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Stereochemistry and Charged State Influence Effector Outcomes of d-2-Hydroxyglutarate Dehydrogenase Ligands. [PDF]
BiochemistryQuaye JA, Gadda G.
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Abnormal von Willebrand factor multimer pattern without <i>VWF</i> variants in autosomal-recessive cutis laxa type IIA. [PDF]
Blood Vessel Thromb HemostJacobs JW +5 more
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Comparative biosafety and efficacy of Pseudomonas fluorescens PFS and Lactiplantibacillus plantarum ZPZ against Ralstonia solanacearum. [PDF]
Sci RepPepoyan A, Chikindas ML.
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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
openaire +2 more sources