Results 191 to 200 of about 349,815 (226)
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Cofactor dependent and cofactor independent anticardiolipin antibodies
Thrombosis Research, 1991Two distinct types of anticardiolipin antibodies are described, one of which requires the presence of a serum factor (cofactor) to bind cardiolipin in ELISA and liposome affinity systems. The second type does not require this cofactor. The requirement of a cofactor for the binding of some but not all anticardiolipin antibodies provides an explanation ...
L W, Chamley, E J, McKay, N S, Pattison
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Novel cofactor derivatives and cofactor-based models
Current Opinion in Chemical Biology, 1998In 1997 and the first half of 1998, numerous publications appeared reporting studies of cofactors and their analogues in classical model systems and in enzyme-catalyzed reactions directed at understanding the enzymatic reactions of their natural cofactors. Model systems based on flavins have provided new insights into enzymatic modulation of the flavin
P K, Mishra, D G, Drueckhammer
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2009
Cofactors are organic molecules, most of them originating from vitamins, that bind to enzymes making them able to catalyze defined reactions. A cofactor-based chemogenomics approach exploits the presence of a cofactor-binding domain to develop compound scaffolds tailored to mimic the cofactor and to replace it within target enzyme classes. As a result,
SINGH R, MOZZARELLI, Andrea
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Cofactors are organic molecules, most of them originating from vitamins, that bind to enzymes making them able to catalyze defined reactions. A cofactor-based chemogenomics approach exploits the presence of a cofactor-binding domain to develop compound scaffolds tailored to mimic the cofactor and to replace it within target enzyme classes. As a result,
SINGH R, MOZZARELLI, Andrea
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1992
MCP serves to down-regulate the activation of complement on host tissue. It performs this function by serving as a cofactor for the factor I-mediated cleavage of C3b and C4b. MCP is most likely an intrinsic regulator, i.e., it primarily protects its home cell.
M K, Liszewski, J P, Atkinson
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MCP serves to down-regulate the activation of complement on host tissue. It performs this function by serving as a cofactor for the factor I-mediated cleavage of C3b and C4b. MCP is most likely an intrinsic regulator, i.e., it primarily protects its home cell.
M K, Liszewski, J P, Atkinson
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Molybdenum cofactor deficiency
The Journal of Pediatrics, 1993We describe a new case of molybdenum cofactor deficiency, an underrecognized inborn error of metabolism that results in neonatal seizures and neurologic abnormalities. Characteristic biochemical defects in affected individuals include hypouricemia, elevated urine sulfate (detectable by dipstick), and elevated S-sulfocysteine (detectable by anion ...
G L, Arnold +3 more
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Molybdenum cofactor deficiency
Molecular Genetics and Metabolism, 2016Molybdenum cofactor deficiency (MoCD) is a severe autosomal recessive inborn error of metabolism first described in 1978. It is characterized by a neonatal presentation of intractable seizures, feeding difficulties, severe developmental delay, microcephaly with brain atrophy and coarse facial features.
Paldeep S, Atwal, Fernando, Scaglia
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Cofactor squelching: Artifact or fact?
BioEssays, 2016Cofactor squelching is the term used to describe competition between transcription factors (TFs) for a limited amount of cofactors in a cell with the functional consequence that TFs in a given cell interfere with the activity of each other. Since cofactor squelching was proposed based primarily on reporter assays some 30 years ago, it has remained ...
Søren Fisker Schmidt +3 more
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Antioxidants & Redox Signaling, 2001
721 REDOX-ACTIVE COFACTORS, including quinones and flavins, are important components in biological systems. Together with the apoprotein, they perform complex redox chemistry, provide an important link in signal transduction, and participate in crucial electron transfer pathways, aspects that are often inefficiently carried out by the proteins ...
V M, Rotello, R P, Swenson
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721 REDOX-ACTIVE COFACTORS, including quinones and flavins, are important components in biological systems. Together with the apoprotein, they perform complex redox chemistry, provide an important link in signal transduction, and participate in crucial electron transfer pathways, aspects that are often inefficiently carried out by the proteins ...
V M, Rotello, R P, Swenson
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2001
Publisher Summary Tyrosyl radicals are found in enzymes that catalyze a wide spectrum of chemical reactions, and their functional importance is well established in class I ribonucleotide reductase (RNR), prostaglandin H synthase (PGHS), and photosystem II (PSII).
R P, Pesavento, W A, van der Donk
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Publisher Summary Tyrosyl radicals are found in enzymes that catalyze a wide spectrum of chemical reactions, and their functional importance is well established in class I ribonucleotide reductase (RNR), prostaglandin H synthase (PGHS), and photosystem II (PSII).
R P, Pesavento, W A, van der Donk
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