Results 331 to 340 of about 418,378 (371)
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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, John 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, John P. Atkinson
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Surprising cofactors in metalloenzymes [PDF]
Current Opinion in Structural Biology, 2003 Transition metal complexes are located at the active sites of a number of enzymes involved in intriguing biochemical reactions. These complexes can exhibit a wide variety of chemical reactivity due to the ease at which transition metals can adopt different coordination environments and oxidation states. Crystallography has been a powerful technique for
John W. Peters, Catherine L. Drennan
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Engineering cofactor supply and recycling to drive phenolic acid biosynthesis in yeast
Nature Chemical Biology, 2022Ruibing Chen +7 more
semanticscholar +1 more source
Prothrombin as cofactor for antiphospholipids
Lupus, 1998Prothrombin is a common antigenic target of antiphospholipid antibodies, since anti-prothrombin antibodies are detected in about 50-90% of the patients. To allow proper immune recognition, prothrombin must be adsorbed on suitable anionic surfaces. The epitope(s) have not yet been identified: the majority of anti-prothrombin antibodies appear to be of ...
T Barbui, M Galli
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1978
It is known that many enzymes function only in conjunction with a coenzyme (cofactor) which is generally a compound of low molecular weight. Immobilization of these compounds has been the focus of much effort because of their potential as bioaffinity ligands and in the search for immobilized coenzymes retaining “biological activity”, which are readily ...
K. Mosbach, P.-O. Larsson
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It is known that many enzymes function only in conjunction with a coenzyme (cofactor) which is generally a compound of low molecular weight. Immobilization of these compounds has been the focus of much effort because of their potential as bioaffinity ligands and in the search for immobilized coenzymes retaining “biological activity”, which are readily ...
K. Mosbach, P.-O. Larsson
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1974
Pollen, a non-chlorophyllous tissue, contains enzymes to metabolize external and internal substrates essential for tube growth. In some species tube extension occurs minutes after a grain lands in the proper environment; in others, growth occurs several days or weeks after pollination.
H. F. Linskens, Robert G. Stanley
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Pollen, a non-chlorophyllous tissue, contains enzymes to metabolize external and internal substrates essential for tube growth. In some species tube extension occurs minutes after a grain lands in the proper environment; in others, growth occurs several days or weeks after pollination.
H. F. Linskens, Robert G. Stanley
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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).
Wilfred A. van der Donk +1 more
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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).
Wilfred A. van der Donk +1 more
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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 ...
Georgianne L. Arnold +3 more
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2017
Enzymes such as oxidoreductases and transferases are able to catalyze industrially useful reactions. However, these enzymes are often cofactor dependent. Cofactors are relatively low molecular weight compounds that are required for the enzymatic reactions.
Camila Flor J. Yagonia +3 more
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Enzymes such as oxidoreductases and transferases are able to catalyze industrially useful reactions. However, these enzymes are often cofactor dependent. Cofactors are relatively low molecular weight compounds that are required for the enzymatic reactions.
Camila Flor J. Yagonia +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 ...
Richard P. Swenson, Vincent M. Rotello
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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 ...
Richard P. Swenson, Vincent M. Rotello
openaire +3 more sources