular senescence appears to be an important part of organismal aging. Cellular senescence is characterized by flattened enlarged morphology, inhibition of DNA replication in response to growth factors, inability to phosphorylate the pRb tumor suppressor protein, inability to produce c-fos or AP-1 and overexpression of a variety of genes, notably p21
M E, Venable, L M, Obeid
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Measurement of Phospholipase D Activity
Analytical Biochemistry, 1997Phosphodiesteric cleavage of phosphatidylcholine by members of a growing family of phospholipases D produces choline and phosphatidic acid. These enzymes can also catalyse a transphosphatidylation reaction in which the aliphatic chain of a primary alcohol is transferred to the phosphatidyl moiety of the phosphatidic acid product.
A J, Morris, M A, Frohman, J, Engebrecht
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