Results 31 to 40 of about 763,041 (124)
, 2006 The Bahamian octocoral Pseudopterogorgia elisabethae is the source of pseudopterosins, diterpene glycosides with potent anti-inflammatory activity.
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Class I HDACs Share a Common Mechanism of Regulation by Inositol Phosphates
Molecules and Cells, 2013 Summary Class I histone deacetylases (HDAC1, HDAC2, and HDAC3) are recruited by cognate corepressor proteins into specific transcriptional repression complexes that target HDAC activity to chromatin resulting in chromatin condensation and transcriptional
C. J. Millard +7 more
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Research of Calcium Phosphates Using Fourier Transform Infrared Spectroscopy
, 2012 In the biomaterial research field, nowadays a great attention is driven onto calcium phosphates synthesis and obtaining of ceramics that can be used in orthopedics and dentistry, in the form of coatings, granules, porous or solid blocks, as well as in ...
L. Bērziņa-Cimdiņa +1 more
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In vivo and in vitro investigations into the biosynthetic relatedness of the pseudopterosins
[formula: see text] Both in vivo and in vitro techniques have been developed to test putative intermediates in the biosynthetic pathway to the pseudopterosins, antiinflammatory compounds isolated from Pseudopterogorgia elisabethae.
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The Journal of biological chemistry, 1998 Microsomal fractions from pig and calf brain catalyze the enzymatic dephosphorylation of endogenous and exogenous dolichyl monophosphate (Dol-P) (Sumbilla, C. A., and Waechter, C. J. (1985) Methods Enzymol. 111, 471-482). The Dol-P phosphatase (EC 3.1.3.51) has been solubilized by extracting pig brain microsomes with the nonionic detergent Nonidet P-40
D W, Frank, C J, Waechter
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Journal of Biological Chemistry, 1992 The prenylation of proteins utilizes the polyisoprenyl pyrophosphates (FPP) and geranylgeranyl pyrophosphate (GGPP) as prenyl donors. These polyisoprenoids are also precursors to ubiquinone and dolichol synthesis.
R. Lutz, T. McLain, M. Sinensky
semanticscholar +1 more source
Structure-Function Analysis of Enzymes of the Polyisoprenyl-Phosphate Hexose-1-Phosphate Transferase family [PDF]
, 2011 Enzymes of the polyisoprenyl-phosphate hexose-1-phosphate transferase (PHPT) family are integral membrane proteins that initiate the synthesis of glycans by catalyzing the transfer of a hexose-1-phosphate sugar from UDP-hexose to the lipid carrier undecaprenyl phosphate (Und-P).
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Structure-Function Analysis of UDP-Sugar: Polyisoprenyl Phosphate Sugar-1-Phosphate Transferases [PDF]
, 2013 The synthesis of lipid-linked glycans is a conserved process in eukaryotes and prokaryotes that is initiated by two major enzyme families: the polyisoprenyl-phosphate hexose-1-phosphate transferases (PHPTs) and the polyisoprenyl-phosphate N-acetylaminosugar-1-phosphate transferases (PNPTs). These enzymes contain multiple membrane domains and transfer a
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Purification and Characterization of a Polyisoprenyl Phosphate Phosphatase from Pig Brain [PDF]
Journal of Biological Chemistry, 1998 David W. Frank, Charles J. Waechter
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The Journal of biological chemistry, 2006 The transfer of mannose from GDP-mannonse to exogenous glycopeptides and simple glycosides has been shown to be carried out by calf thyroid particles (Adamany, A. M., and Spiro, R. G. (1975) J. Biol. Chem. 250, 2830-2841). The present investigation indicates that this mannosylation process is accomplished through two sequential enzymatic reactions. The
A M, Adamany, R G, Spiro
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